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Information on EC 3.4.21.B7 - mannan-binding lectin-associated serine protease 1 and Organism(s) Homo sapiens
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3.4.21.B7 mannan-binding lectin-associated serine protease 1Specify your search results
Word Map
- 3.4.21.B7
- masp-3
-
silk
- spider
- ficolins
-
dragline
- c1s
-
ampullate
-
spidroins
-
convertase
-
collagen-like
- clavipes
-
collectins
- m-ficolin
-
autoactivation
- nephila
-
subcomponents
-
complement-activating
- c1-inhibitor
- latrodectus
-
pattern-recognition
- widow
-
fibrinogen-like
-
protease-2
-
opsonin
-
extensibility
-
urochord
-
c1-inh
- hesperus
- medicine
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
endopeptidase activity. It triggers the activation of complement cascade by activating the C4 and C2 components. It activates the C4 component by cleaving the alpha-chain of C4
Synonyms
masp-1, masp1, mbl-associated serine protease, mbl-masp, ra-reactive factor, mannose-binding lectin-associated serine protease, mannan-binding lectin-associated serine protease-1, mbl-associated serine protease-1, mannan-binding lectin-associated serine protease, mannan-binding lectin-associated serine protease 1, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
MASP-1
MBL-associated serine protease 1
P100
MASP-1
-
-
MASP-1
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
cleavage of C-N-linkage
hydrolysis of peptide bond
CAS REGISTRY NUMBER
COMMENTARY
214915-11-4
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
benzyloxycarbonyl-Val-Pro-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Val-Pro-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
complement component C3 + H2O
complement component C3a + complement component C3b
-
activates complement C3
-
?
complement-activating component of Ra-reactive factor + H2O
?
cleavage at Arg448-/-Ile449
-
-
?
factor XIII A-chain + H2O
?
catalytic activity for factor XIII and fibrinogen cleavage is much lower than that of thrombin
-
-
?
fibrinogen beta-chain + H2O
?
cleavage at R44-/-G45 and other sites
-
-
?
high-molecular weight kininogen + H2O
bradykinin + ?
a noncomplement substrate, activation
-
-
?
low-molecular-weight kininogen + H2O
?
-
the cleavage rate of low-molecular-weight kininogen by MASP-1 is about 5times lower than that of kininogen
-
-
?
MASP1 mannan-binding lectin serine protease 1 isoform 1 precursor + H2O
?
autodegradation pattern of the MASP-1 CCP1-CCP2-SP fragment. Cleavage occurs at the Arg504-Asp505 bond, which results in the removal of a 6000 Da fragment from the active enzyme. The autolysis of the MASP-1 CCP1-CCP2-SP fragment causes the loss of its enzymatic activity due to the removal of the histidine from the catalytic triad
-
-
?
proform mannan-binding lectin-associated serine protease 1 + H2O
mature mannan-binding lectin-associated serine protease 1 + ?
proform mannan-binding lectin-associated serine protease 2 + H2O
mature mannan-binding lectin-associated serine protease 2 + ?
proform mannan-binding lectin-associated serine protease 3 + H2O
mature mannan-binding lectin-associated serine protease 3 + ?
proform protease activated receptor 4 + H2O
mature protease activated receptor 4 + ?
activation
-
-
?
proform thrombin-activatable fibrinolysis inhibitor + H2O
mature thrombin-activatable fibrinolysis inhibitor + ?
complement component C2 + H2O
?
digested by the MASP-1 CCP1-CCP2-SP fragment at a moderate rate
-
-
?
complement component C3 + H2O
?
cleavage with appearance of the alpha-chain
-
-
?
complement component C3i + H2O
?
cleavage of intact C3i (C3 with a reacted thiolester bond) by the MASP-1 CCP1-CCP2-SP fragment with a low but significant efficiency
-
-
?
Fibrinogen + H2O
?
rMASP1 cleavage of fibrinogen leads to the release of the proinflammatory peptide fibrinopeptide B. Catalytic activity for factor XIII and fibrinogen cleavage is much lower than that of thrombin
-
-
?
fibrinogen + H2O
fibrin + ?
MASP-1-induced fibrin formation and activation is thrombin-dependent, in plasma environment fibrin formation is not directly induced by MASP-1 in the absence of prothrombin
-
-
?
proform coagulation factor XIII + H2O
mature coagulation factor XIII + ?
-
-
-
?
proform coagulation factor XIII + H2O
mature coagulation factor XIII + ?
a noncomplement substrate, activation
-
-
?
proform factor XIII + H2O
mature factor XIII + ?
the Val34 variant is a better substrate than the Leu34 variant
-
-
?
proform mannan-binding lectin-associated serine protease 1 + H2O
mature mannan-binding lectin-associated serine protease 1 + ?
autocatalytic cleavage, a complement substrate, activation
-
-
?
proform mannan-binding lectin-associated serine protease 1 + H2O
mature mannan-binding lectin-associated serine protease 1 + ?
-
autocatalytic cleavage, a complement substrate, activation
-
-
?
proform mannan-binding lectin-associated serine protease 1 + H2O
mature mannan-binding lectin-associated serine protease 1 + ?
autocatalytic cleavage
-
-
?
proform mannan-binding lectin-associated serine protease 2 + H2O
mature mannan-binding lectin-associated serine protease 2 + ?
-
-
-
?
proform mannan-binding lectin-associated serine protease 2 + H2O
mature mannan-binding lectin-associated serine protease 2 + ?
activation
-
-
?
proform mannan-binding lectin-associated serine protease 2 + H2O
mature mannan-binding lectin-associated serine protease 2 + ?
a complement substrate, activation
-
-
?
proform mannan-binding lectin-associated serine protease 2 + H2O
mature mannan-binding lectin-associated serine protease 2 + ?
