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alpha-chain of complement C3 + H2O
?
-
-
-
?
alpha-chain of complement C4 + H2O
?
-
preferred substrate
-
?
antithrombin + H2O
?
cleavage at R425-/-S425
-
-
?
benzoyl-L-arginine p-nitroanilide + H2O
benzoyl-L-arginine + 4-nitroaniline
-
-
-
-
?
benzyloxycarbonyl-Val-Pro-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Val-Pro-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
C1-inhibitor + H2O
?
cleavage at R466-/-T467
-
-
?
complement component C2 + H2O
?
complement component C2 + H2O
complement component C2b + ?
-
-
-
-
?
complement component C3 + H2O
?
complement component C3 + H2O
complement component C3a + complement component C3b
-
activates complement C3
-
?
complement component C3 + H2O
complement component C3b + ?
-
-
-
-
?
complement component C3i + H2O
?
complement-activating component of Ra-reactive factor + H2O
?
cleavage at Arg448-/-Ile449
-
-
?
D-Phe-Pip-Arg-4-nitroanilide + H2O
D-Phe-Pip-Arg + 4-nitroaniline
a chromogenic thrombin substrate, recombinant human mannose-binding lectin alone fails to cleave the substrate, but cleavage is restored when the recombinant enzyme MASP-1 is added to either MASP-1/-3 KO sera or rhMBL
-
-
?
factor D zymogen + H2O
mature factor D + ?
-
-
-
?
factor XIII + H2O
factor XIIIa + ?
-
-
-
-
?
factor XIII A-chain + H2O
?
catalytic activity for factor XIII and fibrinogen cleavage is much lower than that of thrombin
-
-
?
fibrinogen + H2O
fibrin + ?
fibrinogen beta-chain + H2O
?
cleavage at R44-/-G45 and other sites
-
-
?
high-molecular weight kininogen + H2O
bradykinin + ?
a noncomplement substrate, activation
-
-
?
kininogen + H2O
bradykinin + ?
-
-
-
-
?
kininogen + H2O
kinin + ?
-
-
-
?
L-lysine thiobenzyl ester + H2O
?
-
C3647
-
-
?
low-molecular-weight kininogen + H2O
?
-
the cleavage rate of low-molecular-weight kininogen by MASP-1 is about 5times lower than that of kininogen
-
-
?
MASP-2 zymogen + H2O
mature MASP-2 + ?
MASP-3 zymogen + H2O
mature MASP-3 + ?
-
-
-
?
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
-
-
?
N-carbobenzoxy-L-alanine-4-nitrophenyl ester + H2O
?
-
-
-
?
N-carbobenzoxy-L-lysine-4-nitrophenyl ester + H2O
N-carbobenzoxy-L-Lys + 4-nitrophenol
-
-
-
?
N-carbobenzoxy-L-tyrosine-4-nitrophenyl ester + H2O
?
-
-
-
?
N-carboxybenzyloxyglycine-L-arginine thiobenzyl ester + H2O
?
-
-
-
?
Nalpha-benzoyl-L-arginine ethyl ester + H2O
?
-
-
-
?
pro-factor D + H2O
factor D + ?
proform coagulation factor XIII + H2O
mature coagulation factor XIII + ?
proform factor XIII + H2O
mature factor XIII + ?
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 + ?
protease activated receptor 4 + H2O
?
protease-activated receptor 4 + H2O
?
-
-
-
-
?
prothrombin + H2O
thrombin + ?
prothrombin + H2O
thrombin a + ?
Val-Pro-Arg-4-methylcoumarin-7-amide + H2O
?
-
-
-
-
?
additional information
?
-
complement component C2 + H2O
?
-
-
-
?
complement component C2 + H2O
?
-
-
-
-
?
complement component C2 + H2O
?
-
-
-
?
complement component C2 + H2O
?
-
-
-
-
?
complement component C2 + H2O
?
-
-
-
?
complement component C2 + H2O
?
-
activates complement C2
-
?
complement component C2 + H2O
?
cleavage at R243-/-K244
-
-
?
complement component C2 + H2O
?
digested by the MASP-1 CCP1-CCP2-SP fragment at a moderate rate
-
-
?
complement component C2 + H2O
?
a complement substrate, activation
-
-
?
complement component C2 + H2O
?
