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Information on EC 3.4.22.53 - calpain-2
for references in articles please use BRENDA:EC3.4.22.53
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EC Tree 3 Hydrolases
3.4 Acting on peptide bonds (peptidases)
3.4.22 Cysteine endopeptidases
3.4.22.53 calpain-2
IUBMB Comments
Type example of peptidase family C2. Requires Ca2+ at millimolar concentrations for activity. Cytosolic in animal cells. The active enzyme molecule is a heterodimer in which the large subunit contains the peptidase unit, and the small subunit is also a component of EC 3.4.22.52, calpain-1.
The enzyme appears in viruses and cellular organisms
- 3.4.22.53
- calpains
- calpastatin
- mu-calpain
-
calcium-dependent
-
ca2+-dependent
- proteinase
- myofibrillar
- cytoskeletal
- cataract
-
zymography
- longissimus
-
meat
-
autolysis
- calpeptin
-
tender
- casein
- cathepsins
-
3.4.22.17
-
postmortem
-
calpain-mediated
- caspase-12
- lumborum
-
autolyzed
-
lens-specific
- talin
- alpha-spectrin
-
canps
-
cataractogenesis
-
warner-bratzler
- spectrin
-
slaughter
- semimembranosus
-
calpain-specific
- desmin
-
calpain-calpastatin
- lenses
-
calpain-dependent
-
atrogin-1
- medicine
-
calpain-induced
- fodrin
- myofibril
-
ca2+-activated
-
calmodulin-like
-
caseinolytic
- thoracis
-
ca2+-requiring
-
troponin-t
- micro-calpain
-
calpain-like
-
proteolyzed
showSynonyms
m-calpain, calpain ii, calpain-2, calpain 2, calpain2, ncl-2, milli-calpain, mitochondrial m-calpain, calcium-activated neutral protease ii, calpain-2-like, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
calcium-activated neutral protease II
-
-
-
-
calpain 2
calpain II
calpain xCL-2 (Xenopus leavis)
-
-
-
-
calpain-2
CAPN2
CAPN2 g.p. (Homo sapiens)
-
-
-
-
EC 3.4.22.17
EC 3.4.24.5
-
-
formerly, part transferred
-
m-calpain
milli-calpain
-
-
-
-
calpain 2
-
-
-
-
calpain 2
-
-
calpain II
-
-
-
-
m-calpain
-
-
-
-
m-calpain
-
-
m-calpain
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
broad endopeptidase specificity
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
hydrolysis of peptide bond
-
-
endopeptidase
-
hydrolysis of peptide bond
-
-
peptides, endopeptidase
-
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CAS REGISTRY NUMBER
COMMENTARY
702693-80-9
-
78990-62-2
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
alpha-neoendorphin + H2O
?
-
Substrates: cleavage of the 6Arg-7Lys bond
Products: -
Products: -
?
alpha-tubulin + H2O
?
-
Substrates: complete digestion of alpha-tubulin with little effect on beta-tubulin
Products: -
Products: -
?
androgen receptor + H2O
low molecular weight androgen receptor + ?
-
Substrates: -
Products: -
Products: -
?
beta-lipotropin(61-91) + H2O
?
-
Substrates: cleavage of the bonds: Thr76-Leu77, Lys84-Asn85 and Lys88-Lys89
Products: -
Products: -
?
beta-neoendorphin + H2O
?
-
Substrates: cleavage of the 6Arg-7Lys bond
Products: -
Products: -
?
beta-transducin repeat containing protein + H2O
?
-
Substrates: -
Products: -
Products: -
?
Boc-Leu-Met-7-amido-4-chloromethylcoumarin + H2O
Boc-Leu-Met + 7-amino-4-chloromethylcoumarin
-
Substrates: 10 microM, 20 min, 37 °C, with or without magnetic bead stimulation
Products: -
Products: -
?
Boc-Leu-Met-7-amino-4-chloromethylcoumarin
?
-
Substrates: -
Products: -
Products: -
?
collapsin response mediator protein 1 + H2O
?
-
Substrates: -
Products: -
Products: -
?
collapsin response mediator protein 2 + H2O
?
-
Substrates: -
Products: -
Products: -
?
collapsin response mediator protein 3 + H2O
?
-
Substrates: -
Products: -
Products: -
?
collapsin response mediator protein 4 + H2O
?
-
Substrates: -
Products: -
Products: -
?
collapsin response mediator protein-1 + H2O
?
-
Substrates: collapsin response mediator protein-1 is cleaved by calpain-2 at the C-terminus
Products: -
Products: -
?
collapsin response mediator protein-2 + H2O
?
-
Substrates: collapsin response mediator protein-2 is cleaved by calpain-2 at the C-terminus
Products: -
Products: -
?
collapsin response mediator protein-4 + H2O
?
-
Substrates: collapsin response mediator protein-4 is cleaved by calpain-2 at the C-terminus
Products: -
Products: -
?
collapsin response mediator protein-5 + H2O
?
-
Substrates: -
Products: -
Products: -
?
dihydropteridine reductase + H2O
?
-
Substrates: the dihydropteridine reductase 29000 Da subunit is cleaved just before the 35th Ser and the 48th Val residue from the N-terminus, generating two new fragments of 21000 Da and 19000 Da which are more active than the native enzyme
Products: -
Products: -
?
dynorphin (1-13) + H2O
?
-
Substrates: cleavage of the 6Arg-7Arg bond
Products: -
Products: -
?
focal adhesion kinase + H2O
?
-
Substrates: the preferred calpain cleavage site is between the two C-terminal proline-rich regions after Ser-745
Products: -
Products: -
?
FRET-based substrate PLFAER + H2O
?
Substrates: 10 microM, pH 7.4, 1 mM of CaCl2 added to initiate the reaction
Products: -
Products: -
?
heterogeneous nuclear ribonucleoprotein F + H2O
?
-
Substrates: -
Products: -
Products: -
?
heterogeneous nuclear ribonucleoprotein K + H2O
?
-
Substrates: -
Products: -
Products: -
?
human junctophilin-2 + H2O
75 kDa junctophilin-2 N-terminal fragment + 25 kDa junctophilin-2 C-terminal fragment
-
Substrates: cleavage occurs between arginine 572 and threonine 573
Products: -
Products: -
?
IP3R1 + H2O
?
-
Substrates: in presence of Ca2þ, m-calpain cleaves IP3R1 in the endoplasmic lumen
Products: -
Products: -
?
junctophilin-2 + H2O
?
Substrates: cleaved between R565 and T566. Calpain-2 cleaves junctophilin-2 at the same functionally conserved R565/T566 site as calpain-1 but with less efficacy
Products: -
Products: -
?
junctophillin-2 + H2O
?
Substrates: junctophillin-2 (JPH2) is cleaved in its C-terminal domain by CAPN2 at the 482G-T483 site forming a 25 kDa JPH2-CTP. The calpain-2 isoform is responsible for the cleavage of JPH2 C-terminal fragment (JPH2-CTP)
Products: -
Products: -
?
Leu-enkephalin + H2O
?
-
Substrates: cleaved only slightly at the 1Tyr-2Gly bond
Products: -
Products: -
?
mammalian actin-binding protein-1 + H2O
?
-
Substrates: the preferred cleavage site occurs between the actin-binding domain and the proline-rich region, generating a C-terminal mAbp1 fragment
Products: -
Products: -
?
Met-enkephalin + H2O
?
-
Substrates: cleaved only slightly at the 1Tyr-2Gly bond
Products: -
Products: -
?
mouse junctophilin-2 + H2O
75 kDa junctophilin-2 N-terminal fragment + 25 kDa junctophilin-2 C-terminal fragment
-
Substrates: cleavage occurs between arginine 565 and threonine 566
Products: -
Products: -
?
N-acetyl-LLY-7-amido-4-trifluoromethylcoumarin + H2O
N-acetyl-LLY + 7-amino-4-trifluoromethylcoumarin
-
Substrates: -
Products: -
Products: -
?
N-succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
N-succinyl-Leu-Leu-Val-Tyr + 7-amino-4-methylcoumarin
N-succinyl-Leu-Tyr-7-amido-4-methylcoumarin + H2O
N-succinyl-Leu-Tyr + 7-amino-4-methylcoumarin
-
Substrates: -
Products: -
Products: -
?
N-succinyl-LLVY-7-amido-4-methylcoumarin + H2O
N-succinyl-LLVY + 7-amino-4-methylcoumarin
Substrates: -
Products: -
Products: -
?
Na+/Ca2+ exchanger-1 + H2O
82 kDa fragment + ?
-
Substrates: calcium-dependent proteolytic cleavage of Na+/Ca2+ exchanger-1 occurs in the caveolae vesicles
Products: -
Products: -
?
neurotensin + H2O
?
-
Substrates: cleavage of the 3Tyr-4Glu bond and the 5Asn-6Lys bond
Products: -
Products: -
?
p35 + H2O
25000 Da fragment of p35 + ?
-
Substrates: calpain-specific substrate
Products: -
Products: -
?
procaspase-12 + H2O
active caspase-12 + ?
Substrates: -
Products: -
Products: -
?
protein tyrosine phosphatase PTPN13 + H2O
?
Substrates: also known as Fas-associated protein-1
Products: -
Products: -
?
protein tyrosine phosphatase, non-receptor type 13 + H2O
?
-
Substrates: -
Products: -
Products: -
?
proteolysis-resistant fragment 130 + H2O
proteolysis-resistant fragment 45 + ?
-
Substrates: -
Products: -
Products: -
?
proteolysis-resistant fragment 72 + H2O
proteolysis-resistant fragment 45 + ?
-
Substrates: -
Products: -
Products: -
?
selenoprotein K + H2O
?
-
Substrates: cleavage occurs only in unactivated macrophages, m-calpain cleavage at Arg81-Gly82 generates the two selenoprotein K isoforms
Products: -
Products: -
?
SLLVY-7-amido-4-methylcoumarin + H2O
SLLVY + 7-amino-4-methylcoumarin
-
Substrates: -
Products: -
Products: -
?
striatal-enriched tyrosine phosphatase + H2O
?
Substrates: -
Products: -
Products: -
?
succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
succinyl-Leu-Leu-Val-Tyr + 7-amino-4-methylcoumarin
succinyl-Leu-Met-7-amido-4-methylcoumarin + H2O
succinyl-Leu-Met + 7-amino-4-methylcoumarin
-
Substrates: -
Products: -
Products: -
?
succinyl-Leu-Tyr-7-amido-4-methylcoumarin + H2O
?
-
Substrates: -
Products: -
Products: -
?
succinyl-Leu-Tyr-7-amido-4-methylcoumarin + H2O
succinyl-Leu-Tyr + 7-amino-4-methylcoumarin
t-butyloxycarbonyl-Val-Leu-Lys-7-amido-4-methylcoumarin + H2O
t-butyloxycarbonyl-Val-Leu-Lys + 7-amino-4-methylcoumarin
-
Substrates: -
Products: -
Products: -
?
tert-butoxycarbonyl-Leu-Met-7-amido-4-chloromethylcoumarin + H2O
tert-butoxycarbonyl-Leu-Met + 7-amino-4-chloromethylcoumarin
-
Substrates: -
Products: -
Products: -
?
tert-butyloxycarbonyl-L-leucyl-L-methionine-7-amido-4-chloromethylcoumarin + H2O
tert-butyloxycarbonyl-L-leucyl-L-methionine + 7-amino-4-chloromethylcoumarin
-
Substrates: -
Products: -
Products: -
?
tuberous sclerosis protein 1 + H2O
?
