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4,4'-dithiopyridine + H2O
?
-
-
-
?
Abz-GLQRALEI-Lys(Dnp)-NH2 + H2O
?
-
-
-
-
?
Abz-SLGRKIQI-Lys(Dnp)-NH2 + H2O
?
-
-
-
-
?
alpha-N-benzyloxycarbonyl-L-lysine thiobenzyl ester + H2O
?
-
-
-
?
benzyloxycarbonyl-Gly-Arg-S-benzyl + H2O
?
-
-
-
?
C1-inhibitor P4-P1 fragment + H2O
?
-
-
-
-
?
C1-inhibitor P4-P4' fragment + H2O
?
-
-
-
-
?
C2 complement component + H2O
?
-
-
-
-
?
C4 complement component + H2O
?
complement component C2 + H2O
2 fragments of complement component C2
complement component C2 + H2O
?
complement component C2 + H2O
complement component C2a + complement component C2b
-
-
-
?
complement component C2 + H2O
complement component C2b + ?
complement component C2 P4-P1 fragment + H2O
?
-
-
-
-
?
complement component C2 P4-P4' fragment + H2O
?
-
-
-
-
?
complement component C3 + H2O
?
complement component C3 + H2O
complement component C3b + ?
-
-
-
-
?
complement component C3i + H2O
?
-
-
-
?
complement component C4 + H2O
2 fragments of complement C4
complement component C4 + H2O
?
complement component C4 + H2O
complement component C4-alpha + complement component C4-alpha'
-
-
-
?
complement component C4 + H2O
complement component C4b
37°C
-
-
?
complement component C4 + H2O
complement component C4b + ?
complement component C4 P4-P1 fragment + H2O
?
-
-
-
-
?
complement component C4 P4-P4' fragment + H2O
?
-
-
-
-
?
factor XIII + H2O
factor XIIIa + ?
-
-
-
-
?
fibrinogen + H2O
fibrin + ?
-
-
-
-
?
Ile-Ala-Arg 4-nitroanilide + H2O
?
-
-
-
?
N-acetylglycine-L-lysine methyl ester + H2O
?
-
-
-
?
N-alpha-benzyloxycarbonyl-L-lysine thiobenzyl ester + H2O
?
-
-
-
-
?
N-carboxybenzoylglycine-L-arginine thiobenzyl ester + H2O
?
-
-
-
?
N-tert-butyloxycarbonyl-L-Leu-Gly-L-Arg-7-amido-4-methylcoumarin + H2O
tert-butyloxycarbonyl-L-Leu-Gly-L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
Nalpha-benzoyl-L-arginine ethyl ester + H2O
?
-
-
-
?
Nalpha-carbobenzoxy-L-lysine-4-nitrophenyl ester + H2O
?
-
-
-
?
p-tosyl-L-arginine methyl ester + H2O
?
-
-
-
?
Phe-Gly-Arg-7-amido-4-methylcoumarin + H2O
Phe-Gly-Arg + 7-amino-4-methylcoumarin
-
recombinant enzyme, low activity
-
-
?
Phe-Pro-Arg-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
Phe-Ser-Arg-7-amido-4-methylcoumarin + H2O
Phe-Ser-Arg + 7-amino-4-methylcoumarin
-
recombinant enzyme, low activity
-
-
?
plasminogen + H2O
plasmin + propeptide of thrombin
prekallikrein + H2O
kallikrein + propeptide of thrombin
prothrombin + H2O
thrombin + ?
-
-
-
-
?
prothrombin + H2O
thrombin + propeptide of thrombin
Val-Leu-Lys-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
additional information
?
-
C4 complement component + H2O
?
-
-
-
?
C4 complement component + H2O
?