-
-
-
-
?
complement component C2 + H2O
?
-
-
-
-
?
complement component C3 + H2O
?
-
-
-
?
complement component C3 + H2O
?
-
-
-
-
?
complement component C3 + H2O
?
-
cleavage with low efficiency
-
-
?
complement component C3 + H2O
?
cleavage with appearance of the alpha-chain
-
-
?
complement component C3 + H2O
?
-
-
-
-
?
complement component C3i + H2O
?
-
-
-
?
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
-
-
?
factor XIII + H2O
?
-
-
-
-
?
factor XIII + H2O
?
cleavage at R38-/-G39
-
-
?
Fibrinogen + H2O
?
-
-
-
-
?
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 + ?
-
-
-
-
?
fibrinogen + H2O
fibrin + ?
-
-
-
?
fibrinogen + H2O
fibrin + ?
low activity
-
-
?
fibrinogen + H2O
fibrin + ?
a noncomplement substrate, activation
-
-
?
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
-
-
?
MASP-2 zymogen + H2O
mature MASP-2 + ?
-
-
-
?
MASP-2 zymogen + H2O
mature MASP-2 + ?
MASP-2 is a key enzyme that cleaves C4 and C2 to assemble a C3 convertase
-
-
?
pro-factor D + H2O
factor D + ?
-
-
-
?
pro-factor D + H2O
factor D + ?
-
-
-
?
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 + ?
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
?
cleavage at R47-/-G48
-
-
?
protease activated receptor 4 + H2O
?
PAR4, a noncomplement substrate, activation
-
-
?
Protein + H2O
?
-
-
-
?
prothrombin + H2O
thrombin + ?
-
-
-
-
?
prothrombin + H2O
thrombin + ?
-
-
-
?
prothrombin + H2O
thrombin + ?
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
?
-
-
no activity with complement C4
-
?
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
?
-
-
involved in innate immunity
-
?
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
?
-
no digestion of complement component C4
-
-
?
additional information
?
-
-
no digestion of complement component C4
-
-
?
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
-
-
?
additional information
?
-
no substrate: complement factor D
-
-
?
additional information
?
-
-
no substrate: complement factor D
-
-
?
additional information
?
-
-
involved in activation of complement cascade
-
?
additional information
?
-
-
involved in activation of complement cascade
-
?
additional information
?
-
involved in activation of complement cascade, enzyme is complexed with the mannose-binding protein
-
?
additional information
?
-
-
involved in activation of complement cascade, enzyme is complexed with the mannose-binding protein
-
?
additional information
?
-
-
involved in activation of complement cascade, forms a complex with mannose-binding lectin
-
?
additional information
?
-
MASP-1 contributes to the activation of the lectin pathway, probably through the activation of MASP-2
-
-
?
additional information
?
-
-
MASP-1 contributes to the activation of the lectin pathway, probably through the activation of MASP-2
-
-
?
additional information
?
-
involved in activation of complement cascade, enzyme is complexed with the mannose-binding protein
-
?
additional information
?
-
-
involved in activation of complement cascade, circulates as a complex with mannose-binding protein, minimal functional unit for complement activation is a MASP homodimer bound to two mannose-binding protein trimeric subunits
-
?
additional information
?
-
-
no cleavage of complement C4 and N-alpha-carbobenzoxy-L-lysine p-nitropenhyl ester
-
-
?
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complement component C2 + H2O
?
complement component C3 + H2O
?
-
-
-
-
?
factor D zymogen + H2O
mature factor D + ?
-
-
-
?
factor XIII + H2O
?
-
-
-
-
?
factor XIII + H2O
factor XIIIa + ?
-
-
-
-
?
Fibrinogen + H2O
?
-
-
-
-
?
fibrinogen + H2O
fibrin + ?
high-molecular weight kininogen + H2O
bradykinin + ?
a noncomplement substrate, activation
-
-
?
kininogen + H2O
bradykinin + ?
-
-
-
-
?
low-molecular-weight kininogen + H2O
?
