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Information on EC 3.4.21.104 - mannan-binding lectin-associated serine protease-2 and Organism(s) Homo sapiens and UniProt Accession O00187
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- 3.4.21.104
-
masps
- spider
-
silk
- ficolins
-
ampullate
-
dragline
-
spidroins
- c1s
- clavipes
- nephila
-
collectins
- m-ficolin
- widow
- hesperus
- latrodectus
- medicine
- molecular biology
- diagnostics
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
Selective cleavage after Arg223 in complement component C2 (-Ser-Leu-Gly-Arg-/-Lys-Ile-Gln-Ile) and after Arg76 in complement component C4 (-Gly-Leu-Gln-Arg-/-Ala-Leu-Glu-Ile)
Synonyms
masp2, map19, mbl-associated serine protease 2, mannan-binding lectin-associated serine protease-2, mbp-associated serine protease, ccp1-ccp2-sp, mannan-binding lectin-associated serine protease 2, mannose-binding lectin-associated serine protease-2, mannose-binding lectin-associated serine protease 2, mannan-binding lectin associated serine protease-2, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
mannan-binding lectin-associated serine protease-2
-
MASP-2
CCP1-CCP2-SP
-
complement control protein-like domain 1-complement control protein-like domain-2-serine protease, catalytic segment of MASP-2
Map19
MASP-2
MBL-associated serine protease-2
MASP-2
-
-
MASP-2
-
protein of the lectin pathway, can autoactivate and cleaves complements C2 and C4
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Selective cleavage after Arg223 in complement component C2 (-Ser-Leu-Gly-Arg-/-Lys-Ile-Gln-Ile) and after Arg76 in complement component C4 (-Gly-Leu-Gln-Arg-/-Ala-Leu-Glu-Ile)
Selective cleavage after Arg223 in complement component C2 (-Ser-Leu-Gly-Arg-/-Lys-Ile-Gln-Ile) and after Arg76 in complement component C4 (-Gly-Leu-Gln-Arg-/-Ala-Leu-Glu-Ile)
catalytic serine residue is located on the light chain subunit
-
Selective cleavage after Arg223 in complement component C2 (-Ser-Leu-Gly-Arg-/-Lys-Ile-Gln-Ile) and after Arg76 in complement component C4 (-Gly-Leu-Gln-Arg-/-Ala-Leu-Glu-Ile)
structure-function analysis of the catalytic unit, enzyme-substrate interaction is different from enzyme C1 which has the same substrate specificity, MASP-2 shows a subsite flexibility in substrate specificity, catalytic residues are Asp526 and His525, active site structure, overview
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
CAS REGISTRY NUMBER
COMMENTARY
214915-16-9
-
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
complement component C2 + H2O
complement component C2a + complement component C2b
-
-
-
?
complement component C4 + H2O
complement component C4-alpha + complement component C4-alpha'
-
-
-
?
N-tert-butyloxycarbonyl-L-Leu-Gly-L-Arg-7-amido-4-methylcoumarin + H2O
tert-butyloxycarbonyl-L-Leu-Gly-L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
Phe-Gly-Arg-7-amido-4-methylcoumarin + H2O
Phe-Gly-Arg + 7-amino-4-methylcoumarin
-
recombinant enzyme, low activity
-
-
?
Phe-Ser-Arg-7-amido-4-methylcoumarin + H2O
Phe-Ser-Arg + 7-amino-4-methylcoumarin
-
recombinant enzyme, low activity
-
-
?
complement component C2 + H2O
?
-
the complement C3 convertase C4bC2b is generated by cleavage of complement C4 and complement C2
-
?
complement component C2 + H2O
?
37°C
the complement C3 convertase C4bC2b is generated by cleavage of complement C4 and complement C2
-
?
complement component C4 + H2O
?
-
the complement C3 convertase C4bC2b is generated by cleavage of complement C4 and complement C2
-
?
complement component C4 + H2O
?
37°C
the complement C3 convertase C4bC2b is generated by cleavage of complement C4 and complement C2
-
?
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
?
-
SP domain alone can autoactivate and cleave C2
-
?
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
?
-
-
-
-
?
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
?
-
determination of C4b deposition on a mannan surface
-
-
?
Protein + H2O
?