-
-
-
-
?
complement component C2 + H2O
2 fragments of complement component C2
-
-
-
-
?
complement component C2 + H2O
2 fragments of complement component C2
-
-
-
?
complement component C2 + H2O
2 fragments of complement component C2
-
-
formation of the C3 convertase C4b2a
-
?
complement component C2 + H2O
2 fragments of complement component C2
-
involved in lectin pathway being part of the innate immune system providing a first line of defense against infections by activation of the complement cascade
-
-
?
complement component C2 + H2O
2 fragments of complement component C2
-
human substrate
-
-
?
complement component C2 + H2O
2 fragments of complement component C2
-
involved in activation of complement cascade
-
-
?
complement component C2 + H2O
2 fragments of complement component C2
-
only the activated enzyme binds to C2-component
C2a and C2b fragments, preferred substrate
-
?
complement component C2 + H2O
?
-
-
-
-
?
complement component C2 + H2O
?
-
-
-
?
complement component C2 + H2O
?
-
-
-
-
?
complement component C2 + H2O
?
-
-
-
?
complement component C2 + H2O
?
-
the complement C3 convertase C4bC2b is generated by cleavage of complement C4 and complement C2
-
?
complement component C2 + H2O
?
-
activates complement C2
-
?
complement component C2 + H2O
?
-
SP domain alone can autoactivate and cleave C2
-
?
complement component C2 + H2O
?
37°C
the complement C3 convertase C4bC2b is generated by cleavage of complement C4 and complement C2
-
?
complement component C2 + H2O
?
formation of C3 convertase C4b2a
-
-
?
complement component C2 + H2O
?
-
-
-
-
?
complement component C2 + H2O
?
-
formation of C3 convertase C4b2a
-
-
?
complement component C2 + H2O
?
-
-
-
-
?
complement component C2 + H2O
?
-
-
-
?
complement component C2 + H2O
?
-
the complement C3 convertase C4bC2b is generated by cleavage of complement C4 and complement C2
-
?
complement component C2 + H2O
complement component C2b + ?
-
-
-
-
?
complement component C2 + H2O
complement component C2b + ?
-
-
-
-
?
complement component C3 + H2O
?
-
-
-
?
complement component C3 + H2O
?
-
-
-
?
complement component C3 + H2O
?
-
very weak substrate
-
?
complement component C4 + H2O
2 fragments of complement C4
-
-
-
-
?
complement component C4 + H2O
2 fragments of complement C4
-
-
-
?
complement component C4 + H2O
2 fragments of complement C4
-
-
formation of the C3 convertase C4b2a
-
?
complement component C4 + H2O
2 fragments of complement C4
-
-
a fragment corresponding to C4b with appearance of the alpha'-chain
-
?
complement component C4 + H2O
2 fragments of complement C4
-
involved in lectin pathway being part of the innate immune system providing a first line of defense against infections by activation of the complement cascade
-
-
?
complement component C4 + H2O
2 fragments of complement C4
-
human substrate
-
-
?
complement component C4 + H2O
2 fragments of complement C4
the complement control protein CCP module is essential for cleavage
-
-
?
complement component C4 + H2O
2 fragments of complement C4
-
-
-
-
?
complement component C4 + H2O
2 fragments of complement C4
-
activated MBL-MASP-2 complex
-
-
?
complement component C4 + H2O
2 fragments of complement C4
-
involved in activation of complement cascade
-
-
?
complement component C4 + H2O
2 fragments of complement C4
-
no activity of the enzyme complexed with myelin basic protein before complex activation by binding to a suitable carbohydrate ligand
C4a fragment, an N-terminal portion, and C4b fragment, the activated form
-
?
complement component C4 + H2O
?
-
-
-
-
?
complement component C4 + H2O
?
-
-
-
?
complement component C4 + H2O
?
-
-
-
?
complement component C4 + H2O
?
-
-
-
?
complement component C4 + H2O
?
-
-
-
-
?
complement component C4 + H2O
?
-
-
-
?
complement component C4 + H2O
?
-
the complement C3 convertase C4bC2b is generated by cleavage of complement C4 and complement C2
-
?
complement component C4 + H2O
?