-
the cleavage rate of low-molecular-weight kininogen by MASP-1 is about 5times lower than that of kininogen
-
-
?
MASP-2 zymogen + H2O
mature MASP-2 + ?
MASP-2 is a key enzyme that cleaves C4 and C2 to assemble a C3 convertase
-
-
?
MASP-3 zymogen + H2O
mature MASP-3 + ?
-
-
-
?
pro-factor D + H2O
factor D + ?
proform coagulation factor XIII + H2O
mature coagulation factor XIII + ?
a noncomplement substrate, activation
-
-
?
proform factor XIII + H2O
mature factor XIII + ?
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
-
-
?
protease-activated receptor 4 + H2O
?
-
-
-
-
?
prothrombin + H2O
thrombin + ?
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
-
-
?
additional information
?
-
complement component C2 + H2O
?
-
-
-
-
?
complement component C2 + H2O
?
-
-
-
?
complement component C2 + H2O
?
a complement substrate, activation
-
-
?
complement component C2 + H2O
?
-
-
-
-
?
complement component C2 + H2O
?
-
-
-
-
?
fibrinogen + H2O
fibrin + ?
-
-
-
-
?
fibrinogen + H2O
fibrin + ?
a noncomplement substrate, activation
-
-
?
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
-
-
?
pro-factor D + H2O
factor D + ?
-
-
-
?
pro-factor D + H2O
factor D + ?
-
-
-
?
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
-
-
?
Protein + H2O
?
-
-
-
?
prothrombin + H2O
thrombin + ?
-
-
-
-
?
prothrombin + H2O
thrombin + ?
activation
-
-
?
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
?
-
-
involved in innate immunity
-
?
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
-
-
?
additional information
?
-
-
involved in activation of complement cascade
-
?
additional information
?
-
-
involved in activation of complement cascade
-
?
additional information
?
-
involved in activation of complement cascade, enzyme is complexed with the mannose-binding protein
-
?
additional information
?
-
-
involved in activation of complement cascade, enzyme is complexed with the mannose-binding protein
-
?
additional information
?
-
-
involved in activation of complement cascade, forms a complex with mannose-binding lectin
-
?
additional information
?
-
MASP-1 contributes to the activation of the lectin pathway, probably through the activation of MASP-2
-
-
?
additional information
?
-
-
MASP-1 contributes to the activation of the lectin pathway, probably through the activation of MASP-2
-
-
?
additional information
?
-
involved in activation of complement cascade, enzyme is complexed with the mannose-binding protein
-
?
additional information
?
-
-
involved in activation of complement cascade, circulates as a complex with mannose-binding protein, minimal functional unit for complement activation is a MASP homodimer bound to two mannose-binding protein trimeric subunits
-
?
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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Angioedemas, Hereditary
The Levels of the Lectin Pathway Serine Protease MASP-1 and Its Complex Formation with C1 Inhibitor Are Linked to the Severity of Hereditary Angioedema.
Arthritis
Essential role of complement mannose-binding lectin-associated serine proteases-1/3 in the murine collagen antibody-induced model of inflammatory arthritis.
Arthritis
Key Components of the Complement Lectin Pathway Are Not Only Required for the Development of Inflammatory Arthritis but Also Regulate the Transcription of Factor D.
Arthritis
Mannan-Binding Lectin-Associated Serine Protease 1/3 Cleavage of Pro-Factor D into Factor D In Vivo and Attenuation of Collagen Antibody-Induced Arthritis through Their Targeted Inhibition by RNA Interference-Mediated Gene Silencing.
Atherosclerosis
Distinct Longitudinal Associations of MBL, MASP-1, MASP-2, MASP-3, and MAp44 With Endothelial Dysfunction and Intima-Media Thickness: The Cohort on Diabetes and Atherosclerosis Maastricht (CODAM) Study.
Autoimmune Diseases
Circulating levels of mannan-binding lectin (MBL) and MBL-associated serine protease 2 in endemic pemphigus foliaceus.
Bacterial Infections
Cutting Edge: A New Player in the Alternative Complement Pathway, MASP-1 Is Essential for LPS-Induced, but Not for Zymosan-Induced, Alternative Pathway Activation.