-
Substrates: also known as hamartin
Products: -
Products: -
?
tuberous sclerosis protein 2 + H2O
?
-
Substrates: also known as tuberin
Products: -
Products: -
?
voltage-dependent anion channel + H2O
?
-
Substrates: mitochondrial m-calpain truncates voltage-dependent anion channel in Ca2+-dependent manner
Products: -
Products: -
?
calmodulin-dependent protein kinase II deltaB + H2O
?
Substrates: angiotensin II enhances the interaction between activated calpain-2 and Ca2+/calmodulin-dependent protein kinase II deltaB (CaMKIIdB), and promotes the degradation of CaMKIIdB by calpain-2 in the nuclei of hypertrophied cardiomyocytes. The depressed CaMKIIdeltaB downregulates the expression of antiapoptotic Bcl-2 leading to mitochondrial depolarization and release of cytochrome c which leads to apoptosis of hypertrophied cardiomyocytes
Products: -
Products: -
?
calmodulin-dependent protein kinase II deltaB + H2O
?
Substrates: -
Products: -
Products: -
?
calpain-1 + H2O
?
-
Substrates: cleavage occurs between 126 and 127 amino acids. The enzyme further trims the N-terminal region of 76-kDa calpain-1 fragment and destabilizes the autolyzed form of calpain-1
Products: -
Products: -
?
calpain-1 + H2O
?
Substrates: calpain-2 cuts calpain-1 specific autolysis sites in its PC1 domain
Products: -
Products: -
?
casein + H2O
?
-
Substrates: -
Products: -
Products: -
?
crystallin + H2O
?
-
Substrates: alphaA crystallin in lenses from wild-type mice is proteolyzed by both calpain 2 and Lp82. Crystallins proteolyzed by calpain Lp82 are more susceptible to insolubilization than crystallins proteolyzed by calpain 2
Products: -
Products: -
?
GAP-43 + H2O
GAP-43-3 + ?
-
Substrates: GAP-43 cleavage at Ser41 residue in synaptosomes is mediated by m-calpain
Products: -
Products: -
?
GAP-43 + H2O
GAP-43-3 + ?
-
Substrates: a GAP-43 fragment, lacking about 40 N-terminal residues (named GAP-43-3), is produced by m-calpain. The fragment prevents complete cleavage of intact GAP-43 by m-calpain as a negative feedback
Products: -
Products: -
?
GAP-43 + H2O
GAP-43-3 + ?
-
Substrates: a GAP-43 fragment, lacking about 40 N-terminal residues (named GAP-43-3), is produced by m-calpain. The fragment prevents complete cleavage of intact GAP-43 by m-calpain as a negative feedback
Products: -
Products: -
?
IkappaBalpha + H2O
?
-
Substrates: a parallel pathway that degrades IkappaBalpha and activates NF-kappaB activation independently of the ubiquitin-proteasome pathway
Products: -
Products: -
?
junctophilin-2 + H2O
C-terminal junctophilin-2 peptide + ?
Substrates: -
Products: -
Products: -
?
junctophilin-2 + H2O
C-terminal junctophilin-2 peptide + ?
-
Substrates: -
Products: -
Products: -
?
LIM kinase-1 + H2O
?
Substrates: cleavage and activation of LIM kinase 1 is a mechanism for calpain 2-mediated regulation of nuclear dynamics
Products: -
Products: -
?
MARCKS protein + H2O
?
Substrates: MARCKS protein i.e. myristoylated alanine-rich C kinase substrate is a substrate of calpain-2 in the presence of Ca2+. Calpain-2 proteolysis of MARCKS promotes its interaction with lipids and ENaC at the plasma membrane to allow for the phosphatidylinositol 4,5-bisphosphate (PIP2)-dependent regulation of epithelial sodium channel (ENaC) activity in the kidney
Products: -
Products: -
?
MARCKS protein + H2O
?
Substrates: MARCKS protein i.e. myristoylated alanine-rich C kinase substrate is a substrate of calpain-2 in the presence of Ca2+
Products: -
Products: -
?
myocillin + H2O
?
-
Substrates: calpain II is responsible for the intracellular processing of myocilin in the lumen of the endoplasmic reticulum. It is proposed that this cleavage might regulate extracellular interactions of myocilin, contributing to the control of intraocular pressure
Products: -
Products: -
?
N-succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
N-succinyl-Leu-Leu-Val-Tyr + 7-amino-4-methylcoumarin
Substrates: -
Products: -
Products: -
?
N-succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
N-succinyl-Leu-Leu-Val-Tyr + 7-amino-4-methylcoumarin
Substrates: -
Products: -
Products: -
?
N-succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
N-succinyl-Leu-Leu-Val-Tyr + 7-amino-4-methylcoumarin
Substrates: -
Products: -
Products: -
?
Reg-1alpha + H2O
?
-
Substrates: also known as pancreatic stone protein or lithostathine. Cleavage occurs between Gln4 and Thr5, impeded by the presence of the neighboring glycosylation of Thr5
Products: -
Products: -
?
Reg-1alpha + H2O
?
Substrates: human Reg-1alpha. The cleavage site between Gln4 and Thr5. The cleavage is impeded by the presence of the neighboring glycosylation of Thr5. Calpain-2 is not able to cleave the glycosylated form of Reg-1alpha
Products: -
Products: -
?
striatal-enriched protein tyrosine phosphatase + H2O
?
Substrates: calpain-2 activation cleaves striatal-enriched protein tyrosine phosphatase and activates STEP-mediated pro-death pathway in retinal ganglion cells after intraocular pressure elevation
Products: -
Products: -
?
striatal-enriched protein tyrosine phosphatase + H2O
?
Substrates: -
Products: -
Products: -
?
succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
?
-
Substrates: -
Products: -
Products: -
?
succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
?
-
Substrates: -
Products: -
Products: -
?
succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
succinyl-Leu-Leu-Val-Tyr + 7-amino-4-methylcoumarin
-
Substrates: -
Products: -
Products: -
?
succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
succinyl-Leu-Leu-Val-Tyr + 7-amino-4-methylcoumarin
-
Substrates: -
Products: -
Products: -
?
succinyl-Leu-Tyr-7-amido-4-methylcoumarin + H2O
succinyl-Leu-Tyr + 7-amino-4-methylcoumarin
-
Substrates: -
Products: -
Products: -
?
succinyl-Leu-Tyr-7-amido-4-methylcoumarin + H2O
succinyl-Leu-Tyr + 7-amino-4-methylcoumarin
-
Substrates: -
Products: -
Products: -
?
succinyl-Leu-Tyr-7-amido-4-methylcoumarin + H2O
succinyl-Leu-Tyr + 7-amino-4-methylcoumarin
-
Substrates: -
Products: -
Products: -
?
t-butyloxycarbonyl-L-leucyl-L-methionine amide + H2O
?
-
Substrates: -
Products: -
Products: -
?
t-butyloxycarbonyl-L-leucyl-L-methionine amide + H2O
?
-
Substrates: -
Products: -
Products: -
?
desmin + H2O
additional information
-
-
Substrates: -
Products: two proteolytic fragments of 35000 Da and of 16000 Da
Products: two proteolytic fragments of 35000 Da and of 16000 Da
?
additional information
?
-
-
Substrates: the enzyme might be involved in light-dependent regulation of disk membrane morphogenesis by proteolysis of myosin II
Products: -
Products: -
?
additional information
?
-
-
Substrates: fetuin A is a potential extracellular regulator of m-calpain at nascent sites of plasma membrane wounding
Products: -
Products: -
?
additional information
?
-
Substrates: enzyme is involved in cytoskeleton remodelling and signal transduction
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme is involved in cytoskeleton remodelling and signal transduction
Products: -
Products: -
?
additional information
?
-
Substrates: enzyme is involved in essential cellular functions mediated by calcium. Tandemly reiterated negative enhancer-like elements regulate transcription of a human gene for the large subunit
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme plays a pivotal role during the earlier stages of myogenesis, particularly during fusion. MyoD and myogenin can transactivate capn2, but MyoD shows a higher transactivation level for the regulatory sequences
Products: -
Products: -
?
additional information
?
-
Substrates: pathological conditions associated with the gene of calpain 2: muscular dystrophy, stroke, traumatic brain injury, spinal cord injury, Alzheimer's diseases, Parkinson's disease, neurodegenerative disorders, cataracts, cancer
Products: -
Products: -
?
additional information
?
-
-
Substrates: pathological conditions associated with the gene of calpain 2: muscular dystrophy, stroke, traumatic brain injury, spinal cord injury, Alzheimer's diseases, Parkinson's disease, neurodegenerative disorders, cataracts, cancer
Products: -
Products: -
?
additional information
?
-
-
Substrates: calpain mediates calcium-induced activation of the Erk1,2 MAPK pathway and cytoskeletal phosphorylation in neurons
Products: -
Products: -
?
additional information
?
-
-
Substrates: calpain mediates angiogenic effects induced by vascular endothelial growth factor by modulating actin cytoskeletal organization
Products: -
Products: -
?
additional information
?
-
-
Substrates: M-calpain is the major candidate of the proteinase to generate the aggrecan product with the COOH terminal neoepitope VPGVA709 (consisting of two NH2 terminal globular domain G1 and G2 and KS side chains) during the intracellular aggrecan processing
Products: -
Products: -
?
additional information
?
-
-
Substrates: catalytic activity of calpain is required to limit pseudopod formation in the direction of chemoattractant and for efficient chemotaxis. Calpain 2 is a novel component of the frontness signal that promotes polarization during chemotaxis
Products: -
Products: -
?
additional information
?
-
-
Substrates: calpain-2 plays an important role in lung endothelial cell migration and proliferation
Products: -
Products: -
?
additional information
?
-
-
Substrates: m-calpain activity is triggered by Ca2+-influx and promoted mainly through the phosphatidylinositol 3-kinase pathway
Products: -
Products: -
?
additional information
?
-
-
Substrates: calpain 2activity is critical for the life cycle of echovirus 1 and important in the multiplication of the viral RNA genome
Products: -
Products: -
?
additional information
?
-
-
Substrates: caspase-8 associates with calpain-2
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is not able to cleave the O-glycosylated form of Reg-1alpha
Products: -
Products: -
-
additional information
?
-
-
Substrates: epidermal growth factor receptor activation of calpain is required for fibroblast motility and occurs via an ERK/MAP kinase signaling pathway
Products: -
Products: -
?
additional information
?
-
-
Substrates: calpain 2 plays a role in limiting membrane protrusion and in regulating lamellipodial dynamics at the leading edge of migrating cells
Products: -
Products: -
?
additional information
?
-
-
Substrates: functions for nCL-2 involve the membrane trafficking of mucus cells by interacting with coat proteins
Products: -
Products: -
?
additional information
?
-
-
Substrates: calpain 2 is likely to be involved with signal transduction events in the lens
Products: -
Products: -
?
additional information
?
-
-
Substrates: CAPN2 may represent a key factor in development from the first cell division
Products: -
Products: -
?
additional information
?
-
Substrates: m-calpain is vital for development of the preimplantation murine embryo
Products: -
Products: -
?
additional information
?