-
a complement substrate, activation
-
-
?
proform mannan-binding lectin-associated serine protease 2 + H2O
mature mannan-binding lectin-associated serine protease 2 + ?
enzyme MASP-1 is the main activator of MASP-2
-
-
?
proform mannan-binding lectin-associated serine protease 3 + H2O
mature mannan-binding lectin-associated serine protease 3 + ?
-
-
-
?
proform mannan-binding lectin-associated serine protease 3 + H2O
mature mannan-binding lectin-associated serine protease 3 + ?
a complement substrate, activation
-
-
?
proform thrombin-activatable fibrinolysis inhibitor + H2O
mature thrombin-activatable fibrinolysis inhibitor + ?
-
-
-
?
proform thrombin-activatable fibrinolysis inhibitor + H2O
mature thrombin-activatable fibrinolysis inhibitor + ?
activation
-
-
?
protease activated receptor 4 + H2O
?
PAR4, a noncomplement substrate, activation
-
-
?
prothrombin + H2O
thrombin + ?
a noncomplement substrate, activation
-
-
?
prothrombin + H2O
thrombin a + ?
enzyme MASP-1 cleaves prothrombinat three cleavage sites, MASP-1 gives rise to an alternative active form of thrombin by cleaving at the cleavage site R393
-
-
?
prothrombin + H2O
thrombin a + ?
enzyme MASP-1 cleaves prothrombinant three cleavage sites
-
-
?
additional information
?
-
-
complexes with mannose-binding lectin in the presence of Ca2+, involved in activation of complement cascade
-
?
additional information
?
-
involved in activation of complement cascade
-
?
additional information
?
-
-
involved in activation of complement cascade
-
?
additional information
?
-
-
involved in activation of complement cascade, circulates in serum complexed with mannose-binding protein
-
?
additional information
?
-
-
involved in activation of complement cascade, forms a complex with mannose-binding lectin
-
?
additional information
?
-
-
involved in activation of complement cascade, smallest functional unit for complement activation consists of serum mannose-binding protein dimers bound to MASP-1 homodimers
-
?
additional information
?
-
-
no cleavage of complement C4 by purified MASP-1
-
-
?
additional information
?
-
-
MASP-1 shows no activity toward complement C4. MASP-1 collaborates with MASP-2 in the generation of C3 convertase, a process observable at high serum concentration, but not at low serum concentration
-
-
?
additional information
?
-
autoactivation by cleavage of R448-/-I449. The enzyme is relatively unspecific
-
-
?
additional information
?
-
complement component C4, similar to C3, is basically resistant to the proteolytic activity of MASP-1. MASP-1 shows extreme Arg selectivity
-
-
?
additional information
?
-
-
MBL-MASP complexes, bound to mannan-agarose, generate clots when incubated with calcified plasma or purified fibrinogen and factor XIII
-
-
?
additional information
?
-
-
MASP-1 cannot cleave complement component C4, recombinant MASP-1 does not activate plasma prekallikrein
-
-
?
additional information
?
-
no activity with complement component C4. Direct activation of C3 convertase by MASP-1 occurs with very low catalytic efficiency and is not of physiological relevance
-
-
?
additional information
?
-
the enzyme MASP-1 shows a more relaxed substrate specificity. MASP-1 zymogen is fairly active on small substrates, and itautoactivates rapidly due to its relatively fast zymogen autoacti-vation step
-
-
?
additional information
?
-
-
the enzyme MASP-1 shows a more relaxed substrate specificity. MASP-1 zymogen is fairly active on small substrates, and itautoactivates rapidly due to its relatively fast zymogen autoacti-vation step
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
high-molecular weight kininogen + H2O
bradykinin + ?
a noncomplement substrate, activation
-
-
?
low-molecular-weight kininogen + H2O
?
-
the cleavage rate of low-molecular-weight kininogen by MASP-1 is about 5times lower than that of kininogen
-
-
?
proform coagulation factor XIII + H2O
mature coagulation factor XIII + ?
a noncomplement substrate, activation
-
-
?
proform mannan-binding lectin-associated serine protease 1 + H2O
mature mannan-binding lectin-associated serine protease 1 + ?
proform mannan-binding lectin-associated serine protease 2 + H2O
mature mannan-binding lectin-associated serine protease 2 + ?
proform mannan-binding lectin-associated serine protease 3 + H2O
mature mannan-binding lectin-associated serine protease 3 + ?
a complement substrate, activation
-
-
?
proform protease activated receptor 4 + H2O
mature protease activated receptor 4 + ?
activation
-
-
?
proform thrombin-activatable fibrinolysis inhibitor + H2O
mature thrombin-activatable fibrinolysis inhibitor + ?
activation
-
-
?
protease activated receptor 4 + H2O
?
PAR4, a noncomplement substrate, activation
-
-
?
prothrombin + H2O
thrombin a + ?
enzyme MASP-1 cleaves prothrombinat three cleavage sites, MASP-1 gives rise to an alternative active form of thrombin by cleaving at the cleavage site R393
-
-
?
fibrinogen + H2O
fibrin + ?
MASP-1-induced fibrin formation and activation is thrombin-dependent, in plasma environment fibrin formation is not directly induced by MASP-1 in the absence of prothrombin
-
-
?
proform mannan-binding lectin-associated serine protease 1 + H2O
mature mannan-binding lectin-associated serine protease 1 + ?
autocatalytic cleavage, a complement substrate, activation
-
-
?
proform mannan-binding lectin-associated serine protease 1 + H2O
mature mannan-binding lectin-associated serine protease 1 + ?
-
autocatalytic cleavage, a complement substrate, activation
-
-
?
proform mannan-binding lectin-associated serine protease 2 + H2O
mature mannan-binding lectin-associated serine protease 2 + ?
a complement substrate, activation
-
-
?
proform mannan-binding lectin-associated serine protease 2 + H2O
mature mannan-binding lectin-associated serine protease 2 + ?