-
cleaves oligopeptides that contain either Arg or Lys at their P1 positions
-
?
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, 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
-
-
?
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
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 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
-
-
?
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
?
-
-
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
?
-
-
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
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Ca2+
-
Ca2+-dependent dimerization, Ca2+ is bound to the distal end of the CUB1 module of MAp19 and of MASP-2
Ca2+
-
interaction of MASP-2 with mannan-binding lectin is Ca2+-dependent, the Ca2+-binding site is located in the CUB1 module, overview
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
-
Schistocerca gregaria protease inhibitor-2 variant VCTKLWCN
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. MASP-2 inhibitor variant VCTKLWCN completely blocks the lectin pathway activation
-
anti-thrombin III
-
recombinant enzyme, inhibition only in presence of heparin
-
Kunitz-type inhibitor tissue factor pathway inhibitor
-
selective inhibitor of enzyme Masp-2, without affecting MASP-1 or the classical pathway proteases C1s and C1r. Kunitz-2 domain of the inhibitor is required for the inhibition of MASP-2
-
alpha-2-Macroglobulin
-
forms a stable complex with the enzyme, inhibits at a large molar excess, 40fold
-
alpha-2-Macroglobulin
-
inhibition of recombinant, not native, enzyme at large molar excess
-
C1 inhibitor
-
recombinant enzyme, at pH 7.4, inhibitor from human, the protease-serpin complex in highly unstable at alkaline pH
-
C1-inhibitor
-
forms a stable complex with the enzyme, 1-3fold excess completely inactivates
-
C1-inhibitor
-
forms equimolar complexes with the enzyme and inhibits its proteolytic activity
-
C1-inhibitor
-
linear relationship between inhibition and the molar ratio of inhibitor:enzyme up to about 50% inhibition
-
C1-inhibitor
-
a serpin, purified human protein, enzyme interaction rates and site specificity of the inhibitor, interaction rates under pseudo-first-order conditions, overview
-
additional information
-
no inhibition of recombinant enzyme by thrombin inhibitor Z-D-Phe-Pro-methoxypropylboroglycinepinanediol ester, i.e. boroMpg, and hirudin
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
MASP-2 is activated by the cleavage of the 76-kDa polypeptide chain into a 52-kDa A chain and a 31-kDa B chain
-
mannan-binding lectin
a C-type serum lectin acting as a pattern recognition molecule, associated to MASPs, binding triggers activation of MASPs, overview
-
mannan-binding lectin
-
MBL, binds and activates MASP-2 by increasing the rate of autocatalysis when it binds to an activating surface, interaction of MASP-2 with mannan-binding lectin is Ca2+-dependent, activation mechanism, overview
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0579
Complement component C4
-
catalytic MASP-2 fragment CCP1CCP2SP, in 0.05 M TrisHCl, 0.15 M NaCl, 0.2% (w/v) PEG 8000, 0.02% (w/v) NaN3, pH 7.4 at 37°C
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.27
Abz-GLQRALEI-Lys(Dnp)-NH2
-
catalytic MASP-2 fragment CCP1CCP2SP, in 0.05 M TrisHCl, 0.15 M NaCl, 0.2% (w/v) PEG 8000, 0.02% (w/v) NaN3, pH 7.4 at 37°C
1.92
Abz-SLGRKIQI-Lys(Dnp)-NH2
-
catalytic MASP-2 fragemt CCP1CCP2SP, in 0.05 M TrisHCl, 0.15 M NaCl, 0.2% (w/v) PEG 8000, 0.02% (w/v) NaN3, pH 7.4 at 37°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.058
Schistocerca gregaria protease inhibitor-2 variant FCTRKLCY
pH not specified in the publication, temperature not specified in the publication
-
0.000006
Schistocerca gregaria protease inhibitor-2 variant VCTKLWCN
pH not specified in the publication, temperature not specified in the publication
-
0.00075
cyclic sunflower MASP inhibitor-1
-
in 20 mM HEPES, 140 mM NaCl, and 10 mM CaCl2 (pH 7.4), at 37°C
0.00103
sunflower MASP inhibitor-1
-
in 20 mM HEPES, 140 mM NaCl, and 10 mM CaCl2 (pH 7.4), at 37°C
0.00018
sunflower MASP inhibitor-2
-
in 20 mM HEPES, 140 mM NaCl, and 10 mM CaCl2 (pH 7.4), at 37°C
additional information
additional information
-
first order rate inhibition kinetics
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
activity of recombinant enzyme with substrates Phe-Gly-Arg-7-amido-4-methylcoumarin and Phe-Ser-Arg-7-amido-4-methylcoumarin