-
SP domain is able to cleave C4, but the presence of the CCP2 domain significantly increases the efficiency
-
?
complement component C4 + H2O
?
37°C
the complement C3 convertase C4bC2b is generated by cleavage of complement C4 and complement C2
-
?
complement component C4 + H2O
?
exclusively cleaves complement C4
-
-
?
complement component C4 + H2O
?
-
activation to C4b
-
-
?
complement component C4 + H2O
?
-
determination of C4b deposition on a mannan surface
-
-
?
complement component C4 + H2O
?
formation of C3 convertase C4b2a
-
-
?
complement component C4 + H2O
?
-
-
-
-
?
complement component C4 + H2O
?
-
formation of C3 convertase C4b2a
-
-
?
complement component C4 + H2O
?
-
-
-
-
?
complement component C4 + H2O
?
-
-
-
?
complement component C4 + H2O
?
-
the complement C3 convertase C4bC2b is generated by cleavage of complement C4 and complement C2
-
?
complement component C4 + H2O
complement component C4b + ?
-
-
-
?
complement component C4 + H2O
complement component C4b + ?
no formation of C4i
-
-
?
complement component C4 + H2O
complement component C4b + ?
-
-
-
-
?
plasminogen + H2O
plasmin + propeptide of thrombin
-
-
-
-
?
plasminogen + H2O
plasmin + propeptide of thrombin
-
activation
-
-
?
prekallikrein + H2O
kallikrein + propeptide of thrombin
-
-
-
-
?
prekallikrein + H2O
kallikrein + propeptide of thrombin
-
activation
-
-
?
Protein + H2O
?
-
-
-
?
Protein + H2O
?
-
cleaves oligopeptides that contain either Arg or Lys at their P1 positions
-
?
Protein + H2O
?
enzyme circulates as a complex with mannose-binding protein, minimal functional unit for complement activation is a ASP homodimer bound to two mannose-binding protein trimeric subunits, complex is formed more readily in the presence of Ca2+
-
?
prothrombin + H2O
thrombin + propeptide of thrombin
-
activation of thrombin covalentyl bound to a bacterial cell surface
-
-
?
prothrombin + H2O
thrombin + propeptide of thrombin
-
cleavage scheme, overview
-
-
?
additional information
?
-
MASP-2 is associated with two mannose-binding lectin homologues, one, designated GalBL, corresponds to the MBL-like molecule with the galactose specificity, the other is an authentic MBL with mannose specificity, overview, bony fish have developed a diverged set of MBL homologs, which function in the lectin complement pathway
-
-
?
additional information
?
-
-
MASP-2 is associated with two mannose-binding lectin homologues, one, designated GalBL, corresponds to the MBL-like molecule with the galactose specificity, the other is an authentic MBL with mannose specificity, overview, bony fish have developed a diverged set of MBL homologs, which function in the lectin complement pathway
-
-
?
additional information
?
-
-
hardly any detectable activity on complement C3
-
?
additional information
?
-
-
complement C3 is not a natural substrate
-
?
additional information
?
-
-
L-ficolin/P35 competes with mannose-binding protein for Ca2+-dependent binding to MASP-2, complex activates complement
-
?
additional information
?
-
-
smallest functional unit for complement activation consists of mannose-binding protein dimers bound to MASP-2 homodimers
-
?
additional information
?
-
-
enzyme in serum is complexed with mannan-binding lectin MBL and ficolins
-
-
?
additional information
?
-
-
enzyme is complexed with the mannose-binding protein, a recognition molecule for the complement pathway
-
-
?
additional information
?
-
-
enzyme is Mg2+-dependently associated with the mannose-binding protein, a C-type lectin binding to terminal mannose and N-acetylglucosamine moieties on surfaces of certain pathogens and activating the classical complement pathway, the enzyme is not identical with C1r or C1s
-
-
?
additional information
?