-
a complement substrate, activation
-
-
?
proform mannan-binding lectin-associated serine protease 2 + H2O
mature mannan-binding lectin-associated serine protease 2 + ?
enzyme MASP-1 is the main activator of MASP-2
-
-
?
prothrombin + H2O
thrombin + ?
a noncomplement substrate, activation
-
-
?
additional information
?
-
-
complexes with mannose-binding lectin in the presence of Ca2+, involved in activation of complement cascade
-
?
additional information
?
-
involved in activation of complement cascade
-
?
additional information
?
-
-
involved in activation of complement cascade
-
?
additional information
?
-
-
involved in activation of complement cascade, circulates in serum complexed with mannose-binding protein
-
?
additional information
?
-
-
involved in activation of complement cascade, forms a complex with mannose-binding lectin
-
?
additional information
?
-
-
involved in activation of complement cascade, smallest functional unit for complement activation consists of serum mannose-binding protein dimers bound to MASP-1 homodimers
-
?
additional information
?
-
-
MASP-1 shows no activity toward complement C4. MASP-1 collaborates with MASP-2 in the generation of C3 convertase, a process observable at high serum concentration, but not at low serum concentration
-
-
?
additional information
?
-
-
MBL-MASP complexes, bound to mannan-agarose, generate clots when incubated with calcified plasma or purified fibrinogen and factor XIII
-
-
?
additional information
?
-
-
MASP-1 cannot cleave complement component C4, recombinant MASP-1 does not activate plasma prekallikrein
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Ca2+
-
provides binding of MASP-1 to immobilized mannan-binding lectin and L-ficolin/P35
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ACTRKLCW
a Schistocerca gregaria protease inhibitor-1 P4-P4' sequence mutant
alpha2-Macroglobulin
may be a physiological inhibitor, 1-3fold molar excess, forms a stable complex with the enzyme
-
antithrombin III
-
inhibitory in the presence of heparin on activity of MASP-1
-
EDTA
-
inhibits binding of MASP-1 to immobilized mannan-binding lectin and L-ficolin/P35, when substituted for Ca2+
lectin pathway C1-inhibitor
the inhibitor is not specific for MASP-1 versus MASP-2
-
MCTRKLCW
a Schistocerca gregaria protease inhibitor-1 P4-P4' sequence mutant
MCTRKLCY
a Schistocerca gregaria protease inhibitor-1 P4-P4' sequence mutant
Schistocerca gregaria protease inhibitor-2 variant FCTRKLCY
randomization of positions P4, P2, P1, P1', P2', and P4' of the protease binding loop while keeping the structurally indispensable Cys at P3 and P3' leads to monospecific MASP inhibitors. Inhibitor variant FCTRKLCY is specific for isoform MASP-1, treatment completely blocks the lectin pathway activation, demonstrating that MASP-1 is not an auxiliary but an essential pathway component
-
SGMI-1
selective MASP-1 inhibitor, based on the Schistocerca gregaria protease inhibitor scaffold
-
VCTRLWCE
a sunflower MASP inhibitor-2 P4-P4' sequence mutant, only slight inhibition
VCTRLWCN
a sunflower MASP inhibitor-2 P4-P4' sequence mutant, only slight inhibition
VCTRLYCN
a sunflower MASP inhibitor-2 P4-P4' sequence mutant, only slight inhibition
C1-inhibitor
completely blocks enzyme activity, 1-3fold molar excess, forms a stable complex with the enzyme
-
Schistocerca gregaria protease inhibitor-1
SGMI-1, sequence P4-P4' is FCTRKLCY, the structure of the MASP-1-SGMI-1 complex does not support the induced fit or conformational selection substrate-binding model, structure analysis, detailed overview
-
Schistocerca gregaria protease inhibitor-1
SGMI-1, specific inhibition of MASP-1 isozyme
-
additional information
-
MASP-1 is not inhibited by sunflower MASP inhibitor-2
-
additional information
no inhibition by Schistocerca gregaria protease inhibitor-2, SGMI-2, and sunflower MASP inhibitor-2, SFMI-2, but slight inhibition by inhibitor mutants, overview; Schistocerca gregaria protease inhibitor-2 variant VCTKLWCN is specific for isoform MASP-2 and not inhibitory for isoform MASP-1
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0048
Complement component C2
37°C, cleavage by the MASP-1 CCP1-CCP2-SP fragment
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.1
Complement component C2
37°C, cleavage by the MASP-1 CCP1-CCP2-SP fragment
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
30
Complement component C2
pH and temperature not specified in the publication
-
6
complement component C3i
pH and temperature not specified in the publication
-
0.4
high-molecular weight kininogen
pH and temperature not specified in the publication
-
0.45
proform mannan-binding lectin-associated serine protease 1
pH and temperature not specified in the publication
-
12
proform mannan-binding lectin-associated serine protease 2
pH and temperature not specified in the publication
-
1.2
proform mannan-binding lectin-associated serine protease 3
pH and temperature not specified in the publication
-
180
protease activated receptor 4
pH and temperature not specified in the publication
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000027
ACTRKLCW
pH and temperature not specified in the publication, recombinant enzyme
0.000275
cyclic GICSRSLPPICIPD
-
in 20 mM HEPES, 145 mM NaCl, 5 mM CaCl2, and 0.05% (v/v) Triton X-100, at pH 7.6 and 22°C
0.000065
GICSRSLPPICIPD
-
in 20 mM HEPES, 145 mM NaCl, 5 mM CaCl2, and 0.05% (v/v) Triton X-100, at pH 7.6 and 22°C
0.00002
MCTRKLCW
pH and temperature not specified in the publication, recombinant enzyme
0.000014
MCTRKLCY
pH and temperature not specified in the publication, recombinant enzyme
0.000007
Schistocerca gregaria protease inhibitor-2 variant FCTRKLCY
pH not specified in the publication, temperature not specified in the publication
-
0.000065
sunflower MASP inhibitor-1
pH and temperature not specified in the publication, recombinant enzyme
0.153
VCTRLWCE
pH and temperature not specified in the publication, recombinant enzyme
0.087
VCTRLWCN
pH and temperature not specified in the publication, recombinant enzyme
0.176
VCTRLYCN