additional information
-
development and evaluation of a fluorochrome-linked immunoassay for quantitative determination of MBL, MASP-2 and C3 convertase activity, overview
additional information
-
lectin pathway of the complement system component activities in healthy individuals and schizophrenia patients, overview
additional information
-
MBL and MASP-2 levels in serum and plasma of healthy individuals over a long time period, independent of gender and age, quantitative anaylsis, overview
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
increased MASP-2 expression in comparison with normal tissue
additional information
-
enzyme content in plasma of blood donors during 1 year, overview
expression of the enzyme, both enzyme splicing variants MASP-2 and MAp19
-
-
-
distribution in the investigated twin sample population, modeling, overview
-
cord blood MASP-2 concentrations in a large, ethnically homogeneous cohort of neonates is investigated: Serum MASP-2 concentrations correlate with gestational age and birth weight and are significantly lower in premature babies and other pre-term babies compared with term babies. Neonates with MASP-2 concentrations below 42 ng/ml are deemed to be MASP-2 deficient. That group has a shorter mean gestational age and a higher incidence of premature and low birth weight babies, but not of perinatal infections when compared with the others. There is a trend towards higher MASP-2 concentrations amongst babies with infections
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
MASP-2 is associated with mannan-binding lectin II
-
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
physiological function
mannan-binding lectin-associated serine proteases MASP-1 and MASP-2 can readily form heterodimers after dissociation and re-association, however, in thepresence 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
the addition of mannan-binding lectin or ficolins allows the formation of serine proteases MASP-1-MASP-2 co-complexes. Such co-complexes have a functional role in activating complement and are present in serum at varying levels, impacting on the degree of complement activation. MASP-2 can be found in complex with each of the other MASPs and mannan-binding lectin-associated proteins in serum, and coexpression of MASP-2 with MASP-1, MASP-3, or mannan-binding lectin-associated protein 4 leads to detectable levels of heterodimers
physiological function
two areas outside of the active site of MASP-2 (so-called exosites) are crucial for efficient cleavage of substrate C4 complement component. Both exosites are required for high affinity binding and efficient cleavage of the substrate protein. Within the SP domain exosite, two arginine residues are most important for high affinity binding and efficient cleavage of C4. The CCP domain exosite appears to play the major role in the initial interaction with C4, whilst the SP domain exosite plays the major role in a secondary conformational change between the two proteins required to form a high affinity complex
physiological function
under physiologic conditions lectin pathway-specific complement component C4 and/or C2 bypass activation of C3 is mediated by direct cleavage of native C3 by mannan-binding lectin-associated serine protease-2 bound to lectin pathway-activation complexes captured on ligand-coated surfaces
physiological function
-
MASP-2 is the main initiator of the lectin complement pathway by cleaving C4 and C2 to form the C4b2a complex leading to further downstream complement activation
physiological function
-
the MBL-MASP pathway of complement activation is of importance to innate immunity and to response to pathogens
physiological function
-
MASP-2 acts as acute-phase reactant, but it is neither marker for severity, multiorgan failure, nor for mortality in acute pancreatitis. MASP-2 plays only a minor role in the inflammatory response in acute pancreatitis
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). MASP2_HUMAN
686
0
75702
Swiss-Prot
Secretory Pathway (Reliability: 2)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
29000
-
calculated molecular mass of the MASP-2 CUB-EGF fragment in the presence of Ca2+
31000
50000
-
x * 75000, full-length proenzyme, SDS-PAGE, x * 50000, A-chain of the enzyme, SDS-PAGE
75000
-
x * 75000, full-length proenzyme, SDS-PAGE, x * 50000, A-chain of the enzyme, SDS-PAGE
76000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
dimer
additional information
?