-
-
Substrates: m-calpain is vital for development of the preimplantation murine embryo
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is involved in myoblast fusion by cleaving certain proteins. This cleavage could modify membrane and cytoskeleton organization for the myoblast to fuse
Products: -
Products: -
?
additional information
?
-
-
Substrates: mu-calpain, m-calpain, 20S proteasome, dipeptidyl peptidase II and III and soluble alanyl aminopeptidase are thought to induce lens opacification kinetically during cataract formation in Shumiya cataract rats through the intracellular turnover of lens proteins
Products: -
Products: -
?
additional information
?
-
-
Substrates: calpain-mediated impairment of Na+/K+-ATPase activity during early reperfusion contributes to cell death after myocardial ischemia
Products: -
Products: -
?
additional information
?
-
-
Substrates: ERp75 plays important role in the refolding of mitochondrial m-calpain large subunit, cytosolic m-calpain does not associate with ERp57
Products: -
Products: -
?
additional information
?
-
-
Substrates: representatives of the protein phosphatase 2A subunit classes C, PR65/A, PR55/B and PR61/B' are resistant to m-calpain-mediated degradation
Products: -
Products: -
?
additional information
?
-
Substrates: enzyme is involved in myofibrillar protein degradation
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme is involved in myofibrillar protein degradation
Products: -
Products: -
?
additional information
?
-
Substrates: hypoxia upregulates calpain activity and mRNA expression in pulmonary artery endothelial cells
Products: -
Products: -
?
vimentin + H2O
additional information
-
-
Substrates: -
Products: four proteolytic fragments: 3 major compounds of 54000 Da, 46000 Da and 20000 Da, and a minor fragment of 28000 Da
Products: four proteolytic fragments: 3 major compounds of 54000 Da, 46000 Da and 20000 Da, and a minor fragment of 28000 Da
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
beta-transducin repeat containing protein + H2O
?
-
Substrates: -
Products: -
Products: -
?
calmodulin-dependent protein kinase II deltaB + H2O
?
Substrates: angiotensin II enhances the interaction between activated calpain-2 and Ca2+/calmodulin-dependent protein kinase II deltaB (CaMKIIdB), and promotes the degradation of CaMKIIdB by calpain-2 in the nuclei of hypertrophied cardiomyocytes. The depressed CaMKIIdeltaB downregulates the expression of antiapoptotic Bcl-2 leading to mitochondrial depolarization and release of cytochrome c which leads to apoptosis of hypertrophied cardiomyocytes
Products: -
Products: -
?
collapsin response mediator protein-1 + H2O
?
-
Substrates: collapsin response mediator protein-1 is cleaved by calpain-2 at the C-terminus
Products: -
Products: -
?
collapsin response mediator protein-2 + H2O
?
-
Substrates: collapsin response mediator protein-2 is cleaved by calpain-2 at the C-terminus
Products: -
Products: -
?
collapsin response mediator protein-4 + H2O
?
-
Substrates: collapsin response mediator protein-4 is cleaved by calpain-2 at the C-terminus
Products: -
Products: -
?
collapsin response mediator protein-5 + H2O
?
-
Substrates: -
Products: -
Products: -
?
crystallin + H2O
?
-
Substrates: alphaA crystallin in lenses from wild-type mice is proteolyzed by both calpain 2 and Lp82. Crystallins proteolyzed by calpain Lp82 are more susceptible to insolubilization than crystallins proteolyzed by calpain 2
Products: -
Products: -
?
dihydropteridine reductase + H2O
?
-
Substrates: the dihydropteridine reductase 29000 Da subunit is cleaved just before the 35th Ser and the 48th Val residue from the N-terminus, generating two new fragments of 21000 Da and 19000 Da which are more active than the native enzyme
Products: -
Products: -
?
GAP-43 + H2O
GAP-43-3 + ?
-
Substrates: GAP-43 cleavage at Ser41 residue in synaptosomes is mediated by m-calpain
Products: -
Products: -
?
heterogeneous nuclear ribonucleoprotein F + H2O
?
-
Substrates: -
Products: -
Products: -
?
heterogeneous nuclear ribonucleoprotein K + H2O
?
-
Substrates: -
Products: -
Products: -
?
IkappaBalpha + H2O
?
-
Substrates: a parallel pathway that degrades IkappaBalpha and activates NF-kappaB activation independently of the ubiquitin-proteasome pathway
Products: -
Products: -
?
IP3R1 + H2O
?
-
Substrates: in presence of Ca2þ, m-calpain cleaves IP3R1 in the endoplasmic lumen
Products: -
Products: -
?
LIM kinase-1 + H2O
?
Substrates: cleavage and activation of LIM kinase 1 is a mechanism for calpain 2-mediated regulation of nuclear dynamics
Products: -
Products: -
?
mammalian actin-binding protein-1 + H2O
?
-
Substrates: the preferred cleavage site occurs between the actin-binding domain and the proline-rich region, generating a C-terminal mAbp1 fragment
Products: -
Products: -
?
MARCKS protein + H2O
?
Substrates: MARCKS protein i.e. myristoylated alanine-rich C kinase substrate is a substrate of calpain-2 in the presence of Ca2+. Calpain-2 proteolysis of MARCKS promotes its interaction with lipids and ENaC at the plasma membrane to allow for the phosphatidylinositol 4,5-bisphosphate (PIP2)-dependent regulation of epithelial sodium channel (ENaC) activity in the kidney
Products: -
Products: -
?
myocillin + H2O
?
-
Substrates: calpain II is responsible for the intracellular processing of myocilin in the lumen of the endoplasmic reticulum. It is proposed that this cleavage might regulate extracellular interactions of myocilin, contributing to the control of intraocular pressure
Products: -
Products: -
?
p35 + H2O
25000 Da fragment of p35 + ?
-
Substrates: calpain-specific substrate
Products: -
Products: -
?
protein tyrosine phosphatase, non-receptor type 13 + H2O
?
-
Substrates: -
Products: -
Products: -
?
selenoprotein K + H2O
?
-
Substrates: cleavage occurs only in unactivated macrophages, m-calpain cleavage at Arg81-Gly82 generates the two selenoprotein K isoforms
Products: -
Products: -
?
striatal-enriched protein tyrosine phosphatase + H2O
?
Substrates: calpain-2 activation cleaves striatal-enriched protein tyrosine phosphatase and activates STEP-mediated pro-death pathway in retinal ganglion cells after intraocular pressure elevation
Products: -
Products: -
?
tuberous sclerosis protein 1 + H2O
?
-
Substrates: also known as hamartin
Products: -
Products: -
?
tuberous sclerosis protein 2 + H2O
?
-
Substrates: also known as tuberin
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme might be involved in light-dependent regulation of disk membrane morphogenesis by proteolysis of myosin II
Products: -
Products: -
?
additional information
?
-
-
Substrates: fetuin A is a potential extracellular regulator of m-calpain at nascent sites of plasma membrane wounding
Products: -
Products: -
?
additional information
?
-
Substrates: enzyme is involved in cytoskeleton remodelling and signal transduction
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme is involved in cytoskeleton remodelling and signal transduction
Products: -
Products: -
?
additional information
?
-
Substrates: enzyme is involved in essential cellular functions mediated by calcium. Tandemly reiterated negative enhancer-like elements regulate transcription of a human gene for the large subunit
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme plays a pivotal role during the earlier stages of myogenesis, particularly during fusion. MyoD and myogenin can transactivate capn2, but MyoD shows a higher transactivation level for the regulatory sequences
Products: -
Products: -
?
additional information
?
-
Substrates: pathological conditions associated with the gene of calpain 2: muscular dystrophy, stroke, traumatic brain injury, spinal cord injury, Alzheimer's diseases, Parkinson's disease, neurodegenerative disorders, cataracts, cancer
Products: -
Products: -
?
additional information
?
-
-
Substrates: pathological conditions associated with the gene of calpain 2: muscular dystrophy, stroke, traumatic brain injury, spinal cord injury, Alzheimer's diseases, Parkinson's disease, neurodegenerative disorders, cataracts, cancer
Products: -
Products: -
?
additional information
?
-
-
Substrates: calpain mediates calcium-induced activation of the Erk1,2 MAPK pathway and cytoskeletal phosphorylation in neurons
Products: -
Products: -
?
additional information
?
-
-
Substrates: calpain mediates angiogenic effects induced by vascular endothelial growth factor by modulating actin cytoskeletal organization
Products: -
Products: -
?
additional information
?
-
-
Substrates: M-calpain is the major candidate of the proteinase to generate the aggrecan product with the COOH terminal neoepitope VPGVA709 (consisting of two NH2 terminal globular domain G1 and G2 and KS side chains) during the intracellular aggrecan processing
Products: -
Products: -
?
additional information
?
-
-
Substrates: catalytic activity of calpain is required to limit pseudopod formation in the direction of chemoattractant and for efficient chemotaxis. Calpain 2 is a novel component of the frontness signal that promotes polarization during chemotaxis
Products: -
Products: -
?
additional information
?
-
-
Substrates: calpain-2 plays an important role in lung endothelial cell migration and proliferation
Products: -
Products: -
?
additional information
?
-
-
Substrates: m-calpain activity is triggered by Ca2+-influx and promoted mainly through the phosphatidylinositol 3-kinase pathway
Products: -
Products: -
?
additional information
?
-
-
Substrates: calpain 2activity is critical for the life cycle of echovirus 1 and important in the multiplication of the viral RNA genome
Products: -
Products: -
?
additional information
?
-
-
Substrates: epidermal growth factor receptor activation of calpain is required for fibroblast motility and occurs via an ERK/MAP kinase signaling pathway
Products: -
Products: -
?
additional information
?
-
-
Substrates: calpain 2 plays a role in limiting membrane protrusion and in regulating lamellipodial dynamics at the leading edge of migrating cells
Products: -
Products: -
?
additional information
?
-
-
Substrates: functions for nCL-2 involve the membrane trafficking of mucus cells by interacting with coat proteins
Products: -
Products: -
?
additional information
?
-
-
Substrates: calpain 2 is likely to be involved with signal transduction events in the lens
Products: -
Products: -
?
additional information
?
-
-
Substrates: CAPN2 may represent a key factor in development from the first cell division
Products: -
Products: -
?
additional information
?
-
Substrates: m-calpain is vital for development of the preimplantation murine embryo
Products: -
Products: -
?
additional information
?
-
-
Substrates: m-calpain is vital for development of the preimplantation murine embryo
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is involved in myoblast fusion by cleaving certain proteins. This cleavage could modify membrane and cytoskeleton organization for the myoblast to fuse
Products: -
Products: -
?
additional information
?
-
-
Substrates: mu-calpain, m-calpain, 20S proteasome, dipeptidyl peptidase II and III and soluble alanyl aminopeptidase are thought to induce lens opacification kinetically during cataract formation in Shumiya cataract rats through the intracellular turnover of lens proteins
Products: -
Products: -
?
additional information
?
-
-
Substrates: calpain-mediated impairment of Na+/K+-ATPase activity during early reperfusion contributes to cell death after myocardial ischemia
Products: -
Products: -
?
additional information
?
-
-
Substrates: ERp75 plays important role in the refolding of mitochondrial m-calpain large subunit, cytosolic m-calpain does not associate with ERp57
Products: -
Products: -
?
additional information
?
-
Substrates: enzyme is involved in myofibrillar protein degradation
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme is involved in myofibrillar protein degradation
Products: -
Products: -
?
additional information
?