pH and temperature not specified in the publication, recombinant enzyme
0.000007
Schistocerca gregaria protease inhibitor-1
pH and temperature not specified in the publication, recombinant enzyme
-
0.000007
Schistocerca gregaria protease inhibitor-1
-
pH and temperature not specified in the publication, recombinant enzyme
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
immunohistochemic determination of enzyme levels in plasma samples and variations over time, MASP-1 levels after the induction of an acute-phase response by operation for colorectal cancer show an initial short decrease, concomitant with an increase in C-reactive protein levels, followed by an increase, doubling the MASP-1 concentration after 2 days, overview
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
additional information
malfunction
increased MASP-1 plasma levels in patients in the suba-cute phase of myocardial infarction, but decreased levels of MASP-1 in patients withacute ischemic stroke
malfunction
N-terminal parts of MASP-1 enzyme which only contain non-enzymatic domains, and a stable zymogen mutant form of enzyme MASP-1 are ineffective to stimulate endothelial cells
malfunction
presence of a functional alternative pathway in a human patient with Malpuech-Michels-Mingarelli-Carnevale (3MC) syndrome caused by a genetic defect in the MASP1 gene, which abolishes the production of all three splice products of this gene: mannan-binding lectin-associated serine proteases 1 and 3, and MBL-associated protein of 44 kDa, a human complement
metabolism
among the components of the mannose-binding lectinMASPs complexes only enzyme MASP-1 is able to trigger response in human umbilical vein endothelial cells and the proteolytic activity of MASP-1 is essential
metabolism
both MASP-1 and MASP-2 are essential for lectin pathway activation in normal human serum
metabolism
human umbilical vein endothelial cells, activated by recombinnat MASP-1, secrete interleukin-6 and interleukin-8, but not interleukin-1alpha, interleukin-1ra, TNFalpha and MCP-1. rMASP-1 induces interleukin-6 and interleukin-8 production with different kinetics. Enzyme-triggered interleukin-6 and interleukin-8 production is regulated predominantly by the p38-MAPK pathway. The supernatant of rMASP-1-stimulated cells activates the chemotaxis of neutrophil granulocytes as an integrated effect of cytokine production
metabolism
target binding of pattern recognition molecules leads to the activation of zymogen mannan-binding lectin-associated serine proteases and triggers the lectin pathway, an antibody-independent activation route of the complement system, which provides immediate defense against pathogens and altered self-cells, but also causes severe tissue damage after stroke, heart attack, and other ischemia reperfusion injuries. MASP-2 and MASP-1 are both essential pathway components
metabolism
the enzyme is associated with humoral pattern-recognition molecules, overview
physiological function
-
the bradykinin production by MASP-1 may contribute to the pro-inflammatory effect of the lectin pathway of complement and to the elevated bradykinin levels in hereditary angioedema patients
physiological function
besides playing a crucial role in complement activation, the enzyme also triggers other cascade systems and even cells to mount a more powerful innate immune response, multiple roles of MASP-1 in the initiation of the innate immune response, overview. Enzyme MASP-1 is the one responsible for triggering the lectin pathway via its ability to rapidly autoactivate then cleave MASP-2, and possibly MASP-3. MASP-1 interacts with the coagulation cascade and the kinin generating system, and it can also activate endothelial cells eliciting pro-inflammatory signaling. MASP-1 seems to be a major link between the complementsystem and coagulation. Role of MASP-1 in endothelial cell activation and blood coagulation, and role of the enzyme in cardiovascular diseases, detailed overview
physiological function
enzyme MASP-1 plays a central role in the early innate immune response. The initiation complexes of the lectin pathway, consisting of mannose-binding lectin and associated serine proteases (MASPs) elicit Ca2+-signaling in cultured endothelial cells. The recombinant catalytic fragment of MASP-1 activates endothelial cells by cleaving protease activated receptor 4. Mannose binding lectin-mannan-binding lectin-associated serine protease 1 complexes trigger intracellular Ca2+-signaling in human umbilical vein endothelial cells, overview
physiological function
mannan-binding lectin-associated serine proteases MASP-1 and MASP-2 can readily form heterodimers after dissociation and re-association, however, in the presence of Ca2+ exchange of subunits is slow between the homodimers. Modeling of isoforms MASP-1:MASP-3 heterodimer formation indicates that subunits of these proteins are readily exchanged even in the presence of Ca2+
physiological function
MASP-1 cleaves complement component C2 but not complement component C4 and therefore is not capable of generating C3 convertase alone
physiological function
MASP-1, the most abundant enzyme of the complement lectin pathway, can induce p38-MAPK activation, NFkappaB signaling, and Ca2+-mobilization in endothelial cells and induces a unique cytokine pattern in endothelial cells linking complement system and neutrophil granulocytes. Besides initializing the complement lectin pathway, MASP-1 may activate neutrophils indirectly, via the endothelial cells, which link these effective antimicrobial host defense mechanisms
physiological function
the addition of mannan-binding lectin or ficolins allows the formation of serine proteases MASP-1-MASP-2 co-complexes. Co-complexes have a functional role in activating complement and are present in serum at varying levels, impacting on the degree of complement activation. Coexpression of MASP-2 with MASP-1, MASP-3, or mannan-binding lectin-associated protein 4 leads to detectable levels of heterodimers
physiological function