Bacterial Infections
Functional characterization of a ficolin-mediated complement pathway in amphioxus.
Bacterial Infections
Mannan-binding lectin-associated serine protease-1 (MASP-1) mediates immune responses against Aeromonas hydrophila in vitro and in vivo in grass carp.
Blindness
Proteomics-based identification and validation of novel plasma biomarkers phospholipid transfer protein and mannan-binding lectin serine protease-1 in age-related macular degeneration.
Brain Injuries
Mannan binding lectin-associated serine protease-2 (MASP-2) critically contributes to post-ischemic brain injury independent of MASP-1.
Brain Ischemia
Mannan binding lectin-associated serine protease-2 (MASP-2) critically contributes to post-ischemic brain injury independent of MASP-1.
Carcinoma
Identification of novel candidate target genes, including EPHB3, MASP1 and SST at 3q26.2-q29 in squamous cell carcinoma of the lung.
Carcinoma, Squamous Cell
Identification of novel candidate target genes, including EPHB3, MASP1 and SST at 3q26.2-q29 in squamous cell carcinoma of the lung.
Cardiovascular Diseases
MASPs at the crossroad between the complement and the coagulation cascades - the case for COVID-19.
Cerebrovascular Disorders
MASPs at the crossroad between the complement and the coagulation cascades - the case for COVID-19.
Cervical Intraepithelial Neoplasia
MASP-1 and MASP-2 Serum Levels Are Associated With Worse Prognostic in Cervical Cancer Progression.
COVID-19
MASPs at the crossroad between the complement and the coagulation cascades - the case for COVID-19.
Crohn Disease
Polymorphisms in the Mannose-Binding Lectin Gene are Associated with Defective Mannose-Binding Lectin Functional Activity in Crohn's Disease Patients.
Diabetes Mellitus
Plasma Levels of MASP-1 and MASP-2 are Elevated in Type 1 Diabetes and Correlate with Glycaemic Control.
Diabetes Mellitus, Type 1
Plasma Levels of MASP-1 and MASP-2 are Elevated in Type 1 Diabetes and Correlate with Glycaemic Control.
Diabetes Mellitus, Type 2
MASP1, THBS1, GPLD1 and ApoA-IV are novel biomarkers associated with prediabetes: the KORA F4 study.
Diabetes Mellitus, Type 2
Plasma levels of MASP-1, MASP-3 and MAp44 in patients with type 2 diabetes - influence of glycaemic control, body composition and polymorphisms in the MASP1 gene.
Glioma
Dibutyryl cAMP- or Interleukin-6-induced astrocytic differentiation enhances mannose binding lectin (MBL)-associated serine protease (MASP)-1/3 expression in C6 glioma cells.
Glioma
Expression of H-ficolin/Hakata antigen, mannose-binding lectin-associated serine protease (MASP)-1 and MASP-3 by human glioma cell line T98G.
Glomerulonephritis
Glomerular deposition of mannose-binding lectin (MBL) indicates a novel mechanism of complement activation in IgA nephropathy.
Heart Arrest
The complement lectin pathway after cardiac arrest.
Hepatitis C
Mannan binding lectin-associated serine protease 1 is induced by hepatitis C virus infection and activates human hepatic stellate cells.
Hyperglycemia
Comprehensive transcriptome analysis of colorectal cancer risk of hyperglycemia in humans.
Hypertension
MASPs at the crossroad between the complement and the coagulation cascades - the case for COVID-19.
Infections
Circulating levels of mannan-binding lectin (MBL) and MBL-associated serine protease 2 in endemic pemphigus foliaceus.
Infections
Cleavage of kininogen and subsequent bradykinin release by the complement component: mannose-binding lectin-associated serine protease (MASP)-1.
Infections
Mannan binding lectin-associated serine protease 1 is induced by hepatitis C virus infection and activates human hepatic stellate cells.
Infections
MASP-1 Increases Endothelial Permeability.
Ischemic Stroke
Serine proteases of the complement lectin pathway and their genetic variations in ischaemic stroke.
Leprosy
Adding MASP1 to the lectin pathway-Leprosy association puzzle: Hints from gene polymorphisms and protein levels.