-
Substrates: hypoxia upregulates calpain activity and mRNA expression in pulmonary artery endothelial cells
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Al3+
-
millimolar concentrations of Al3+ activate at at submillimolar concentrations of Ca2+
Ba2+
Ca2+
Mg2+
Mn2+
Sr2+
Ba2+
-
1 mM, decreases the Ca2+-requirement for maximal activity from 0.4 mM to 0.3 mM. Synergistic activating effect with Ca2+
Ca2+
-
half maximal activity for retina and brain enzyme is 0.262 mM and 0.311 mM, maximal activity near 1 mM, no activity in presence of 0.03 mM
Ca2+
-
treatment of the endoplasmic reticulum with Ca2+ (5 mM) dissociates m-calpain-calpastatin association leading to the activation of m-calpain
Ca2+
-
best activator at 2.5 mM, maximal caseinolytic activity at 2.2 mM, half-maximal caseinolytic activity at 0.312 mM
Ca2+
-
Kd-value: 0.325 mM. 25% of the difference in Kd values between mu-calpain and m-calpain can be ascribed to the N-terminal peptide of the large subunit, whereas the C-terminal EF-hand-containing domain IV accounts for 65% of the difference
Ca2+
-
the Ca2+ dependency of mitochondrial m-calpain is similar to that of cytosolic m-calpain, 1 mM Ca2+ activates.
Ca2+
-
Ca2+-induced calpain translocation to the membrane during ischemia is independent of its activation
Ca2+
Ca2+-binding must induce conformational changes that reorient the protease domains to form a functional active site
Ca2+
activates. The results support the hypothesis that Ca2+ induces movement of domains I and II closer together to form the functional active site of calpain
Ca2+
half-maximal activity is 0.242 mM for wilde-type enzyme, 0.129 mM for the E504S mutant, 0.226 mM for the K226S mutant, 0.261 mM for the K230S mutant, 0.183 mM for the K234 mutant, 0.256 mM for the K230E mutant and 0.159 mM for the K234E mutant
Mg2+
-
1 mM decreases the Ca2+-requirement for maximal activity from 0.4 mM to 0.3 mM. Synergistic activating effect with Ca2+
Mn2+
-
1 mM, decreases the half-maximal Ca2+-requirement from 0.4 mM to 0.1 mM, decreases the Ca2+-requirement for maximal activity from 1.5 mM to 1 mM
Mn2+
-
5 mM 73.6% of the activation with 5 mM Ca2+. Synergistic activating effect with Ca2+
Sr2+
-
2.5 mM, 66% of the activation obtained with Ca2+, maximal caseinolytic activity at 5.9 mM, half-maximal caseinolytic activity at 1.886 mM. Autolysis in presence of 5 mM Ca2+. The 80000 Da subunit is rapidly autolyzed in two smaller bands of 73000 Da and 69000 Da. The small subunit of 24000 da is degraded into three bands of 22000 Da, 19300 Da and 17800 Da. It is not clear whether autolysis is necessary for calpain to become proteolytically active
Sr2+
-
1 mM, decreases the half-maximal Ca2+-requirement from 0.4 mM to 0.1 mM, decreases the Ca2+-requirement for maximal activity from 1.5 mM to 1 mM. Synergistic activating effect with Ca2+
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(2S)-3-phenyl-2-([[(2S)-1-(phenylsulfonyl)pyrrolidin-2-yl]carbonyl]amino)propanoic acid
-
-
(2S,3S)-trans-epoxysuccinyl-L-leucylamido-3-methylbutane ethyl ester
-
0.01 mM, 50% inhibition
1,2-bis(o-aminophenoxy)ethane-N,N,N',N'-tetraacetic acid tetra(acetoxymethyl) ester
-
-
4-[[(3,4-dinitrophenyl)carbonyl]amino]-2-(6-hydroxy-3-oxo-3H-xanthen-9-yl)benzoic acid
-
5 mM, 23% inhibition
benzyloxycarbonyl-Leu-Abu-CONH-CH2-C6H3(3,5-(OMe)2)
calpain-2 selective inhibitor. A selective calpain-2 inhibitor could prevent acute glaucoma-induced retinal ganglion cell death and blindness
Ep-475
-
0.001 mM, 49% inhibition of the enzyme from retina, 46% inhibition of the enzyme from brain
N2-[(benzyloxy)carbonyl]-N-[(3S)-1-[(3,5-dimethoxybenzyl)amino]-1,2-dioxo-3-pentanyl]-L-leucinamide
-
i.e. NA101, selective inhibitor
-
Polyethylene glycol
-
PEG-4000, PEG-100000 or PEG-20000, inhibition at concentrations higher than 0.5%
calpastatin
-
inhibition of m-calpain is greater at pH 7.5 than at pH 6.5 at both 165 mM and 295 mM NaCl. Percentage inhibition is greater at 295 mM than at 165 mM NaCl
-
calpastatin
-
oxidation lowers calpastatin inhibition of m-calpain at al pH and ionic strength combinations
-
calpeptin
-
50% inhibition of maximal caseinolytic activity at 10 nM and 21 nM for retinal and brain calpain
GAP-43-3
-
a GAP-43 fragment, lacking about 40 N-terminal residues (named GAP-43-3), is produced by m-calpain-mediated cleavage of GAP-43. The fragment prevents complete cleavage of intact GAP-43 by m-calpain as a negative feedback. GAP-43-3 also blocks m-calpain activity against casein
-
GAP-43-3
-
a GAP-43 fragment, lacking about 40 N-terminal residues (named GAP-43-3), is produced by m-calpain-mediated cleavage of GAP-43. The fragment prevents complete cleavage of intact GAP-43 by m-calpain as a negative feedback. GAP-43-3 also blocks m-calpain activity against casein
-
additional information
-
suppression of calpain-2 expression with adenovirus vector-mediated RNAi
-
additional information
-
specific capn2 shRNA reduces expression of the targeted isoform
-
additional information
-
not inhibited by benzyloxycarbonyl-VAD-fluoromethylketone
-
additional information
-
not inhibited by Ac-Thr-Pro-Leu-alpha-azaglycine-Ser-Pro-NH2, Ac-Pro-Leu-alpha-azaglycine-Ser-Pro-Pro-Pro-Ser-NH2, Ac-Leu-alpha-azaglycine-Ser-Pro-Pro-Pro-Ser-NH2, Ac-alpha-azaglycine-Ser-Pro-Pro-Pro-Ser-NH2, Ac-Thr-Pro-Thr-alpha-azaglycine-Ser-Pro-Pro-Pro-Ser-NH2, Ac-Thr-Pro-Leu-alpha-azaglycine-Ser-Ser-Pro-Pro-Ser-NH2, Ac-Thr-Pro-Leu-alpha-azaglycine-Ser-Gln-Pro-Pro-Ser-NH2, Ac-Thr-Pro-Val-alpha-azaglycine-Ser-Pro-Pro-Pro-Ser-NH2, Ac-Thr-Pro-Leu-alpha-azaglycine-Thr-Pro-Pro-Pro-Ser-NH2, and Ac-Thr-Pro-Leu-alpha-azaglycine-Arg-Pro-Pro-Pro-Ser-NH2
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
upregulation of calpain 2 post eccentric exercise
-
additional information
-
increase of m-calpain expression by mechanical stimulation via laminin receptors
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.459
succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin
-
endoplasmic reticulum lumen m-calpain, in 100 mM imidazole-HCl buffer (pH 7.5), 5 mM L-cysteine, 2.5 mM 2-mercaptoethanol, 5 mM CaCl2, and 4% (v/v) dimethyl sulfoxide, at 30°C
0.461
succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin
-
endoplasmic reticulum membrane m-calpain, in 100 mM imidazole-HCl buffer (pH 7.5), 5 mM L-cysteine, 2.5 mM 2-mercaptoethanol, 5 mM CaCl2, and 4% (v/v) dimethyl sulfoxide, at 30°C
4.66
succinyl-Leu-Met-7-amido-4-methylcoumarin
-
endoplasmic reticulum membrane m-calpain, in 100 mM imidazole-HCl buffer (pH 7.5), 5 mM L-cysteine, 2.5 mM 2-mercaptoethanol, 5 mM CaCl2, and 4% (v/v) dimethyl sulfoxide, at 30°C
4.68
succinyl-Leu-Met-7-amido-4-methylcoumarin
-
endoplasmic reticulum lumen m-calpain, in 100 mM imidazole-HCl buffer (pH 7.5), 5 mM L-cysteine, 2.5 mM 2-mercaptoethanol, 5 mM CaCl2, and 4% (v/v) dimethyl sulfoxide, at 30°C
2.1
succinyl-Leu-Tyr-7-amido-4-methylcoumarin
-
endoplasmic reticulum lumen m-calpain, in 100 mM imidazole-HCl buffer (pH 7.5), 5 mM L-cysteine, 2.5 mM 2-mercaptoethanol, 5 mM CaCl2, and 4% (v/v) dimethyl sulfoxide, at 30°C
2.13
succinyl-Leu-Tyr-7-amido-4-methylcoumarin
-
endoplasmic reticulum membrane m-calpain, in 100 mM imidazole-HCl buffer (pH 7.5), 5 mM L-cysteine, 2.5 mM 2-mercaptoethanol, 5 mM CaCl2, and 4% (v/v) dimethyl sulfoxide, at 30°C
8.11
t-butyloxycarbonyl-Val-Leu-Lys-7-amido-4-methylcoumarin
-
endoplasmic reticulum membrane m-calpain, in 100 mM imidazole-HCl buffer (pH 7.5), 5 mM L-cysteine, 2.5 mM 2-mercaptoethanol, 5 mM CaCl2, and 4% (v/v) dimethyl sulfoxide, at 30°C
8.12
t-butyloxycarbonyl-Val-Leu-Lys-7-amido-4-methylcoumarin
-
endoplasmic reticulum lumen m-calpain, in 100 mM imidazole-HCl buffer (pH 7.5), 5 mM L-cysteine, 2.5 mM 2-mercaptoethanol, 5 mM CaCl2, and 4% (v/v) dimethyl sulfoxide, at 30°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.062
succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin
-
endoplasmic reticulum lumen m-calpain, in 100 mM imidazole-HCl buffer (pH 7.5), 5 mM L-cysteine, 2.5 mM 2-mercaptoethanol, 5 mM CaCl2, and 4% (v/v) dimethyl sulfoxide, at 30°C
0.063
succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin
-
endoplasmic reticulum membrane m-calpain, in 100 mM imidazole-HCl buffer (pH 7.5), 5 mM L-cysteine, 2.5 mM 2-mercaptoethanol, 5 mM CaCl2, and 4% (v/v) dimethyl sulfoxide, at 30°C
0.186
succinyl-Leu-Met-7-amido-4-methylcoumarin
-
endoplasmic reticulum membrane m-calpain, in 100 mM imidazole-HCl buffer (pH 7.5), 5 mM L-cysteine, 2.5 mM 2-mercaptoethanol, 5 mM CaCl2, and 4% (v/v) dimethyl sulfoxide, at 30°C
0.189
succinyl-Leu-Met-7-amido-4-methylcoumarin
-
endoplasmic reticulum lumen m-calpain, in 100 mM imidazole-HCl buffer (pH 7.5), 5 mM L-cysteine, 2.5 mM 2-mercaptoethanol, 5 mM CaCl2, and 4% (v/v) dimethyl sulfoxide, at 30°C
0.083
succinyl-Leu-Tyr-7-amido-4-methylcoumarin
-
endoplasmic reticulum lumen m-calpain, in 100 mM imidazole-HCl buffer (pH 7.5), 5 mM L-cysteine, 2.5 mM 2-mercaptoethanol, 5 mM CaCl2, and 4% (v/v) dimethyl sulfoxide, at 30°C
0.084
succinyl-Leu-Tyr-7-amido-4-methylcoumarin
-
endoplasmic reticulum membrane m-calpain, in 100 mM imidazole-HCl buffer (pH 7.5), 5 mM L-cysteine, 2.5 mM 2-mercaptoethanol, 5 mM CaCl2, and 4% (v/v) dimethyl sulfoxide, at 30°C
1.06
t-butyloxycarbonyl-Val-Leu-Lys-7-amido-4-methylcoumarin
-
endoplasmic reticulum membrane m-calpain, in 100 mM imidazole-HCl buffer (pH 7.5), 5 mM L-cysteine, 2.5 mM 2-mercaptoethanol, 5 mM CaCl2, and 4% (v/v) dimethyl sulfoxide, at 30°C
1.08
t-butyloxycarbonyl-Val-Leu-Lys-7-amido-4-methylcoumarin
-
endoplasmic reticulum lumen m-calpain, in 100 mM imidazole-HCl buffer (pH 7.5), 5 mM L-cysteine, 2.5 mM 2-mercaptoethanol, 5 mM CaCl2, and 4% (v/v) dimethyl sulfoxide, at 30°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.135
succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin
-
endoplasmic reticulum lumen m-calpain, in 100 mM imidazole-HCl buffer (pH 7.5), 5 mM L-cysteine, 2.5 mM 2-mercaptoethanol, 5 mM CaCl2, and 4% (v/v) dimethyl sulfoxide, at 30°C
0.137
succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin
-
endoplasmic reticulum membrane m-calpain, in 100 mM imidazole-HCl buffer (pH 7.5), 5 mM L-cysteine, 2.5 mM 2-mercaptoethanol, 5 mM CaCl2, and 4% (v/v) dimethyl sulfoxide, at 30°C
0.0399
succinyl-Leu-Met-7-amido-4-methylcoumarin
-
endoplasmic reticulum membrane m-calpain, in 100 mM imidazole-HCl buffer (pH 7.5), 5 mM L-cysteine, 2.5 mM 2-mercaptoethanol, 5 mM CaCl2, and 4% (v/v) dimethyl sulfoxide, at 30°C
0.0404