the enzyme MASP-1 is part of the lectin pathway of the complement system and is able to induce and promote clot formation, MASP-1-induced clotting is dependent on prothrombin
physiological function
the pro-factor D cleaving activity of MASP-1/-3 is not required for alternative pathway function, overview. In humans, neither MASP-1 nor MASP-3 are required for alternative pathway function, overview
physiological function
addition of recombinant active MASP-1 to a a microvascular, whole blood flow model results in accelerated fibrin clot formation while addition of inhibitor SGMI-1 delays it. MASP-1 inhibition and especially inhibition of both lectin pathway and complement pathway significantly diminishes fibrin deposition upon complement activation
physiological function
MASP-1 is not an activator of complement factor D precursor
physiological function
recombinant expression of MASP-1 in HUVECs decreases the expression of ICAM-2 and increases that of E-selectin, whereas ICAM-1, VCAM-1 and P-selectin expression remain unchanged. These changes result in increased adherence between differentiated PLB-985 cells and endothelial cells. Complement MASP-1 can increase adhesion between neutrophils and endothelial cells ina direct fashion
additional information
enzyme MASP-1 shows a more relaxed substrate specificity compared to the related complement enzymes, crystal structure analysis, overview. The catalytic triad of zymogen MASP-1 is in an active-like conformation, while the S1 pocket is blocked and the oxyanion hole is distorted, which are typical features of zymogen serine proteases. Upon activation, the new amino-terminus forms a salt-bridge with Asp645 rearranging the surface loopsand allowing the oxyanion hole and the S1 pocket to form. In the structure of zymogen MASP-1 two positive side chains might be able to substitute for the amino-terminus aiding Aspc194to rotateto the active-like position
additional information
-
enzyme MASP-1 shows a more relaxed substrate specificity compared to the related complement enzymes, crystal structure analysis, overview. The catalytic triad of zymogen MASP-1 is in an active-like conformation, while the S1 pocket is blocked and the oxyanion hole is distorted, which are typical features of zymogen serine proteases. Upon activation, the new amino-terminus forms a salt-bridge with Asp645 rearranging the surface loopsand allowing the oxyanion hole and the S1 pocket to form. In the structure of zymogen MASP-1 two positive side chains might be able to substitute for the amino-terminus aiding Aspc194to rotateto the active-like position
additional information
the catalytic activity of MASP-1 suppresses its expression through intracellular rapid autoactivation and autodegradation
additional information
-
the catalytic activity of MASP-1 suppresses its expression through intracellular rapid autoactivation and autodegradation
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
38000
-
calculated molecular mass of the MASP-1 CUB-EGF fragment in the presence of Ca2+
90000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
additional information
dimer
enzyme three-dimensional structure analysis, the enzyme monomer domains are CUB1-EGF-CUB2-CCP1-CCP2-SP, standing for C1r/C1s-Uegf-BMP domain 1, epidermal growth factor domain, C1r/C1s-Uegf-BMP domain 2, complement control protein domain 1, complement control protein domain 2, and serine protease domain, overview. the enzyme dimer is formed by binding of monomers via CUB1 and EGF domains
dimer
the enzyme monomer domains are CUB1-EGF-CUB2-CCP1-CCP2-SP, standing for C1r/C1s-Uegf-BMP domain 1, epidermal growth factor domain, C1r/C1s-Uegf-BMP domain 2, complement control protein domain 1, complement control protein domain 2, and serine protease domain
additional information
in buffer containing EDTA, MASP-1 regions D1-3 dissociate slowly to monomers. Upon re-calcification dimers are re-formed, but this process is even slower
additional information
-
in buffer containing EDTA, MASP-1 regions D1-3 dissociate slowly to monomers. Upon re-calcification dimers are re-formed, but this process is even slower
additional information
the enzyme monomer domains are CUB1-EGF-CUB2-CCP1-CCP2-SP, standing for C1r/C1s-Uegf-BMP domain 1, epidermal growth factor domain, C1r/C1s-Uegf-BMP domain 2, complement control protein domain 1, complement control protein domain 2, and serine protease domain, domain organization of MASP-1, overview
additional information
-
the enzyme monomer domains are CUB1-EGF-CUB2-CCP1-CCP2-SP, standing for C1r/C1s-Uegf-BMP domain 1, epidermal growth factor domain, C1r/C1s-Uegf-BMP domain 2, complement control protein domain 1, complement control protein domain 2, and serine protease domain, domain organization of MASP-1, overview
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
proteolytic modification
-
unactivated proenzyme is converted into the active form comprised of two polypeptides by cleavage between Arg448 and Ile449
proteolytic modification
enzyme MASP-1 performs autoactivation through proteolytic cleavage of its zymogen
proteolytic modification
enzyme MASP-1 performs autoactivation through proteolytic cleavage of its zymogen. Natural MASP-1 is activated by cleavage in the activation peptide, generating an A-chain (CUB-EGF-CUB-CCPCCP) and a B-chain (the serine protease domain), which remain associated through a disulphide bridge. MASP-1 autodegradation occurs intracellularly, not inhibited by addition of inhibitors to the culture medium
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
catalytic region of MASP-1, hanging-drop vapour-diffusion method, the best crystal diffract to 2.55 A resolution and belongs to space group P2(1)2(1)2(1), with unit-cell parameters a = 68.4, b = 70.4, c = 121.4 A
hanging drop vapor diffusion method, X-ray structure of the CUB1-EGF-CUB2 domain of human MASP-1/3, responsible for interaction of MASP-1 and -3 with their partner proteins mannan-binding lectin and ficolins, is solved to a resolution of 2.3 A
in complex with Schistocerca gregaria protease inhibitor-2 variant VCTKLWCN, to 1.28 A resolution. Structure reveals significant plasticity of the protease