-
x * 75000, full-length proenzyme, SDS-PAGE, x * 50000, A-chain of the enzyme, SDS-PAGE
dimer
-
Ca2+-dependent homodimerization, no formation of heterodimers between MASP-2 and MAp19, even though they share the same N-terminal domains
additional information
recombinant CUB1-EGF-CUB2 regions of MASP-2 show a slow and incomplete dissociation of dimer by EDTA and appearance of high molecular weight aggregates
additional information
-
enzyme in serum is complexed with mannan-binding lectin MBL and ficolins
additional information
enzyme surface segment analysis, structure-function analysis
additional information
-
domain organizations of MASP-2 and mannan-binding lectin, MBL, overview, 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, overview, enzyme structure and domain organization: CUB1 module, EGF module, CUB2 module, CCP1, CCP2, and serine protease domains, the very flexible C-terminal catalytic SP region, active site structure, overview
additional information
-
enzyme structure and domain organization: CUB1 module, EGF module, CUB2 module, CCP1, CCP2, and serine protease domains, overview
additional information
enzyme structure and domain organization: CUB1 module, EGF module, CUB2 module, CCP1, CCP2, and serine protease domains, overview
additional information
-
enzyme structure and domain organization: CUB1 module, EGF module, CUB2 module, CCP1, CCP2, and serine protease domains, the very flexible C-terminal catalytic SP region shows a typical chymotrypsin fold with two six-stranded beta-barrels with the catalytic triad located at the junction of the to barrels and formed by Ser195, His57, and Asp102, active site structure, overview
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
no glycoprotein
proteolytic modification
proteolytic modification
-
the enzyme performs autoactivation, C4 binding to the zymogen stabilizes the activating enzyme, overview
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in complex with Schistocerca gregaria protease inhibitor-2 variant VCTKLWCN, to 1.28 A resolution. Strucutre reveals significant plasticity of the protease
C-terminal catalytic region of MASP-2, X-ray diffraction structure determination and anaylsis
-
catalytic fragment encompassing the second complement control protein module and the serine protease domain, in presence of Na+, in absence of Mg2+, 0.8 mg/ml purified recombinant protein in 140 mM NaCl, 20 mM Tris-HCl, pH 7.4, and 0.05% w/v NaN3, hanging drop vapour diffusion method at 20°C, mixing with equal volume of reservoir solution containing 30% w/v PEG 6000, 0.2 M NaCl, 10% v/v glycerol, 0.1 M Tris-HCl, pH 7.5, X-ray diffraction structure determination and analysis at 2.25 A resolution
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C1s(MASP-2CCP1/2)
hybrid C1s/MASP-2 molecule, swapped complement control protein, 21-27fold higher kcat/Km-ratio for complement C4 than C1s(MASP-2SP)
C1s(MASP-2SP)
hybrid C1s/MASP-2 molecule, swapped serine protease, 21-27fold lower kcat/Km-ratio for complement C4 than C1s(MASP-2CCP1/2)
D105G
P111L
found in 4% of studied North Africans, not found in Sub-Saharans and Spaniards
R103C
found in 2% of studied North Africans, not found in Sub-Saharans and Spaniards
R84Q
found in 13.33% of studied Sub-Saharans, 1% of studied North Africans, not found in Spaniards
D105G
D120G
H155R
-
the mutant cleaves complement component C4 slightly better than the wild type MASP-2
P126L
-
the mutant cleaves complement component C4 with an activity comparable to wild type MASP-2
R439H
-
the mutant is deficient in cleavage of complement component C4 despite its normal binding to mannan-binding lectin, the mutant is not able to autoactivate in the presence of mannan-binding lectin and mannan
R99Q
-
the mutant cleaves complement component C4 with an activity comparable to wild type MASP-2
V377A
-
the mutant cleaves complement component C4 with an activity comparable to wild type MASP-2
additional information
D105G
inactive, MASP-2 deficiency, the index case suffers from recurrent severe infections and autoimmune reactions
D105G
incapable of forming a complex with mannan-binding lectin, found in 1.44% of studied Spaniards, 2% of studied North Africans, not found in Sub-Saharans
D105G
-
it is investigated whether partial or total MASP-2 deficiencies resulting from D105G mutation are associated with rheumatic fever and chronic rheumatic heart disease: 148 patients are analyzed with a history of rheumatic fever, including 106 with chronic rheumatic heart and 42 without cardiac sequelae, and 129 control subjects. The D105G mutation is detected in four patients with chronic rheumatic heart and in five control subjects , all in the heterozygous state. None of the patients without cardiac sequelae has the mutation. No significant difference is found in the frequency of the mutant allele between the groups. D105G mutation in the MASP2 gene does not play a major role in the pathogenesis of rheumatic fever
D105G
-
the mutation causes impaired binding to mannan-binding lectin and low circulating plasma levels of MASP-2
D120G
-