succinyl-Leu-Met-7-amido-4-methylcoumarin
-
endoplasmic reticulum lumen m-calpain, in 100 mM imidazole-HCl buffer (pH 7.5), 5 mM L-cysteine, 2.5 mM 2-mercaptoethanol, 5 mM CaCl2, and 4% (v/v) dimethyl sulfoxide, at 30°C
0.0394
succinyl-Leu-Tyr-7-amido-4-methylcoumarin
-
endoplasmic reticulum membrane m-calpain, in 100 mM imidazole-HCl buffer (pH 7.5), 5 mM L-cysteine, 2.5 mM 2-mercaptoethanol, 5 mM CaCl2, and 4% (v/v) dimethyl sulfoxide, at 30°C
0.0395
succinyl-Leu-Tyr-7-amido-4-methylcoumarin
-
endoplasmic reticulum lumen m-calpain, in 100 mM imidazole-HCl buffer (pH 7.5), 5 mM L-cysteine, 2.5 mM 2-mercaptoethanol, 5 mM CaCl2, and 4% (v/v) dimethyl sulfoxide, at 30°C
0.131
t-butyloxycarbonyl-Val-Leu-Lys-7-amido-4-methylcoumarin
-
endoplasmic reticulum membrane m-calpain, in 100 mM imidazole-HCl buffer (pH 7.5), 5 mM L-cysteine, 2.5 mM 2-mercaptoethanol, 5 mM CaCl2, and 4% (v/v) dimethyl sulfoxide, at 30°C
0.133
t-butyloxycarbonyl-Val-Leu-Lys-7-amido-4-methylcoumarin
-
endoplasmic reticulum lumen m-calpain, in 100 mM imidazole-HCl buffer (pH 7.5), 5 mM L-cysteine, 2.5 mM 2-mercaptoethanol, 5 mM CaCl2, and 4% (v/v) dimethyl sulfoxide, at 30°C
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0898
Ac-Thr-Pro-Leu-alpha-azaglycine-Ser-Pro-Pro-NH2
-
in 10 mM HEPES, 150 mM NaCl, 1 mM EDTA, pH 7.5, at 22°C
0.0087
Ac-Thr-Pro-Leu-alpha-azaglycine-Ser-Pro-Pro-Pro-Ser-NH2
-
in 10 mM HEPES, 150 mM NaCl, 1 mM EDTA, pH 7.5, at 22°C
0.0072
Ac-Thr-Pro-Leu-alpha-azaglycine-Ser-Pro-Pro-Pro-Ser-Pro-Arg-NH2
-
in 10 mM HEPES, 150 mM NaCl, 1 mM EDTA, pH 7.5, at 22°C
0.0035
Ac-Thr-Ser-Leu-alpha-azaglycine-Ser-Pro-Pro-Pro-Ser-NH2
-
in 10 mM HEPES, 150 mM NaCl, 1 mM EDTA, pH 7.5, at 22°C
0.0058
Ac-Thr-Trp-Leu-alpha-azaglycine-Ser-Pro-Pro-Pro-Ser-NH2
-
in 10 mM HEPES, 150 mM NaCl, 1 mM EDTA, pH 7.5, at 22°C
0.00206
antipain
-
room temperature, pH 7.5, with succinyl-Met-Leu-methylcoumarin as substrate
0.000286
Cbz-Leu-DL-Abu-CONH-(CH2)3-(4-methylpiperazin-1-yl)
-
in 50 mM Tris-HCl, 50 mM NaCl, 1 mM EDTA, 1 mM EGTA, 0.1% CHAPS, pH 7.5, 10 mM dithiothreitol, 5 mM CaCl2, and less than 5% (v/v) DMSO, temperature not specified in the publication
0.000077
Cbz-Leu-DL-Abu-CONH-(CH2)3-2-methoxyadenin-9-yl
-
in 50 mM Tris-HCl, 50 mM NaCl, 1 mM EDTA, 1 mM EGTA, 0.1% CHAPS, pH 7.5, 10 mM dithiothreitol, 5 mM CaCl2, and less than 5% (v/v) DMSO, temperature not specified in the publication
0.00007
Cbz-Leu-DL-Abu-CONH-(CH2)3-adenin-9-yl
-
in 50 mM Tris-HCl, 50 mM NaCl, 1 mM EDTA, 1 mM EGTA, 0.1% CHAPS, pH 7.5, 10 mM dithiothreitol, 5 mM CaCl2, and less than 5% (v/v) DMSO, temperature not specified in the publication
0.00114
Cbz-Leu-DL-Abu-CONH-(CH2)3-cytosin-3-yl
-
in 50 mM Tris-HCl, 50 mM NaCl, 1 mM EDTA, 1 mM EGTA, 0.1% CHAPS, pH 7.5, 10 mM dithiothreitol, 5 mM CaCl2, and less than 5% (v/v) DMSO, temperature not specified in the publication
0.000041
Cbz-Leu-DL-Abu-CONH-(CH2)3-morpholine
-
in 50 mM Tris-HCl, 50 mM NaCl, 1 mM EDTA, 1 mM EGTA, 0.1% CHAPS, pH 7.5, 10 mM dithiothreitol, 5 mM CaCl2, and less than 5% (v/v) DMSO, temperature not specified in the publication
0.00352
CBZ-Leu-DL-Phe-CONH-(CH2)2-N-(CH3)2
-
in 50 mM Tris-HCl, 50 mM NaCl, 1 mM EDTA, 1 mM EGTA, 0.1% CHAPS, pH 7.5, 10 mM dithiothreitol, 5 mM CaCl2, and less than 5% (v/v) DMSO, temperature not specified in the publication
0.00636
CBZ-Leu-DL-Phe-CONH-(CH2)3-(4-methylpiperazin-1-yl)
-
in 50 mM Tris-HCl, 50 mM NaCl, 1 mM EDTA, 1 mM EGTA, 0.1% CHAPS, pH 7.5, 10 mM dithiothreitol, 5 mM CaCl2, and less than 5% (v/v) DMSO, temperature not specified in the publication
0.000209
CBZ-Leu-DL-Phe-CONH-(CH2)3-2-methoxyadenin-9-yl
-
in 50 mM Tris-HCl, 50 mM NaCl, 1 mM EDTA, 1 mM EGTA, 0.1% CHAPS, pH 7.5, 10 mM dithiothreitol, 5 mM CaCl2, and less than 5% (v/v) DMSO, temperature not specified in the publication
0.000068
CBZ-Leu-DL-Phe-CONH-(CH2)3-adenin-9-yl
-
in 50 mM Tris-HCl, 50 mM NaCl, 1 mM EDTA, 1 mM EGTA, 0.1% CHAPS, pH 7.5, 10 mM dithiothreitol, 5 mM CaCl2, and less than 5% (v/v) DMSO, temperature not specified in the publication
0.000438
CBZ-Leu-DL-Phe-CONH-(CH2)3-cytosin-3-yl
-
in 50 mM Tris-HCl, 50 mM NaCl, 1 mM EDTA, 1 mM EGTA, 0.1% CHAPS, pH 7.5, 10 mM dithiothreitol, 5 mM CaCl2, and less than 5% (v/v) DMSO, temperature not specified in the publication
0.000844
CBZ-Leu-DL-Phe-CONH-(CH2)3-N-(CH3)2
-
in 50 mM Tris-HCl, 50 mM NaCl, 1 mM EDTA, 1 mM EGTA, 0.1% CHAPS, pH 7.5, 10 mM dithiothreitol, 5 mM CaCl2, and less than 5% (v/v) DMSO, temperature not specified in the publication
0.00092
leupeptin
-
room temperature, pH 7.5, with succinyl-Met-Leu-methylcoumarin as substrate
0.0203
Thr-Pro-Leu-alpha-azaglycine-Ser-Pro-Pro-Pro-Ser-Pro-Arg-NH2
-
in 10 mM HEPES, 150 mM NaCl, 1 mM EDTA, pH 7.5, at 22°C
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00014
(2S)-3-phenyl-2-([[(2S)-1-(phenylsulfonyl)pyrrolidin-2-yl]carbonyl]amino)propanoic acid
Rattus norvegicus
-
temperature not specified in the publication, in 20 mM Tris-HCl, pH 7.4
0.00041
(2S)-4-methyl-2-[(phenylsulfonyl)amino]pentanoic acid
Rattus norvegicus
-
temperature not specified in the publication, in 20 mM Tris-HCl, pH 7.4
0.00000052
110 kDa calpastatin
Bos taurus
-
in 100 mM imidazole-HCl buffer (pH 7.5),5 mM cysteine and 5 mM CaCl2, at 30°C
-
0.0000008
70 kDa calpastatin
Bos taurus
-
in 100 mM imidazole-HCl buffer (pH 7.5),5 mM cysteine and 5 mM CaCl2, at 30°C
-
0.00024
ethyl N-(phenylsulfonyl)-L-leucyl-L-phenylalaninate
Rattus norvegicus
-
temperature not specified in the publication, in 20 mM Tris-HCl, pH 7.4
0.00015
MDL28170
Rattus norvegicus
-
temperature not specified in the publication, in 20 mM Tris-HCl, pH 7.4
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
endoplasmic reticulum membrane m-calpain shows 170 units/mg specific activity after 323fold purification, endoplasmic reticulum lumen m-calpain shows 324 units/mg specific activity after 463fold purification one unit is defined as the amount of the enzyme that causes a change of 1.0 in A750 for the trichloroacetic acid-soluble products after incubation of the enzyme in the assay mixture
additional information
initial activity as relative fluorescence units per s: 1.3 for wild type calpain 2, 0.84 for mutant G423R, 0.19 for mutant R628Q, 0.36 for mutant T344M, 0.7 for mutant D346E, 1.0 for mutant D362K
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.9
7.5
7.5 - 8
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 8.5
-
pH 5.0: about 50% of maximal activity, pH 8.5: about 30% of maximal activity
6 - 8
-
pH 6.0: about 40% of maximal activity, pH 8.0: about 50% of maximal activity, enzyme from retina and brain
6 - 8.5
-
pH 6.0: about 50% of maximal activity, pH 8.5: about 60% of maximal activity
6.5 - 8.5
-
pH 6.5: about 50% of maximal activity, pH 8.5: about 40% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
30
37
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10 - 40
-
10°C: about 60% of maximal activity, 40°C: about 45% of maximal activity
10 - 45
-
10°C: about 60% of maximal activity, 45°C: about 35% of maximal activity
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
brenda
-
644029, 644051, 667136, 667778, 681694, 684326, 686159, 686630, 687441, 687611, 687908, 688909, 688945
-
-
brenda
-
707044, 707365, 707902, 707980, 708151, 708416, 709126, 709329, 709540, 709641, 709652, 718169, 718262, 731892
-
-
brenda
-
-
-
brenda
calpain-2 catalytic subunit
SwissProt
brenda
-
644049, 665705, 667378, 668497, 668509, 670249, 687156, 695462, 697162, 707385, 708018, 708140, 708389, 709031, 717669, 732050, 732688
-
-
brenda
calpain-2 catalytic subunit
SwissProt
brenda
homozygous disruption of the Capn2 gene (encoding the catalytic subunit of m-calpain) results in preimplantation embryonic lethality between the morula and blastocyst stage
SwissProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
calpain 2 is important for both the formation of invadopodia and invasive capacity of breast cancer cells
brenda
cell line DLD-1. In KRASWT/- cells serum starvation induces CAPN2 expression, nucleolar accumulation
brenda
-
nCL-2 is localized strictly to the surface cells in the gastric epithelium and the mucus-secreting goblet cells in the duodenum
brenda
-
analysis from E8.5 to 14.5 stages indicates high levels of capn2 expression in the nervous system, heart and mesodermal tissues. Up-regulation is maintained during later developmental stages in proliferating cells and in precursor cells involved in muscle (myoblasts) or bone formation (chondrocytes). At later developmental stages, elevated mRNA levels coincide with CAPN2 nuclear localization in these cell types, while differentiated cells maintain cytoplasmic expression
brenda
-
pulmonary microvascular endothelial cell. Incubation of the cells with vascular endothelial growth factor results in dose- and time-dependent increases in calpain activity and protein content of calpain-2. Vascular endothelial growth factor does not change the protein contents of calpain-1 and the small subunit or of calpastatin. Inhibition of calpain activity by siRNA directed against calpain-2 and by overexpression of calpastatin prevents vascular endothelial growth factor-induced increases in actin stress fibers in endothelial cells and angiogenesis
brenda
-
calpain 2 is first expressed late in embryonic development and localizes to the lens epithelium and transition zone
brenda
-
nCL-2 is localized strictly to the surface cells in the gastric epithelium and the mucus-secreting goblet cells in the duodenum
brenda
-
calpain 2 localizes to GM-3-rich lipid rafts at the leading edge
brenda
-
prefominantly localized in the growing hyphal and rhizoidal apices
brenda
-
membrane abnormalities and altered signaling pathways observed in Duchenne muscular dystrophy lymphocytes may be due to the increased association of calpain II onto membrane and cytosol
brenda
the large catalytic subunits of calpains 2 and the small regulatory subunit common to calpains 1 and 2 are weakly expressed in the parotid gland, sublingual gland, and submandibular gland at similar levels in males and females
brenda
-
calpain 2 activity is critical for the life cycle of echovirus 1 and important in the multiplication of the viral RNA genome
brenda
the large catalytic subunits of calpains 2 and the small regulatory subunit common to calpains 1 and 2 are weakly expressed in the parotid gland, sublingual gland, and submandibular gland at similar levels in males and females
brenda
-
active calpain 2 is concentrated in the trailing edge of the migrating T cell