MASP-1 catalytic domain in complex with protease inhibitor SGPI-1, recombinant CCP1-CCP2-SP fragment of MASP-1 and SGMI-1 inhibitor are mixed in a 2:3 molar ratio and concentrated to 5 mg/ml, hanging drop vapor diffusion method, mixing of 0.001 ml of protein and 0.001 ml of reservoir solution comprising 0.1 M HEPES, pH 7.0, 25% PEG 1000, 0.3 M NaNO3, at 20°C, crystal structure determination and analysis at 3.2 A resolution, molecular replacement
the collagen-like domain of mannan-binding lectin in complex with the binding domain of its associated protease MASP-1
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
R504Q
site-directed mutagenesis, construction of a MASP-1 catalytic fragment, that has a molecular weight of 45.5 kDa and consists of the three C-terminal domains complement control protein 1 and 2 followed by the serine protease domain
S627A
-
kinetic parameters similiar to wild type, mutant is activated by its active counterpart
S646A
additional information
additional information
generation of a MASP-1 catalytic fragment encoding the CCP1-CCP2-SP region (rMASPcf)
additional information
generation of a truncated enzyme version comprising the MAPS-1 CUB1-EGF-CUB2 domains, i.e. MASP-1 D1-3 CBD, rapid dissociation upon EDTA treatment, and heterodimer formation, exchange of subunits between dimers in the presence of Ca2+, overview. Heterodimer formation between N-terminal fragemnts of MASP1 and MASP-2, i.e. MASP-1 D1-3 and MASP-2 D1-3, is structurally allowed but takes place to only a small amount
additional information
-
generation of a truncated enzyme version comprising the MAPS-1 CUB1-EGF-CUB2 domains, i.e. MASP-1 D1-3 CBD, rapid dissociation upon EDTA treatment, and heterodimer formation, exchange of subunits between dimers in the presence of Ca2+, overview. Heterodimer formation between N-terminal fragemnts of MASP1 and MASP-2, i.e. MASP-1 D1-3 and MASP-2 D1-3, is structurally allowed but takes place to only a small amount
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
mutant R504Q catalytic fragment, the mutant is resistant to autolysis and preserves its enzymatic activity during prolonged incubation, estimated half-life of several hours in plasma at 37°C
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant wild-type and mutant MASP-1 catalytic fragments encoding the complement control protein domains 1 and 2, CCP1-CCP2-SP, region from Escherichia coli by repeated anion exchange chromatography and gel filtration
refolded recombinant chitin-binding domain-tagged MAPS-1 CUB1-EGF-CUB2 by anion echange chromatography and gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
catalytic region of MASP-1 and MASP-2, consisting of the two CCP modules and the SP domain (CCP1-CCP2-SP) is expressed in Escherichia coli BL-21
expression of chitin-binding domain-tagged MAPS-1 CUB1-EGF-CUB2 construct in Escherichia coli strain BL21 (DE3) pLysS in inclusion bodies
expression of wild-type and catalytically inactive mutant full-length recombinant human MASP-1 entirely in the zymogen form in Hep-G2 and Chang liver cells or HEK-293F cells. The active protease is produced through co-expression with the serine protease inhibitor C1 inhibitor avoiding the self-suppression of enzyme expression by its autocatalytic activity, the expressed protease is capable of binding MBL and autoactivating, and is catalytically active
recombinant expression of the CCP1-CCP2-SP fragment of enzyme MASP-1 in Escherichia coli
recombinant expression of wild-type and mutant MASP-1 catalytic fragments encoding the complement control protein domains 1 and 2, CCP1-CCP2-SP, region (rMASPcf) in Escherichia coli
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the catalytic activity of MASP-1 suppresses its expression through rapid auto-activation and autodegradation intracellularly, not inhibited by addition of inhibitors to the culture medium
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
solubilization of recombinant chitin-binding domain-tagged MAPS-1 CUB1-EGF-CUB2 from Escherichia coli strain BL21 (DE3) pLysS inclusion bodies by 7 M guanidinium hydrochloride in 50 mM Tris, 50 mM DTT, pH 8.0, followed by dilution to 5.5 mg/ml protein, and refolding by diluting 20 ml of the 5 mg/mL solution into 1 l of 0.75 M Arg, 200 mM CaCl2, 3 mM glutathione, 2 mM oxidized glutathione, pH 8.0, refolding buffer, at least one week at 4°C, followed by dialysis
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
additional information
-
native MBL-MASP complexes on average do not have fixed MBL-(MASP-1)-(MASP-2) stoichometry
medicine
-
there is an association of higher MBL/MASP-1 complex activity with liver disease and an association with severity of fibrosis
medicine
proteases MASP-1 and MASP-2 levels are significantly higher in children and adults with type 1 diabetes mellitus than in their respective control groups, whereas proteases MASP-3 and MAp44 levels do not differ between patients and controls. MASP-1 and MASP-2 levels correlate with hemoglobin HbA1c, and MASP levels decrease when glycaemic control improves
REF.
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TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Takada, F.; Takayama, Y.; Hatsuse, H.; Kawakami, M.
A new member of the C1s family of complement proteins found in a bactericidal factor, Ra-reactive factor, in human serum
Biochem. Biophys. Res. Commun.
196
1003-1009
1993
Homo sapiens (P48740), Homo sapiens
Matsushita, M.; Ezekowitz, R.A.; Fujita, T.
The Gly-54--Asp allelic form of human mannose-binding protein (MBP) fails to bind MBP-associated serine protease
Biochem. J.
311
1021-1023
1995
Homo sapiens
-
Matsushita, M.; Endo, Y.; Fujita, T.
MASP1 (MBL-associated serine protease 1)
Immunobiology
199
340-347
1998
Homo sapiens, Mus musculus
Chen, C.B.; Wallis, R.
Stoichiometry of complexes between mannose-binding protein and its associated serine proteases. Defining functional units for complement activation
J. Biol. Chem.
276
25894-25902
2001
Homo sapiens
Rossi, V.; Cseh, S.; Bally, I.; Thielens, N.M.; Jensenius, J.C.; Arlaud, G.J.