-
-
substrate specificity, fluorescent amide compounds are poor substrates, overview
-
-
?
additional information
?
-
-
binding of MBL or ficolins to the cell surface carbohydrates of microbes initiates MASP activation, autoactivation of MASP-2 is the first step in the complement cascade, overview
-
-
?
additional information
?
-
binding of MBL or ficolins to the cell surface carbohydrates of microbes initiates MASP activation, autoactivation of MASP-2 is the first step in the complement cascade, overview
-
-
?
additional information
?
-
-
MASP-2 is a central component of the MBL pathway of complement activation, MBL and MASP-2 levels in serum and plasma of healthy individuals are similar and independent of gender and age, while they are increased in colorectal cancer patients, overview
-
-
?
additional information
?
-
-
the enzyme binds to the mannan-binding lectin, MBL, the complex activates the lectin pathway of the complement system, overview
-
-
?
additional information
?
-
-
the enzyme binds to the mannan-binding lectin, the complex activates the lectin pathway of the complement system, increased activity of MBL-bound MASP-2 and MASP-2-mediated complement activation in schizophrenia, while the levels of MASP-1 and unbound MBL are similar to healthy persons' levels, overview
-
-
?
additional information
?
-
-
the enzyme binds to the mannan-binding lectin, the complex activates the lectin pathway of the complement system, MASP-2 is the major protease of the lectin pathway besides MASP-1 and the minor component MASP-3, autoactivation of MASP-2 is the first step in the complement cascade, MASP-3 might be able to downregulate MASP-2 activity, overview
-
-
?
additional information
?
-
-
the enzyme binds to the mannan-binding lectin, the complex activates the lectin pathway of the complement system, overview
-
-
?
additional information
?
-
-
the enzyme binds to the mannan-binding lectin, the complex activates the lectin pathway of the complement system, overview
-
-
?
additional information
?
-
-
the lectin pathway is one of the ways leading to the cleavage of complement factor C3, a central event in the activation of the complement system, mannan-binding lectin, MBL, promotes the activation of C3 through the combined action of MASP-1 and MASP-2 without appreciable involvement of the alternative pathway, protease MASP-1 collaborates with MASP-2 in the generation of C3 convertase, overview
-
-
?
additional information
?
-
-
the lectin pathway of complement plays a key role in the immune system by recognising pathogens through patterns of sugar moities displayed on their cell sufaces and neutralizing them in an antibody-independent reaction cascade, MASP-2 binds to the mannan-binding lectin, MBL, the complex activates the lectin pathway of the complement system, interactions analysis, overview
-
-
?
additional information
?
-
-
development and evaluation of a fluorochrome-linked immunoassay for quantitative determination of MBL, MASP-2 and C3 convertase activity in serum samples, overview
-
-
?
additional information
?
-
-
MASP-2 acts in complex with mannan-binding lectin, MBL, overview
-
-
?
additional information
?
-
-
substrate specificity of MASP-2, overview
-
-
?
additional information
?
-
-
substrate specificity, overview, no activity with gelatin, the enzyme performs proteolytic autoactivation, the N-terminal third of MASP-2, i.e. MAp19 or sMAp, comprises the CUB1 and EGF modules of MASP-2 plus an extra C-terminal EQSL tetrapeptide, which is encoded by a separate exon, MAp19 is a product of alternative splicing of the MASP-2 gene and is catalytically inactive
-
-
?
additional information
?
-
-
the enzyme performs proteolytic autoactivation, mannan-binding lectin, MBL, structure and Ca2+-dependent interaction with the enzyme, overview, MAp19 is a product of alternative splicing of the MASP-2 gene and is catalytically inactive, overview
-
-
?
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-2 has all the activities required for lectin pathway activation, it can autoactivate and cleave both complement components C4 and C2
-
-
?
additional information
?
-
-
binding of MBL or ficolins to the cell surface carbohydrates of microbes initiates MASP activation, autoactivation of MASP-2 is the first step in the complement cascade, overview
-
-
?
additional information
?