brenda
isoform-specific hyperactivation of calpain-2, but not calpain-1 occurs at the synapse early in the pathogenesis of Alzheimer's disease potentially contributing to the deregulation of synaptic signaling in Alzheimer's disease
brenda
-
longissimus dorsi lumbar, longissimus dorsi thoracic, psoas major, semimembraneous triceps brachii. Activity of m-calpain decreases more slowly in the triceps brachii muscle than in the other 4 muscvles during postmortem storage
brenda
-
m-calpain localizes to phosphoinositide lipids in membranes in contact with the extracellular matrix. m-Calpain accumulates towards the rear membrane of a moving cell in an epidermal growth factor-dependent manner. Its activation is absent from forming lamellipodia
brenda
-
highest activity in plexiform layers and in the photoreceptor outer segments. In dark-adapted retinas the label is distributed throughout the outer segments. In light-adapted retinas, outer segment labelling is concentrated in the connecting cilium and the inner segments are labeled
brenda
-
calpains 2 is involved in atrophy development in slow type muscle. Calpains 2 is autolyzed in the early stage of skeletal muscle atrophy. This autolysis is specific to the soluble fraction for calpain 2. Calpain 2 autolysis is associated with an increased amount of calpain 2 content. Calpain autolysis is only seen in the slow soleus muscle, while the fast plantaris muscle is not affected
brenda
the large catalytic subunits of calpains 2 and the small regulatory subunit common to calpains 1 and 2 are weakly expressed in the parotid gland, sublingual gland, and submandibular gland at similar levels in males and females
brenda
-
physiological shear stress elicits Ca2+ influx-sensitive activation of m-calain in umbilical vein endothelial cells
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
in KRASWT/- cells serum starvation induces CAPN2 expression, nucleolar accumulation
brenda
-
in caveolae vesicles isolated from bovine pulmonary artery smooth muscle plasma membrane
brenda
-
from ES cells and the 8-cell stage to late neurulation stages, CAPN2 is expressed in the cytoplasm and nuclear compartments
brenda
-
membrane abnormalities and altered signaling pathways observed in Duchenne muscular dystrophy lymphocytes may be due to the increased association of calpain II onto membrane and cytosol
brenda
-
the 80000 Da catalytic subunit and the 28000 Da regulatory subunit of m-calpain are localized at the cytolsolic side of the ER membrane
brenda
-
membrane abnormalities and altered signaling pathways observed in Duchenne muscular dystrophy lymphocytes may be due to the increased association of calpain II onto membrane and cytosol
brenda
-
in isolated rat hearts, ischemia induces a time-dependent translocation of m-calpain to the membrane that is not associated with calpain activation
brenda
-
m-calpain is present in the intermembrane space of the mitochondria
brenda
-
from ES cells and the 8-cell stage to late neurulation stages, CAPN2 is expressed in the cytoplasm and nuclear compartments, with a clear co-localisation with chromatin. Nuclear localization was associated either with active cell mitosis in embryonic stem cells and early developmental stages or with precursor cells later during organogenesis
brenda
angiotensin II increases nuclear translocation of intracellular Ca2þ activated calpain-2 in hypertrophied cardiomyocytes
brenda
-
m-calpain localizes to phosphoinositide lipids in membranes in contact with the extracellular matrix. m-Calpain accumulates towards the rear membrane of a moving cell in an epidermal growth factor-dependent manner. Its activation is absent from forming lamellipodia
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug target
malfunction
metabolism
physiological function
drug target
calpain-2 is a potential therapeutic target in various forms of neurodegeneration, including traumatic brain injury and repeated concussions
drug target
calpain-2 is a anti-metastasis target. Targeted downregulation or pharmacological inhibition of calpain-2 restors talin-1 integrity, beta1 integrin engagement and reverts amoeboid to elongated phenotypes under hypoxia. Attenuation of calpain activity prevents hypoxia-induced metastasis to the lungs
drug target
inhibiting the expression or activity of calpain-2 protein may suppress chikungunya virus replication and repress the intracellular vimentin rearrangement caused by chikungunya virus infection
drug target
calpain-2 might be an important target with therapeutic potential for the design of inhibitors of the LIMK1/CFL1 signaling pathway in breast cancer
drug target
calpain-2 is a a potential therapeutic target responsible for SARS-CoV-2 infection at the entry step
drug target
calpain-2 is a anti-metastasis target. Targeted downregulation or pharmacological inhibition of calpain-2 restors talin-1 integrity, beta1 integrin engagement and reverts amoeboid to elongated phenotypes under hypoxia. Attenuation of calpain activity prevents hypoxia-induced metastasis to the lungs
malfunction
-
calpain inhibition blocks the increased colonic epithelial cell invasion caused by NM IIA knockdown
malfunction
-
in vivo knockdown of calpain2 disrupts metastasis among apoptosis-resistant tumors
malfunction
-
short interfering RNA-induced silencing of m-calpain results in increased RhoA activity and hyperpermeability in the aortic arch, which is accompanied by ROCK inhibitor-sensitive phosphorylation of downstream effecter LIM kinase 2, stress fibre accumulation in endothelium and enhanced interendothelial gaps
malfunction
-
inhibition of m-calpain induces expression of the adult alpha- and beta-globin genes
malfunction
-
the blockage of calpain 2 suppresses p38 MAPK phosphorylation
malfunction
-
calpain 2 depletion impairs mitosis and induces apoptosis, low Capn2 levels induce chromosome alignment defects, the loss of histone H3 threonine 3 phosphorylation at centromeres, and premature sister chromatid separation
malfunction
-
knockdown of calpain 2 inhibits T cell migration at both the level of single cell tracking and general cell speed
malfunction
-
inhibition of calpain activity limits cell migration and in vitro wound healing of IEC-6 cells
malfunction
-
knockdown of calpain 2 expression or chemical inhibition of calpain activity reduces glioblastoma cell invasion by 90%. Decreased expression of calpain 2 does not influence morphology or migration
malfunction
-
the knockdown of calpain 2 significantly reduces cord formation, adhesion, and migration of human lymphatic microvascular dermal-derived endothelial cells on Matrigel compared to the control
malfunction
-
calpain inhibition favors differentiation of neuronal stem cells. Calpain 2 silencing elicits decreased levels of glial fibrillary acidic protein
malfunction
-
calpain 2 knockdown in breast cancer cells correlates with reduced in vitro proliferation, migration, and in vivo tumorigenicity as well as reduced Akt activation, increased nuclear FoxO localization, and increased p27Kip1 expression
malfunction
-
knockdown of calpain 2 results in a 2.9fold decrease in the invasion of human glioblastoma cells in zebrafish brain. Calpain 2 knockdown cells demonstrate a 2.3fold lower area of dispersal compared with control cells
malfunction
-
the absence of the enzyme reduces viral binding to host cells and RNA production during early steps of the SARS-CoV-2 replication cycle
metabolism
-
calpain 2 regulates endothelial nitric oxide synthase phosphorylation during cord formation by lymphatic endothelial cells on Matrigel
metabolism
isoform-specific hyperactivation of calpain-2, but not calpain-1 occurs at the synapse early in the pathogenesis of Alzheimer's disease potentially contributing to the deregulation of synaptic signaling in Alzheimer's disease
metabolism
MARCKS protein i.e. myristoylated alanine-rich C kinase substrate is a substrate of calpain-2 in the presence of Ca2+. Calpain-2 proteolysis of MARCKS promotes its interaction with lipids and ENaC at the plasma membrane to allow for the phosphatidylinositol 4,5-bisphosphate (PIP2)-dependent regulation of epithelial sodium channel (ENaC) activity in the kidney
metabolism
nuclear translocation of calpain-2 mediates apoptosis of hypertrophied cardiomyocytes in transverse aortic constriction rat. Angiotensin II enhances the interaction between activated calpain-2 and Ca2+/calmodulin-dependent protein kinase II deltaB (CaMKIIdB), and promotes the degradation of CaMKIIdB by calpain-2 in the nuclei of hypertrophied cardiomyocytes. The depressed CaMKIIdeltaB downregulates the expression of antiapoptotic Bcl-2 leading to mitochondrial depolarization and release of cytochrome c which leads to apoptosis of hypertrophied cardiomyocytes
metabolism
the enzyme plays a role on mitotic activation of LIM kinase 1 and subsequent phosphorylation of its substrate cofilin-1
physiological function
-
m-calpain translocates during ischemia and activates at reperfusion in isolated rat hearts
physiological function
-
mitochondrial m-calpain is associated with ERp75 and plays an important role in releasing of truncated apoptosis-inducing factor from mitochondria
physiological function
-
an endoplasmic reticulum stress-related calpain-down-regulated PPAR-gamma/HO-1 pathway is involved in the interleukin-13-enhanced activated death of microglia
physiological function
-
mitochondrial m-calpain plays a role in the release of truncated apoptosis-inducing factor from the mitochondria by cleaving voltage-dependent anion channel
physiological function
-
calpain-2 is crucial for promotion of migration and metastasis by caspase-8
physiological function
-
m-calpain antagonizes RhoA overactivation and endothelial barrier dysfunction under disturbed shear conditions
physiological function
-
Ca2+ overload induces apoptosis, which was correlated with calpain-2 activation
physiological function
-
calpain 2-mediated proteolysis of focal adhesion kinase regulates adhesion dynamics in motile cells
physiological function
-
calpain 2 plays a role in the generation of the low molecular weight-androgen receptor in CWR22-R1 cells
physiological function
-
calpain 2 activation is an early event in heat stress-induced male germ cell apoptosis
physiological function
-
calpain 2 proteolysis of mAbp1 negatively regulates dorsal ruffle formation
physiological function
-
m-calpain up-regulates alpha- and beta-actin in alveolar rhabdomyosarcoma cells