Substrate specificities of recombinant mannan-binding lectin-associated serine proteases-1 and -2
J. Biol. Chem.
276
40880-40887
2001
Homo sapiens
Matsushita, M.; Thiel, S.; Jensenius, J.C.; Terai, I.; Fujita, T.
Proteolytic activities of two types of mannose-binding lectin-associated serine protease
J. Immunol.
165
2637-2642
2000
Homo sapiens (P48740), Homo sapiens
Thielens, N.M.; Cseh, S.; Thiel, S.; Vorup-Jensen, T.; Rossi, V.; Jensenius, J.C.; Arlaud, G.J.
Interaction properties of human mannan-binding lectin (MBL)-associated serine proteases-1 and -2, MBL-associated protein 19, and MBL
J. Immunol.
166
5068-5077
2001
Homo sapiens
Ambrus, G.; Gal, P.; Kojima, M.; Szilagyi, K.; Balczer, J.; Antal, J.; Graf, L.; Laich, A.; Moffatt, B.E.; Schwaeble, W.; Sim, R.B.; Zavodszky, P.
Natural substrates and inhibitors of mannan-binding lectin-associated serine protease-1 and -2: a study on recombinant catalytic fragments
J. Immunol.
170
1374-1382
2003
Homo sapiens (P48740)
Sorensen, R.; Thiel, S.; Jensenius, J.C.
Mannan-binding-lectin-associated serine proteases, characteristics and disease associations
Semin. Immunopathol.
27
299-319
2005
Homo sapiens
Schwaeble, W.J.; Stover, C.; Reid, K.B.
Mannan-binding lectin-associated serine proteases
Handbook of Proteolytic Enzymes(Barrett,A. J. ,Rawlings,N. D. ,Woessner,J. F. ,Eds. )Academic Press
2
1623-1627
2004
Lethenteron camtschaticum, Halocynthia roretzi, Homo sapiens, Mus musculus, Rattus norvegicus, Xenopus laevis, Branchiostoma belcheri
-
Zundel, S.; Cseh, S.; Lacroix, M.; Dahl, M.R.; Matsushita, M.; Andrieu, J.P.; Schwaeble, W.J.; Jensenius, J.C.; Fujita, T.; Arlaud, G.J.; Thielens, N.M.
Characterization of recombinant mannan-binding lectin-associated serine protease (MASP)-3 suggests an activation mechanism different from that of MASP-1 and MASP-2
J. Immunol.
172
4342-4350
2004
Homo sapiens
Mayilyan, K.R.; Presanis, J.S.; Arnold, J.N.; Hajela, K.; Sim, R.B.
Heterogeneity of MBL-MASP complexes
Mol. Immunol.
43
1286-1292
2006
Homo sapiens
Brown, K.S.; Keogh, M.J.; Tagiuri, N.; Grainge, M.J.; Presanis, J.S.; Ryder, S.D.; Irving, W.L.; Ball, J.K.; Sim, R.B.; Hickling, T.P.
Severe fibrosis in hepatitis C virus-infected patients is associated with increased activity of the mannan-binding lectin (MBL)/MBL-associated serine protease 1 (MASP-1) complex
Clin. Exp. Immunol.
147
90-98
2007
Homo sapiens
Moller-Kristensen, M.; Thiel, S.; Sjoeholm, A.; Matsushita, M.; Jensenius, J.C.
Cooperation between MASP-1 and MASP-2 in the generation of C3 convertase through the MBL pathway
Int. Immunol.
19
141-149
2007
Homo sapiens
Dobo, J.; Harmat, V.; Sebestyen, E.; Beinrohr, L.; Zavodszky, P.; Gal, P.
Purification, crystallization and preliminary X-ray analysis of human mannose-binding lectin-associated serine protease-1 (MASP-1) catalytic region
Acta Crystallogr. Sect. F
64
781-784
2008
Homo sapiens (P48740), Homo sapiens
Krarup, A.; Gulla, K.C.; Gal, P.; Hajela, K.; Sim, R.B.
The action of MBL-associated serine protease 1 (MASP1) on factor XIII and fibrinogen
Biochim. Biophys. Acta
1784
1294-1300
2008
Homo sapiens (P48740)
Teillet, F.; Gaboriaud, C.; Lacroix, M.; Martin, L.; Arlaud, G.J.; Thielens, N.M.
Crystal structure of the CUB1-EGF-CUB2 domain of human MASP-1/3 and identification of its interaction sites with mannan-binding lectin and ficolins
J. Biol. Chem.
283
25715-25724
2008
Homo sapiens (P48740), Homo sapiens
Gal, P.; Dobo, J.; Zavodszky, P.; Sim, R.B.
Early complement proteases: C1r, C1s and MASPs. A structural insight into activation and functions
Mol. Immunol.
46
2745-2752
2009
Homo sapiens (P48740)
Gulla, K.C.; Gupta, K.; Krarup, A.; Gal, P.; Schwaeble, W.J.; Sim, R.B.; OConnor, C.D.; Hajela, K.
Activation of mannan-binding lectin-associated serine proteases leads to generation of a fibrin clot
Immunology
129
482-495
2010
Homo sapiens
Kocsis, A.; Kekesi, K.A.; Szasz, R.; Vegh, B.M.; Balczer, J.; Dobo, J.; Zavodszky, P.; Gal, P.; Pal, G.
Selective inhibition of the lectin pathway of complement with phage display selected peptides against mannose-binding lectin-associated serine protease (MASP)-1 and -2: significant contribution of MASP-1 to lectin pathway activation
J. Immunol.
185
4169-4178
2010
Homo sapiens
Dobo, J.; Major, B.; Kekesi, K.A.; Szabo, I.; Megyeri, M.; Hajela, K.; Juhasz, G.; Zavodszky, P.; Gal, P.