among 362 samples tested for the D120G single nucleotide polymorphism of the MASP2 gene, no homozygote for that mutation is found. Heterozygosity for this allele significantly influences the protein concentration, but not the lectin pathway of complement activity (MBL-MASP-2 complex activity). No association of this single nucleotide polymorphism is apparent with prematurity, low birth weight or perinatal infections
D120G
-
when D120G is mixed with mannan-binding lectin, no activation of complement component C4 is observed
additional information
-
serum depleted of MASP-1, MASP-2 and MASP-3, shows synergetic effect of reconstitution with MASP-1 and MASP-2, overview
additional information
-
transcription activity is decreased 5fold when the StatB binding site of the MASP-2 promoter is mutated in the wild-type reporter gene construct
additional information
-
when the mutant enzyme 156_159dupCHNH (CHNHdup) is mixed with mannan-binding lectin, no activation of complement component C4 is observed
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
enzyme activity is decreased due to aging, loss of 90% activity after 48-120 h
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
from serum by sequential affinity chromatography, separation from serum mannose-binding protein MBP in presence of EDTA
-
recombinant catalytic fragment encompassing the second complement control protein module and the serine protease domain, i.e. MASP-2-CCP2-SP, from Escherichia coli strain BL21(DE3)
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of the catalytic fragment encompassing the second complement control protein module and the serine protease domain, i.e. MASP-2-CCP2-SP, in Escherichia coli strain BL21(DE3), the recombinant construct contains an extra-tetrapeptide ASMT at the N-terminus
MASP-2 genetic structure, localization of the gene on chromosome 1p36.3-p36.2, overview, 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, predominantly expressed in liver, and is catalytically inactive
MASP-2 promoter sequence analysis, phylogenetic analysis, expression regulation involves Stat3 and StatB, Stat3 is more important, overview
-
the MASP-2 catalytic SP-domain is encoded by a single exon, evolutionary aspects, overview
-
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
combination of isolated MASP and MBP restores the complex and the complement activating activity
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
diagnostics
-
MASP-2 may have potential as clinical biomarkers in colorectal cancer
medicine
-
it is investigated whether the concentration of mannose-binding lectin and MASP-2 is associated with prognosis in pediatric patients with cancer. In the 372 patients studied, median serum concentration of mannose-binding lectin (MBL) is 2.808 mg/l and 391 mg/l for MASP-2. The estimated 4-year event-free survival is 0.60. In the entire, heterogeneous sample, MBL and MASP-2 are not significantly associated with overall survival or event-free survival. In patients with hematologic malignancies, higher MASP-2 is associated with better event-free survival in a significant and clinically relevant way. This is due to patients with lymphoma, but less for those with acute leukemia
molecular biology
-
near monodisperse endotoxin-free polyethylene glycol, at concentrations relevant to therapeutic effects, trigger complement activation in human sera. Depending on polyethylene glycol concentration and average molecular weight, complement activation proceeds either exclusively through MASP-2 activation, and a likely role for the lectin pathway, or through both MASP-2-mediated C4 cleavage and accelerated alternative pathway turnover
medicine
evaluation of the role of MASP-2 in HIV infection. The MASP-2 .126L variant is associated with MASP-2 levels <200 ng/ml and increases the susceptibility to HIV infection and to HIV plus hepatitis B virus positive status. p.126L in addition to other variants associated with low MASP-2 levels such as p.120G, p.377A and p.439H, presents a protective effect against AIDS, independently of age, sex, hepatic function andviral load. MASP-2 serum levels are lower in HIV positive and HIV plus hepatitis B virus positive patients than in controls. Among patients, MASP-2 levels are higher in patients with opportunistic diseases and AIDS. MASP-2 levels correlate positively with MBL/MASP2-mediated complement component C4 and negatively with CD4+ cell counts
medicine
MASP-2 serum levels vary between younger children (12 years and less) and older children (above 12 years) and adults. Younger children with a patent infection with with Schistosoma haematobium have significantly lower MASP-2 serum levels than uninfected children. Older children and adults with a current infection have higher serum MASP-2 levels than controls. mannose-binding lectin serum levels correlate positively with MASP-2 serum levels. MASP2 secretor haplotypes are associated with MASP-2 serum levels in healthy subjects. The heterozygous MASP2 P126L variant is associated with reduced serum MASP-2 levels
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.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
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
Cseh, S.; Vera, L.; Matsushita, M.; Fujita, T.; Arlaud, G.J.; Thielens, N.M.