Liver Cirrhosis
Mannan binding lectin-associated serine protease 1 is induced by hepatitis C virus infection and activates human hepatic stellate cells.
Liver Diseases
Mannan binding lectin-associated serine protease 1 is induced by hepatitis C virus infection and activates human hepatic stellate cells.
Lupus Erythematosus, Systemic
Mesangial IgA2 deposits and lectin pathway-mediated complement activation in IgA glomerulonephritis.
Lupus Erythematosus, Systemic
The lectin complement pathway serine proteases (MASPs) represent a possible crossroad between the coagulation and complement systems in thromboinflammation.
Macular Degeneration
Proteomics-based identification and validation of novel plasma biomarkers phospholipid transfer protein and mannan-binding lectin serine protease-1 in age-related macular degeneration.
Mastitis
Polymorphisms of mannose-binding lectin-associated serine protease 1 (MASP1) and its relationship with milk performance traits and complement activity in Chinese Holstein cattle.
Meningitis, Pneumococcal
Mannose-binding lectin-associated serine protease 2 (MASP-2) contributes to poor disease outcome in humans and mice with pneumococcal meningitis.
Mucocutaneous Lymph Node Syndrome
Plasma MASP-1 concentration and its relationship to recovery from coronary artery lesion in children with Kawasaki disease.
Myocardial Infarction
Association between endogenous complement inhibitor and myocardial salvage in patients with myocardial infarction.
Neoplasms
Comprehensive Identification of the Human Secretome as Potential Indicators in Treatment Outcome of HPV-Positive and -Negative Cervical Cancer Patients.
Neoplasms
Mannose-Binding Lectin (MBL) and MBL-associated serine protease-2 (MASP-2) in women with malignant and benign ovarian tumours.
Neoplasms
MASP-1 and MASP-2 Serum Levels Are Associated With Worse Prognostic in Cervical Cancer Progression.
Ovarian Neoplasms
Mannose-Binding Lectin (MBL) and MBL-associated serine protease-2 (MASP-2) in women with malignant and benign ovarian tumours.
Peptic Ulcer
Protective effect and mechanisms of action of Mongolian medicine Sulongga-4 on pyloric ligation-induced gastroduodenal ulcer in rats.
Pre-Eclampsia
Polymorphisms in complement genes and risk of preeclampsia in Taiyuan, China.
Prediabetic State
MASP1, THBS1, GPLD1 and ApoA-IV are novel biomarkers associated with prediabetes: the KORA F4 study.
Proteinuria
Clinical Value of Complement Activation Biomarkers in Overt Diabetic Nephropathy.
Pulmonary Disease, Chronic Obstructive
MASPs at the crossroad between the complement and the coagulation cascades - the case for COVID-19.
Renal Insufficiency, Chronic
MASPs at the crossroad between the complement and the coagulation cascades - the case for COVID-19.
Sepsis
MASP-1 of the complement system alters fibrinolytic behaviour of blood clots.
Sepsis
Reduced Mannose-Binding Lectin-Associated Serine Protease (MASP)-1 is Associated with Disturbed Coagulation in Septic Shock.
Shock, Septic
Reduced Mannose-Binding Lectin-Associated Serine Protease (MASP)-1 is Associated with Disturbed Coagulation in Septic Shock.
Stroke
Plasma levels of mannan-binding lectin (MBL)-associated serine proteases (MASPs) and MBL-associated protein in cardio- and cerebrovascular diseases.
Stroke
Serine proteases of the complement lectin pathway and their genetic variations in ischaemic stroke.
Thrombosis
Mannose-binding lectin-associated serine protease-1 is a significant contributor to coagulation in a murine model of occlusive thrombosis.
Thrombosis
MASP-1 of the complement system alters fibrinolytic behaviour of blood clots.
Thrombosis
Plasma levels of mannan-binding lectin (MBL)-associated serine proteases (MASPs) and MBL-associated protein in cardio- and cerebrovascular diseases.
Thrombosis
Targeted sequencing to identify novel genetic risk factors for deep vein thrombosis: a study of 734 genes.