-
-
the enzyme binds to the mannan-binding lectin, the complex activates the lectin pathway of the complement system, overview, a truncated form of MASP-2, named small MBL-associated protein, sMAP, is also associated with MBL/ficolin-MASP complexes, MASP-2 is essential for the activation of C4 and sMAP plays a regulatory role in the activation of the lectin pathway, overview
-
-
?
additional information
?
-
-
MASP-2 acts in complex with mannan-binding lectin, MBL, a truncated form of MASP-2, named small MBL-associated protein, sMAP, is also associated with MBL/ficolin-MASP complexes, overview
-
-
?
additional information
?
-
no substrate: complement factor D
-
-
?
additional information
?
-
-
substrate specificity, overview
-
-
?
additional information
?
-
-
the enzyme binds to the mannan-binding lectin, the complex activates the lectin pathway of the complement system, MASP-2 is the major protease of the lectin pathway besides MASP-1 and the minor component MASP-3, autoactivation of MASP-2 is the first step in the complement cascade, MASP-3 might be able to downregulate MASP-2 activity, overview
-
-
?
additional information
?
-
-
the enzyme is part of the lectin pathway of the complement system, it is also capable of promoting fibrinogen turnover by cleavage of prothrombin, generating thrombin
-
-
?
additional information
?
-
-
MASP-2 interactions with wild-type and mutant ficolins, overview
-
-
?
additional information
?
-
-
MASP2 acts in a mannan-bound MBL/MASP2 complex
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
C2 complement component + H2O
?
-
-
-
-
?
C4 complement component + H2O
?
-
-
-
-
?
complement component C2 + H2O
2 fragments of complement component C2
complement component C2 + H2O
?
complement component C2 + H2O
complement component C2b + ?
-
-
-
-
?
complement component C4 + H2O
2 fragments of complement C4
complement component C4 + H2O
?
complement component C4 + H2O
complement component C4b + ?
-
-
-
?
factor XIII + H2O
factor XIIIa + ?
-
-
-
-
?
fibrinogen + H2O
fibrin + ?
-
-
-
-
?
plasminogen + H2O
plasmin + propeptide of thrombin
-
activation
-
-
?
prekallikrein + H2O
kallikrein + propeptide of thrombin
-
activation
-
-
?
prothrombin + H2O
thrombin + ?
-
-
-
-
?
prothrombin + H2O
thrombin + propeptide of thrombin
-
activation of thrombin covalentyl bound to a bacterial cell surface
-
-
?
additional information
?
-
complement component C2 + H2O
2 fragments of complement component C2
-
-
-
-
?
complement component C2 + H2O
2 fragments of complement component C2
-
-
-
?
complement component C2 + H2O
2 fragments of complement component C2
-
-
formation of the C3 convertase C4b2a
-
?
complement component C2 + H2O
2 fragments of complement component C2
-
involved in lectin pathway being part of the innate immune system providing a first line of defense against infections by activation of the complement cascade
-
-
?
complement component C2 + H2O
2 fragments of complement component C2
-
involved in activation of complement cascade
-
-
?
complement component C2 + H2O
?
-
-
-
?
complement component C2 + H2O
?
-
-
-
-
?
complement component C2 + H2O
?
-
-
-
-
?
complement component C2 + H2O
?
-
-
-
-
?
complement component C2 + H2O
?
-
-
-
?
complement component C4 + H2O
2 fragments of complement C4
-
-
-
-
?
complement component C4 + H2O
2 fragments of complement C4
-
-
-
?
complement component C4 + H2O
2 fragments of complement C4
-
-
formation of the C3 convertase C4b2a
-
?
complement component C4 + H2O
2 fragments of complement C4
-
involved in lectin pathway being part of the innate immune system providing a first line of defense against infections by activation of the complement cascade
-
-
?
complement component C4 + H2O
2 fragments of complement C4
-
-
-
-
?
complement component C4 + H2O
2 fragments of complement C4
-
involved in activation of complement cascade
-
-
?
complement component C4 + H2O
?