Characterization of the interaction between L-ficolin/p35 and mannan-binding lectin-associated serine proteases-1 and -2
J. Immunol.
169
5735-5743
2002
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
Wong, N.K.H.; Kojima, M.; Dobo, J.; Ambrus, G.; Sim, R.B.
Activities of the MBL-associated serine proteases (MASPs) and their regulation by natural inhibitors
Mol. Immunol.
36
853-861
1999
Homo sapiens
Thiel, S.; Vorup-Jensen, T.; Stover, C.M.; Schwaeble, W.; Laursen, S.B.; Poulsen, K.; Willis, A.C.; Eggleton, P.; Hansen, S.; Holmskov, U.; Reid, K.B.; Jensenius, J.C.
A second serine protease associated with mannan-binding lectin that activates complement
Nature
386
506-510
1997
Homo sapiens
Matsushita, M.; Fujita, T.
Activation of the classical complement pathway by mannose-binding protein in association with a novel C1s-lik serine protease
J. Exp. Med.
176
1497-1502
1992
Homo sapiens
Moller-Kristensen, M.; Jensenius, J.C.; Jensen, L.; Thielens, N.; Rossi, V.; Arlaud, G.; Thiel, S.
Levels of mannan-binding lectin-associated serine protease-2 in healthy individuals
J. Immunol. Methods
282
159-167
2003
Homo sapiens
Harmat, V.; Gal, P.; Kardos, J.; Szilagyi, K.; Ambrus, G.; Vegh, B.; Naray-Szabo, G.; Zavodszky, P.
The structure of MBL-associated serine protease-2 reveals that identical substrate specificities of C1s and MASP-2 are realized through different sets of enzyme-substrate interactions
J. Mol. Biol.
342
1533-1546
2004
Homo sapiens (Q92876)
Presanis, J.S.; Hajela, K.; Ambrus, G.; Gal, P.; Sim, R.B.
Differential substrate and inhibitor profiles for human MASP-1 and MASP-2
Mol. Immunol.
40
921-929
2004
Homo sapiens
Verma, A.; Matta, A.; Shukla, N.K.; Deo, S.V.; Gupta, S.D.; Ralhan, R.
Clinical significance of mannose-binding lectin-associated serine protease-2 expression in esophageal squamous cell carcinoma
Int. J. Cancer
118
2930-2935
2006
Homo sapiens (O00187), Homo sapiens
Gal, P.; Harmat, V.; Kocsis, A.; Bian, T.; Barna, L.; Ambrus, G.; Vegh, B.; Balczer, J.; Sim, R.B.; Naray-Szabo, G.; Zavodszky, P.
A true autoactivating enzyme. Structural insight into mannose-binding lectin-associated serine protease-2 activations
J. Biol. Chem.
280
33435-33444
2005
Homo sapiens (O00187)
Rossi, V.; Teillet, F.; Thielens, N.M.; Bally, I.; Arlaud, G.J.
Functional characterization of complement proteases C1s/mannan-binding lectin-associated serine protease-2 (MASP-2) chimeras reveals the higher C4 recognition efficacy of the MASP-2 complement control protein modules
J. Biol. Chem.
280
41811-41818
2005
Homo sapiens (O00187)
Teillet, F.; Dublet, B.; Andrieu, J.P.; Gaboriaud, C.; Arlaud, G.J.; Thielens, N.M.