physiological function
-
calpain 2 controls turnover of lymphocyte function-associated antigen-1 adhesions on migrating T lymphocytes
physiological function
-
the Ca2+-dependent release of m-calpain from the mitochondrial outer membrane has important implications in facilitating apoptotic cell death
physiological function
-
calpain 2 is required for matrix metalloproteinase-2 activity in glioblastoma cells. Calpain 2 is required for glioblastoma cell invasion, but not migration
physiological function
-
calpain-2 is a mediator of beta cell dysfunction and apoptosis in type 2 diabetes
physiological function
-
calpain 2 promotes proliferation of cancer cells through Akt-FoxO-p27Kip1 signaling
physiological function
-
calpain 2 is required for the invasion of glioblastoma cells in the living zebrafish brain microenvironment
physiological function
calpain-1 and calpain-2 play opposite functions in both synaptic plasticity/learning and memory and neuroprotection/neurodegeneration. Calpain-1 activation is necessary for certain forms of synaptic plasticity and learning and memory, while calpain-2 activation during a brief consolidation period limits the extent of plasticity/learning. Calpain-1 is neuroprotective, while calpain-2 is neurodegenerative. Calpain-2 activation, through the selective degradation of phosphatase PTEN, is linked to the regulation of mTOR-mediated local protein synthesis
physiological function
calpain-1 and calpain-2 play opposite roles in retinal ganglion cell death induced by acute intraocular pressure elevation. Calpain-1 activity supports survival of retinal ganglion cell after intraocular pressure elevation. Calpain-2 activity promotes cell death of retinal ganglion cells after intraocular pressure elevation. Calpain-2 activation cleaves striatal-enriched protein tyrosine phosphatase and activates STEP-mediated pro-death pathway in retinal ganglion cells after intraocular pressure elevation
physiological function
nuclear localization of a novel calpain-2 mediated junctophilin-2 C-terminal cleavage peptide promotes cardiomyocyte remodeling
physiological function
calpain-2 is neurodegenerative. Critical role of calpain-2 in neuronal death
physiological function
hypoxia induces calpain-2 mediated amoeboid conversion by deactivating beta1 integrins, through enzymatic cleavage of the focal adhesion adaptor protein talin-1
physiological function
calpain-2 protein influences chikungunya virus replication and regulated vimentin rearrangement caused by chikungunya virus infection
physiological function
the enzyme plays a critical role in neuronal autophagy induced by inflammation. Calpain-2 plays a pivotal role in the inhibitory effects of propofol against TNF-alpha-induced autophagy in mouse hippocampal neurons
physiological function
cleavage and activation of LIM kinase 1 is a mechanism for calpain 2-mediated regulation of nuclear dynamics
physiological function
-
the enzyme limits the extent of synaptic plasticity in the brain and is neurodegenerative
physiological function
calpain-2 activity promotes the aberrant endoplasmic stress-related apoptosis of rat hepatocytes by activating caspase-12 in the endoplasmic reticulum
physiological function
calpain-2 is required for an early step of the SARS-CoV-2 replication cycle. It mediates SARS-CoV-2 entry via regulating ACE2 levels
physiological function
calpain-2 participates in the process of calpain-1 inactivation
physiological function
calpain-2 protein influences chikungunya virus replication and regulates vimentin rearrangement caused by chikungunya virus infection
physiological function
the enzyme plays a pivotal role in the inhibitory effects of propofol against tumor necrosis factor-alpha-induced autophagy in mouse hippocampal neurons
physiological function
-
calpain-2 facilitates severe acute respiratory syndrome coronavirus 2 spike protein-mediated cell attachment by positively regulating the cell surface levels of ACE2
physiological function
enzyme activity promotes the aberrant endoplasmic reticulum stress-related apoptosis of rat hepatocytes by activating caspase-12 in the endoplasmic reticulum. The enzyme activity is crucial for dithiothreitol-induced endoplasmic reticulum stress-related hepatocyte apoptosis by activating caspase-12 in vitro
physiological function
the enzyme functions as a down-regulation of calpain-1
physiological function
enzyme activation prevents autophagy and stimulates apoptosis
physiological function
-
the enzyme is a key regulator and anti-metastasis target of hypoxia-induced transition from collective to amoeboid dissemination of breast carcinoma cells. The enzyme activity is required for hypoxia-induced amoeboid conversion in the orthotopic mouse dermis. Enzyme activation dampens integrin activity and mediates hypoxia inducible factor-induced amoeboid conversion. The enzyme cleaves talin-1 to enable cell rounding and blebbing-amoeboid migration
physiological function
hypoxia induces calpain-2 mediated amoeboid conversion by deactivating beta1 integrins, through enzymatic cleavage of the focal adhesion adaptor protein talin-1
physiological function
-
the enzyme is a key regulator and anti-metastasis target of hypoxia-induced transition from collective to amoeboid dissemination of head and neck carcinoma cells. Enzyme activation dampens integrin activity and mediates hypoxia inducible factor-induced amoeboid conversion. The enzyme cleaves talin-1 to enable cell rounding and blebbing-amoeboid migration
Show AA Sequence and Transmembrane Helices (2100 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
110000
21000
28000
32000
-
1 * 80000 + 1 * 32000, only the 80000 Da subunit shows catalytic ativity, SDS-PAGE
58000
8000
-
1 * 8000 + 1 * 28000, gel filtration, the endoplasmic reticulum membrane m-calpain containing 80000 Da large and 28000 Da small subunit is non-phosphorylated
80000
28000
-
1 * 8000 + 1 * 28000, gel filtration, the endoplasmic reticulum membrane m-calpain containing 80000 Da large and 28000 Da small subunit is non-phosphorylated
80000
-
1 * 80000 + 1 * 32000, only the 80000 Da subunit shows catalytic ativity, SDS-PAGE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
heterodimer
dimer
-
1 * 80000 + 1 * 32000, only the 80000 Da subunit shows catalytic ativity, SDS-PAGE
heterodimer
-
1 * 8000 + 1 * 28000, gel filtration, the endoplasmic reticulum membrane m-calpain containing 80000 Da large and 28000 Da small subunit is non-phosphorylated
heterodimer
-
1 * 75000 + 1 * ?, SDS-PAGE. The heterodimer is comprised of a large about 75 kDa catalytic subunit (CAPN2), and a common small regulatory subunit CAPNS1, also known as calpain 4
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
side-chain modification
-
calpain-2 is small ubiquitin-like modifier-modified at lysine residue 390, sumoylation is important for calpain-2 activity
additional information
-
the enzyme is neither glycosylated nor phosphorylated
phosphoprotein
-
the endoplasmic reticulum lumen m-calpain containing only 80000 Da large subunit is phosphorylated
phosphoprotein
-
brain-derived neurotrophic factor stimulates m-calpain serine phosphorylation
phosphoprotein
-
ERK activation directly phosphorylates and activates the enzyme
phosphoprotein
tumor necrosis factor-alpha induces the phosphorylation of the enzyme which is ameliorated by propofol
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
full-length human m-calpain containing an N-terminal Gly-Arg-Arg-Asp-Arg-Ser L-chain elongation overexpressed in a baculovirus expression system. Crystals grown by vapor diffusion. The 2.3 A crystal structure of full length heterodimeric m-calpain crystallized in the absence of calcium reveals an oval disc-like shape, with the papain-like catalytic domain dII and the two calmodulin, like domains dIV+dVI occupying opposite poles, and the tumor necrosis factor alpha-like beta-sandwich domain dIII and the N-terminal segments dI+dV located between
2.6 A crystal structure of m-calpain that has a C-terminal histidine-tag and a mutation of the active site C105S in the large subunit in the Ca2+-free form
calpastatin inhibitory domain 1 crystallized with calpain 2, calpastatin inhibitory domain 4 crystallized with calpain 2
-
crystallization of recombinant C105S mutant enzyme by hanging drop method
-
the refined crystal structure of the mutant enzymes K226S, K230E, K234S and E504S in absence of Ca2+ are indistinguishable from wilde-type calpain
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C105S
-
mutant enzyme of mutant large subunit m-C105S-80K, coexpressed with 30000 Da subunit in Sf-9 cells does not degrade casein nor the artificial substrate succinyl-Leu-Leu-Val-Tyr-4-methylcoumaryl-7-amide. The mutant enzyme does not show autolytic activity with Ca2+
K390R
-
overexpression of K390R mutant fails to increase the calpain activity since sumoylation at K390 is important for calpain-2 activity
C105S
D346E
mutant with decreased enzymatic activity, increased rate of autoproteolytic degradation
D362K
mutant with decreased enzymatic activity, increased rate of autoproteolytic degradation
E504S
G423R
mutant with decreased enzymatic activity, increased rate of autoproteolytic degradation
K225S
mutation decreases specific activity to 88% compared to wild-type enzyme
K226S
Ca2+ concentration required for half-maximal activity is 0.226 mM compared to 0.242 mM for the wild-type enzyme. Refined structure of the mutant enzyme in absence of Ca2+ is indistinguishable from wild-type enzyme
K230E
K230S
K234E
mutation decreases the specific activity of the enzyme to 16% compared with the wild-type enzyme
K234S
K234W
Ca2+ concentration required for half-maximal activity is 0.159 mM compared to 0.242 mM for the wild-type enzyme
R417W
mutant with decreased enzymatic activity, increased rate of autoproteolytic degradation
S50D
-
mutant enzyme has the same specific activity and Ca2+ requirement as the wild-type enzyme
S50E
-
mutant enzyme has the same specific activity and Ca2+ requirement as the wild-type enzyme
S67E
-
mutant enzyme has the same specific activity and Ca2+ requirement as the wild-type enzyme
T344M
mutant with decreased enzymatic activity, increased rate of autoproteolytic degradation
T70E
-
mutant enzyme has the same specific activity and Ca2+ requirement as the wild-type enzyme
additional information
C105S
-
inactive mutant enzyme. The mutant enzyme provides a purified calpain, that is stable to autolysis and oxidation, which is likely to facilitate crystallization in both the presence and absence of calcium