-
-
-
?
complement component C4 + H2O
?
-
-
-
-
?
complement component C4 + H2O
?
-
activation to C4b
-
-
?
complement component C4 + H2O
?
-
-
-
-
?
complement component C4 + H2O
?
-
-
-
-
?
complement component C4 + H2O
?
-
-
-
?
Protein + H2O
?
-
-
-
?
Protein + H2O
?
enzyme circulates as a complex with mannose-binding protein, minimal functional unit for complement activation is a ASP homodimer bound to two mannose-binding protein trimeric subunits, complex is formed more readily in the presence of Ca2+
-
?
additional information
?
-
MASP-2 is associated with two mannose-binding lectin homologues, one, designated GalBL, corresponds to the MBL-like molecule with the galactose specificity, the other is an authentic MBL with mannose specificity, overview, bony fish have developed a diverged set of MBL homologs, which function in the lectin complement pathway
-
-
?
additional information
?
-
-
MASP-2 is associated with two mannose-binding lectin homologues, one, designated GalBL, corresponds to the MBL-like molecule with the galactose specificity, the other is an authentic MBL with mannose specificity, overview, bony fish have developed a diverged set of MBL homologs, which function in the lectin complement pathway
-
-
?
additional information
?
-
-
complement C3 is not a natural substrate
-
?
additional information
?
-
-
L-ficolin/P35 competes with mannose-binding protein for Ca2+-dependent binding to MASP-2, complex activates complement
-
?
additional information
?
-
-
smallest functional unit for complement activation consists of mannose-binding protein dimers bound to MASP-2 homodimers
-
?
additional information
?
-
-
enzyme in serum is complexed with mannan-binding lectin MBL and ficolins
-
-
?
additional information
?
-
-
enzyme is complexed with the mannose-binding protein, a recognition molecule for the complement pathway
-
-
?
additional information
?
-
-
enzyme is Mg2+-dependently associated with the mannose-binding protein, a C-type lectin binding to terminal mannose and N-acetylglucosamine moieties on surfaces of certain pathogens and activating the classical complement pathway, the enzyme is not identical with C1r or C1s
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additional information
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binding of MBL or ficolins to the cell surface carbohydrates of microbes initiates MASP activation, autoactivation of MASP-2 is the first step in the complement cascade, overview
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additional information
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binding of MBL or ficolins to the cell surface carbohydrates of microbes initiates MASP activation, autoactivation of MASP-2 is the first step in the complement cascade, overview
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additional information
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MASP-2 is a central component of the MBL pathway of complement activation, MBL and MASP-2 levels in serum and plasma of healthy individuals are similar and independent of gender and age, while they are increased in colorectal cancer patients, overview
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additional information
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the enzyme binds to the mannan-binding lectin, MBL, the complex activates the lectin pathway of the complement system, overview
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additional information
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the enzyme binds to the mannan-binding lectin, the complex activates the lectin pathway of the complement system, increased activity of MBL-bound MASP-2 and MASP-2-mediated complement activation in schizophrenia, while the levels of MASP-1 and unbound MBL are similar to healthy persons' levels, overview
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additional information
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the enzyme binds to the mannan-binding lectin, the complex activates the lectin pathway of the complement system, MASP-2 is the major protease of the lectin pathway besides MASP-1 and the minor component MASP-3, autoactivation of MASP-2 is the first step in the complement cascade, MASP-3 might be able to downregulate MASP-2 activity, overview
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additional information
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the enzyme binds to the mannan-binding lectin, the complex activates the lectin pathway of the complement system, overview
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additional information
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the enzyme binds to the mannan-binding lectin, the complex activates the lectin pathway of the complement system, overview
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additional information