Uterine Cervical Neoplasms
Comprehensive Identification of the Human Secretome as Potential Indicators in Treatment Outcome of HPV-Positive and -Negative Cervical Cancer Patients.
Uterine Cervical Neoplasms
MASP-1 and MASP-2 Serum Levels Are Associated With Worse Prognostic in Cervical Cancer Progression.
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malfunction
enzyme-deficient mice lack alternative pathway activation because factor D remains as a proenzyme in the serum
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
influence of buffer composition on the activity of the alternative pathway of complement activation in mice in the presence and the absence of the Masp1 gene products: MASP-1, MASP-3, and MAp44
metabolism
MASP-1 is a protease of the lectin pathway of complement
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
metabolism
the enzyme is part of the lectin pathway complement cascade, that is part of the innate immune system responsible for the initiation of inflammation and elimination of invading foreign cells
physiological function
-
MASP-1 does not require binding to mannose binding lectin-A, mannose binding lectin-C, or ficolin-A to activate the alternative pathway of complement
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 and MASP-3 seem to be involved in activation of both the lectin and alternative complement system pathways
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 mannose-binding lectin-associated serine protease-1 is a significant contributor to coagulation in a murine model of occlusive thrombosis, it plays a key role in thrombus formation in vitro and in vivo. Whole blood aggregation demonstrated increased mannose-binding lectin-mannose-binding lectin-associated serine protease complex-dependent platelet aggregation
physiological function
the pro-factor D cleaving activity of MASP-1/-3 is not required for alternative pathway function, overview
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
-
in cells over-expressing gcMASP-1, transcript levels of almost all immune components, except gcMBL and gcC5, are significantly enhanced, and gcIL1beta, gcTNF-alpha, gcIFN, gcCD59, gcC5aR1, and gcITGb-2 are significantly upregulated after exposure to Aeromonas hydrophila. MASP-1 interference downregulates the transcript levels after Aeromonas hydrophila challenge. In addition, gcMASP-1 activates NF-kappaB signaling
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
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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)
brenda
La Bonte, L.; Pavlov, V.; Tan, Y.; Takahashi, K.; Takahashi, M.; Banda, N.; Zou, C.; Fujita, T.; Stahl, G.
Mannose-binding lectin-associated serine protease-1 is a significant contributor to coagulation in a murine model of occlusive thrombosis
J. Immunol.
188
885-891
2012
Mus musculus (P98064), Mus musculus
brenda
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)
brenda
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)
brenda
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
brenda
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)
brenda
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
brenda
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)
brenda
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)
brenda
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
brenda
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
brenda
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
brenda
Dang, Y.F.; Shen, Y.B.; Xu, X.Y.; Wang, S.T.; Meng, X.Z.; Li, L.S.; Zhang, M.; Hu, M.Y.; Lv, L.Q.; Wang, R.Q.; Li, J.L.
Mannan-binding lectin-associated serine protease-1 (MASP-1) mediates immune responses against Aeromonas hydrophila invitro and invivo in grass carp
Fish Shellfish Immunol.
66
93-102
2017
Ctenopharyngodon idella
brenda
Mu, L.; Yin, X.; Wu, H.; Han, K.; Wu, L.; Ding, M.; Bian, X.; Li, B.; Fu, S.; Liang, F.; Guo, Z.; Ye, J.
Expression and functional characterization of a mannose-binding lectin-associated serine protease-1 (MASP-1) from Nile tilapia (Oreochromis niloticus) in host defense against bacterial infection
Fish Shellfish Immunol.
91
68-77
2019
Oreochromis niloticus
brenda
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
brenda
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)
brenda
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
brenda
Jenny, L.; Dobo, J.; Gal, P.; Schroeder, V.
MASP-1 induced clotting - the first model of prothrombin activation by MASP-1
PLoS ONE
10
e0144633
2015
Homo sapiens (P48740)
brenda
Nan, R.; Furze, C.M.; Wright, D.W.; Gor, J.; Wallis, R.; Perkins, S.J.
Flexibility in mannan-binding lectin-associated serine proteases-1 and -2 provides insight on lectin pathway activation
Structure
25
364-375
2017
Rattus norvegicus (Q8CHN8)
brenda