Cleavage of kininogen and subsequent bradykinin release by the complement component: mannose-binding lectin-associated serine protease (MASP)-1
PLoS ONE
6
e20036
2011
Homo sapiens
Gingras, A.R.; Girija, U.V.; Keeble, A.H.; Panchal, R.; Mitchell, D.A.; Moody, P.C.; Wallis, R.
Structural basis of mannan-binding lectin recognition by its associated serine protease MASP-1: implications for complement activation
Structure
19
1635-1643
2011
Homo sapiens
Thiel, S.; Jensen, L.; Degn, S.E.; Nielsen, H.J.; Gal, P.; Dobo, J.; Jensenius, J.C.
Mannan-binding lectin (MBL)-associated serine protease-1 (MASP-1), a serine protease associated with humoral pattern-recognition molecules: normal and acute-phase levels in serum and stoichiometry of lectin pathway components
Clin. Exp. Immunol.
169
38-48
2012
Homo sapiens (P48740)
Heja, D.; Harmat, V.; Fodor, K.; Wilmanns, M.; Dobo, J.; Kekesi, K.A.; Zavodszky, P.; Gal, P.; Pal, G.
Monospecific inhibitors show that both mannan-binding lectin-associated serine protease-1 (MASP-1) and -2 are essential for lectin pathway activation and reveal structural plasticity of MASP-2
J. Biol. Chem.
287
20290-20300
2012
Homo sapiens (P48740)
Degn, S.E.; Jensen, L.; Olszowski, T.; Jensenius, J.C.; Thiel, S.
Co-complexes of MASP-1 and MASP-2 associated with the soluble pattern-recognition molecules drive lectin pathway activation in a manner inhibitable by MAp44
J. Immunol.
191
1334-1345
2013
Homo sapiens (P48740)
Degn, S.; Jensenius, J.; Thiel, S.
The pro-factor D cleaving activity of MASP-1/-3 is not required for alternative pathway function
J. Immunol.
192
5447-5448
2014
Homo sapiens (P48740), Mus musculus (P48740)
Parej, K.; Hermann, A.; Donath, N.; Zavodszky, P.; Gal, P.; Dobo, J.
Dissociation and re-association studies on the interaction domains of mannan-binding lectin (MBL)-associated serine proteases, MASP-1 and MASP-2, provide evidence for heterodimer formation
Mol. Immunol.
59
1-9
2014
Homo sapiens (P48740), Homo sapiens
Megyeri, M.; Jani, P.K.; Kajdacsi, E.; Dobo, J.; Schwaner, E.; Major, B.; Rigo, J.; Zavodszky, P.; Thiel, S.; Cervenak, L.; Gal, P.
Serum MASP-1 in complex with MBL activates endothelial cells
Mol. Immunol.
59
39-45
2014
Homo sapiens (P48740)
Dobo, J.; Schroeder, V.; Jenny, L.; Cervenak, L.; Zavodszky, P.; Gal, P.
Multiple roles of complement MASP-1 at the interface of innate immune response and coagulation
Mol. Immunol.
61
69-78
2014
Homo sapiens (P48740), Homo sapiens
Jenny, L.; Dobo, J.; Gal, P.; Schroeder, V.
MASP-1 of the complement system promotes clotting via prothrombin activation
Mol. Immunol.
65
398-405
2015
Homo sapiens (P48740)
Hess, K.; Ajjan, R.; Phoenix, F.; Dobo, J.; Gal, P.; Schroeder, V.
Effects of MASP-1 of the complement system on activation of coagulation factors and plasma clot formation
PLoS ONE
7
e35690
2012
Homo sapiens (P48740)
Jani, P.K.; Kajdacsi, E.; Megyeri, M.; Dobo, J.; Doleschall, Z.; Futosi, K.; Timar, C.I.; Mocsai, A.; Mako, V.; Gal, P.; Cervenak, L.
MASP-1 induces a unique cytokine pattern in endothelial cells: a novel link between complement system and neutrophil granulocytes
PLoS ONE
9
e87104
2014
Homo sapiens (P48740), Homo sapiens
Degn, S.E.; Thiel, S.; Jensenius, J.C.
Recombinant expression of the autocatalytic complement protease MASP-1 is crucially dependent on co-expression with its inhibitor, C1 inhibitor
Protein Expr. Purif.
88
173-182
2013
Homo sapiens (P48740), Homo sapiens
Jenny, L.; Ajjan, R.; King, R.; Thiel, S.; Schroeder, V.
Plasma levels of mannan-binding lectin-associated serine proteases MASP-1 and MASP-2 are elevated in type 1 diabetes and correlate with glycaemic control
Clin. Exp. Immunol.
180
227-232
2015
Homo sapiens (P48740), Homo sapiens
Oroszlan, G.; Kortvely, E.; Szakacs, D.; Kocsis, A.; Dammeier, S.; Zeck, A.; Ueffing, M.; Zavodszky, P.; Pal, G.; Gal, P.; Dobo, J.
MASP-1 and MASP-2 do not activate pro-factor D in resting human blood, whereas MASP-3 is a potential activator kinetic analysis involving specific MASP-1 and MASP-2 inhibitors
J. Immunol.
196
857-865
2016
Homo sapiens (P48740), Homo sapiens
Jenny, L.; Dobo, J.; Gal, P.; Schroeder, V.
MASP-1 of the complement system promotes clotting via prothrombin activation
Mol. Immunol.
65
398-405
2015
Homo sapiens (P48740)
Jani, P.K.; Schwaner, E.; Kajdacsi, E.; Debreczeni, M.L.; Ungai-Salanki, R.; Dobo, J.; Doleschall, Z.; Rigo, J.; Geiszt, M.; Szabo, B.; Gal, P.; Cervenak, L.
Complement MASP-1 enhances adhesion between endothelial cells and neutrophils by up-regulating E-selectin expression
Mol. Immunol.
75
38-47
2016
Homo sapiens (P48740), Homo sapiens
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