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the lectin pathway is one of the ways leading to the cleavage of complement factor C3, a central event in the activation of the complement system, mannan-binding lectin, MBL, promotes the activation of C3 through the combined action of MASP-1 and MASP-2 without appreciable involvement of the alternative pathway, protease MASP-1 collaborates with MASP-2 in the generation of C3 convertase, overview
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additional information
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the lectin pathway of complement plays a key role in the immune system by recognising pathogens through patterns of sugar moities displayed on their cell sufaces and neutralizing them in an antibody-independent reaction cascade, MASP-2 binds to the mannan-binding lectin, MBL, the complex activates the lectin pathway of the complement system, interactions analysis, overview
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additional information
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MBL-MASP complexes, bound to mannan-agarose, generate clots when incubated with calcified plasma or purified fibrinogen and factor XIII
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additional information
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MASP-2 has all the activities required for lectin pathway activation, it can autoactivate and cleave both complement components C4 and C2
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additional information
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binding of MBL or ficolins to the cell surface carbohydrates of microbes initiates MASP activation, autoactivation of MASP-2 is the first step in the complement cascade, overview
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additional information
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the enzyme binds to the mannan-binding lectin, the complex activates the lectin pathway of the complement system, overview, a truncated form of MASP-2, named small MBL-associated protein, sMAP, is also associated with MBL/ficolin-MASP complexes, MASP-2 is essential for the activation of C4 and sMAP plays a regulatory role in the activation of the lectin pathway, overview
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additional information
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the enzyme binds to the mannan-binding lectin, the complex activates the lectin pathway of the complement system, MASP-2 is the major protease of the lectin pathway besides MASP-1 and the minor component MASP-3, autoactivation of MASP-2 is the first step in the complement cascade, MASP-3 might be able to downregulate MASP-2 activity, overview
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additional information
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the enzyme is part of the lectin pathway of the complement system, it is also capable of promoting fibrinogen turnover by cleavage of prothrombin, generating thrombin
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2015
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Homo sapiens (O00187)
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59
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Homo sapiens (O00187)
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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
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227-232
2015
Homo sapiens (O00187)
brenda
Yaseen, S.; Demopulos, G.; Dudler, T.; Yabuki, M.; Wood, C.L.; Cummings, W.J.; Tjoelker, L.W.; Fujita, T.; Sacks, S.; Garred, P.; Andrew, P.; Sim, R.B.; Lachmann, P.J.; Wallis, R.; Lynch, N.; Schwaeble, W.J.
Lectin pathway effector enzyme mannan-binding lectin-associated serine protease-2 can activate native complement C3 in absence of C4 and/or C2
FASEB J.
31
2210-2219
2017
Homo sapiens (O00187)
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
Mus musculus (Q91WP0)
brenda
Drentin, N.; Conroy, P.; Gunzburg, M.J.; Pike, R.N.; Wijeyewickrema, L.C.
Investigation of the mechanism of interaction between Mannose-binding lectin-associated serine protease-2 and complement C4
Mol. Immunol.
67
287-293
2015
Homo sapiens (O00187)
brenda
Boldt, A.B.; Beltrame, M.H.; Catarino, S.J.; Meissner, C.G.; Tizzot, R.; Messias-Reason, I.J.
A dual role for Mannan-binding lectin-associated serine protease 2 (MASP-2) in HIV infection
Mol. Immunol.
78
48-56
2016
Homo sapiens (O00187), Homo sapiens
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 (Q9JJS8)
brenda
Ojurongbe, O.; Antony, J.S.; Van Tong, H.; Meyer, C.G.; Akindele, A.A.; Sina-Agbaje, O.R.; Kremsner, P.G.; Velavan, T.P.
Low MBL-associated serine protease 2 (MASP-2) levels correlate with urogenital schistosomiasis in Nigerian children
Trop. Med. Int. Health
20
1311-1319
2015
Homo sapiens (O00187), Homo sapiens
brenda