E504S
Ca2+ concentration required for half-maximal activity is 0.129 mM compared to 0.242 mM for the wild-type enzyme. Refined structure of the mutant enzyme in absence of Ca2+ is indistinguishable from wild-type enzyme
E504S
mutation decreases specific activity to 90% compared to wild-type enzyme
K230E
Ca2+ concentration required for half-maximal activity is 0.256 mM compared to 0.242 mM for the wild-type enzyme. Refined structure of the mutant enzyme in absence of Ca2+ is indistinguishable from wild-type enzyme
K230E
mutation decreases the specific activity of the enzyme to 16% compared with the wild-type enzyme
K230S
Ca2+ concentration required for half-maximal activity is 0.261 mM compared to 0.242 mM for the wild-type enzyme
K234S
Ca2+ concentration required for half-maximal activity is 0.183 mM compared to 0.242 mM for the wild-type enzyme. Refined structure of the mutant enzyme in absence of Ca2+ is indistinguishable from wild-type enzyme
K234S
mutation decreases specific activity to 81% compared to wild-type enzyme
additional information
used as a model for calpain 3 in combination with calpastatin-inhibited rat calpain 2
additional information
-
replacement of the five m-calpain residues 517-521, Glu-Ala-Asn-Ile-Glu by the corresponding six mu-calpain residues 528-533, Gln-Ala-Asn-Leu-Pro-Asp, replacement of three m-calpain residues 639-641, Pro-Cys-Gln, by the corresponding three mu-calpain residues 651-653, Asn-Lys-Lys, or replacement of two m-calpain residues 578-579, Lys-Ile by the corresponding mu-calpain residues 590-591, Arg-Ser. Mutations do not affect the expression and Kd values of the resultant calpains. In a series of hybrid mu/m large-subunit calpains, the Kd values decrease progressively towards that of mu-calpain as the portion of mu-type sequence increases from 0 to 90%
additional information
used as a model for calpain 3 in combination with calpastatin-inhibited rat calpain 2
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
60
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
bovine fetuin A stabilizes proteolytic activity of purified m-calpain incubated in the presence of mM calcium chloride and prevents calcium-dependent m-calpain aggregation
-
m-calpain loses 50-55% of its proteolytic activity within 5 min during incubation at pH 7.5 in 300 mM or high salt and at a slower rat in 100 mM salt. This loss of activity is not reversed by dialysis for 18 h against a low-ionic-strength buffer at pH 7.5. Proteolytic activity of the unautolyzed calpains is not affected by incubation for 45 min at ionic strength up to 1000 mM. Ionic strengths of 100 mM or above cause dissociation of the two subunits of autolyzed calpains. The dissociated large subunits aggregate to form dimers and trimers, which are proteolytically inactive
-
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
the pre-incubation of m-calpain with H2O2 results in a significant decrease of m-calpain activity under non-reducing condition. The addition of calcium lactate (5 mM) to the pre-incubation mixture of m-calpain with H2O2 (0.05 mM) results in a more extensive loss of m-calpain activity compared to the equal amount of CaCl2 addition to the pre-incubation mixture
-
717628
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, DEAE-cellulose column chromatography, phenyl-Sepharose column chromatography, DEAE-TSK column chromatography, and Reactive Red gel filtration
-
ammonium sulfate precipitation, DEAE-cellulose column chromatography, phenyl-Sepharose column chromatography, Reactive Red column chromatography, and DEAE-TSK anion exchange column chromatography
-
recombinant enzyme
single-step purification of calpain-1, calpain-2, and calpastatin using anion-exchange chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
a 629 bp fragment is cloned into the EcoRV site of pBluescript II KS+ vector
cDNA fragments corresponding to the domains with E-F hand structures in the large and small subunits are inserted into an expression vector pIC18 or pUC8. The resulting plasmids are used to transform Escherichia coli and isopropyl-1-thio-beta-D-galactoside-inducible expression is induced
coexpression from large-subunit and small-subunit plasmids in Escherichia coli strain BL21(DE3)
-
development of an adenoviral vector harboring calpain-2 siRNA expression unit in which sense and anti-sense strands composing the siRNA duplex are connected by a loop and transcribed into a siRNA in porcine pulmonary artery endothelial cells. The adenoviral vector harboring calpain-2 siRNA expression unit is a valuable tool to study the biology of calpains
-
expression of mutated calpain 2 C105A is driven in lens by coupling the mutated gene to the betaB1-crystallin promoter
-
functional analysis of the upstream region of the gene for the large subunit by means of transient expression assay on HeLa cells using chloramphenicol transferase constructs identifies four negative regulatory regions tandemly reiterated just upstream of the promoter region, P1 and P2
molecular cloning of the cDNA for the 80000 Da subunit and expression in Escherichia coli
the bacterial production of recombinant rat calpain II is improved greatly by the use of two compatible plasmids for the two subunits. The calpain small subunit C-terminal fragment is expressed from a new A15-based vector created by cloning T7 contol elements into pACYC177. This vector is compatible with the ColE1-based pET-24d(+) vector containing the calpain large subunit and the yield of calpain activity is increased at least 16fold by coexpression from theses two vectors. A high level of activity is also obtained from a bicistronic construct containing the subunit cDNAs under the control of one T7 promoter
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
0.1 mM indomethacin and 0.1 mM NS-398 decrease expression of calpain 2 in total membrane fractions and in plasma membranes by 70%, while 0.001 mM SC-560 decreases expression of calpain 2 in total membrane fractions and in plasma membranes by 30%
-
a 6-day treatment with siRNA results in an about 60% reduction of calpain 2 protein levels in R1 cells
-
a heat stress stimulus induces massive germ cells apoptosis, which is associated with an increase in the levels of mRNA encoding calpain 2
-
brain-derived neurotrophic factor and epidermal growth factor activate neuronal m-calpain via mitogen-activated protein kinase-dependent phosphorylation
-
calpain activation occurs during reperfusion, but only after intracellular pH normalization, and is not prevented by inhibiting its translocation during ischemia with methyl-beta-cyclodextrin
-
calpain-2 is upregulated in invasive head and neck tumor xenografts in vivo
endoplasmic reticulum stress stimulates calpain II activation, interleukin-13 enhances endoplasmic reticulum stress-regulated calpain activation and calpain-II expression in lipopolysaccaride-activated microglia
-
incubation of human retinal microvascular endothelial cells with vascular endothelial growth factor results in 1.6fold increased activity of calpain 2 at 24 h
-
m-calpain activation occurs during reperfusion, but only after intracellular pH normalization, and is not prevented by inhibiting its translocation during ischemia with methyl-beta-cyclodextrin
-
m-calpain expression levels in aorta in siRNAtreated mice are significantly diminished by 63.5% in comparison to those in control RNA-transfected mice with no alteration of m-calpain or beta-actin expression
-
microRNA MiR-145 overexpression decreases CAPN2 expression. The effect is indirect. MiR-145 targets histone deacetylase (HDAC) 2, and HDAC inhibition transcriptionally regulates CAPN2 expression by hyperacetylation of the promoter of CAPN2 gene and a subsequent decrease in polymerase 2 binding
microRNA Mir-223 overexpression decreases CAPN2 protein levels in cultured cells. miR-223, acting directly on the 3'-untranslated region
microRNAs Mir-223 and MiR-145 overexpression decreases enzyme protein levels. Protein levels of the enzyme are regulated by miR-223, acting directly on the 3'-untranslated region as well as by miR-145,which acts via an increase in histone deacetylase 2
p38 MAPK and JNK are required to stimulate m-calpain activity when TRPM7 is overexpressed, TRPM7-mediated activation of m-calpain is not dependent on the nature of the divalent conducted by the channel
-
the enzyme is upregulated in invasive head and neck carcinoma tumor xenografts in vivo
-
the enzyme is upregulated in weakly adhesive cells after treatment with dimethyl oxalylglycine
-
calpain-2 is upregulated in invasive head and neck tumor xenografts in vivo
calpain-2 is upregulated in invasive head and neck tumor xenografts in vivo
microRNA MiR-145 overexpression decreases CAPN2 expression. The effect is indirect. MiR-145 targets histone deacetylase (HDAC) 2, and HDAC inhibition transcriptionally regulates CAPN2 expression by hyperacetylation of the promoter of CAPN2 gene and a subsequent decrease in polymerase 2 binding
microRNA MiR-145 overexpression decreases CAPN2 expression. The effect is indirect. MiR-145 targets histone deacetylase (HDAC) 2, and HDAC inhibition transcriptionally regulates CAPN2 expression by hyperacetylation of the promoter of CAPN2 gene and a subsequent decrease in polymerase 2 binding
microRNA Mir-223 overexpression decreases CAPN2 protein levels in cultured cells. miR-223, acting directly on the 3'-untranslated region
microRNA Mir-223 overexpression decreases CAPN2 protein levels in cultured cells. miR-223, acting directly on the 3'-untranslated region
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
medicine
-
m-calpain inhibition at the time of reperfusion is a potentially useful strategy to limit infarct size
medicine
-
m-calpain is a marker of tumor aggressiveness and is apotential target for limiting development of rhabdomyosarcoma tumor as well as their metastatic behavior
medicine
a selective calpain-2 inhibitor could prevent acute glaucoma-induced retinal ganglion cell death and blindness
medicine
-
the enzyme is a potential therapeutic target responsible for SARS-CoV-2 infection at the entry step
medicine
the enzyme is a potential therapeutic target in various forms of neurodegeneration, including traumatic brain injury and repeated concussions
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Release 2026.1 (March 2026)
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