The Two Major Oligomeric Forms of Human Mannan-Binding Lectin: Chemical Characterization, Carbohydrate-Binding Properties, and Interaction with MBL-Associated Serine Proteases
J. Immunol.
174
2870-2877
2005
Homo sapiens (O00187), Homo sapiens
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 (O00187), Rattus norvegicus (Q9JJS8)
Lozano, F.; Suarez, B.; Munoz, A.; Jensenius, J.C.; Mensa, J.; Vives, J.; Horcajada, J.P.
Novel MASP2 variants detected among North African and Sub-Saharan individuals
Tissue Antigens
66
131-135
2005
Homo sapiens (O00187), Homo sapiens
Takahashi, M.; Mori, S.; Shigeta, S.; Fujita, T.
Role of MBL-associated serine protease (MASP) on activation of the lectin complement pathway
Adv. Exp. Med. Biol.
598
93-104
2007
Homo sapiens, Homo sapiens (O00187), Mus musculus
Gal, P.; Barna, L.; Kocsis, A.; Zavodszky, P.
Serine proteases of the classical and lectin pathways: similarities and differences
Immunobiology
212
267-277
2007
Homo sapiens, Rattus norvegicus
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
Teillet, F.; Lacroix, M.; Thiel, S.; Weilguny, D.; Agger, T.; Arlaud, G.J.; Thielens, N.M.
Identification of the site of human mannan-binding lectin involved in the interaction with its partner serine proteases: the essential role of Lys55
J. Immunol.
178
5710-5716
2007
Homo sapiens
Weiss, G.; Madsen, H.O.; Garred, P.
A novel mannose-binding lectin-associated serine protease 1/3 gene variant
Scand. J. Immunol.
65
430-434
2007
Homo sapiens (O00187)
Unterberger, C.; Hanson, S.; Klingenhoff, A.; Oesterle, D.; Frankenberger, M.; Endo, Y.; Matsushita, M.; Fujita, T.; Schwaeble, W.; Weiss, E.H.; Ziegler-Heitbrock, L.; Stover, C.
Stat3 is involved in control of gene expression
Biochem. Biophys. Res. Commun.
364
1022-1025
2007
Homo sapiens, Mus musculus (Q91WP0), Mus musculus, Rattus norvegicus
Sorensen, G.L.; Petersen, I.; Thiel, S.; Fenger, M.; Christensen, K.; Kyvik, K.O.; S?rensen, T.I.; Holmskov, U.; Jensenius, J.C.
Genetic influences on mannan-binding lectin (MBL) and mannan-binding lectin associated serine protease-2 (MASP-2) activity
Genet. Epidemiol.
31
31-41
2007
Homo sapiens
Wallis, R.
Interactions between mannose-binding lectin and MASPs during complement activation by the lectin pathway
Immunobiology
212
289-299
2007
Homo sapiens
Walsh, M.C.; Shaffer, L.A.; Guikema, B.J.; Body, S.C.; Shernan, S.K.; Fox, A.A.; Collard, C.D.; Fung, M.; Taylor, R.P.; Stahl, G.L.
Fluorochrome-linked immunoassay for functional analysis of the mannose binding lectin complement pathway to the level of C3 cleavage
J. Immunol. Methods
323
147-159
2007
Homo sapiens
Kerr, F.K.; Thomas, A.R.; Wijeyewickrema, L.C.; Whisstock, J.C.; Boyd, S.E.; Kaiserman, D.; Matthews, A.Y.; Bird, P.I.; Thielens, N.M.; Rossi, V.; Pike, R.N.
Elucidation of the substrate specificity of the MASP-2 protease of the lectin complement pathway and identification of the enzyme as a major physiological target of the serpin, C1-inhibitor
Mol. Immunol.
45
670-677
2008
Homo sapiens
Mayilyan, K.R.; Arnold, J.N.; Presanis, J.S.; Soghoyan, A.F.; Sim, R.B.
Increased complement classical and mannan-binding lectin pathway activities in schizophrenia
Neurosci. Lett.
404
336-341
2006
Homo sapiens
Ytting, H.; Christensen, I.J.; Thiel, S.; Jensenius, J.C.; Svendsen, M.N.; Nielsen, L.; Lottenburger, T.; Nielsen, H.J.
Biological variation in circulating levels of mannan-binding lectin (MBL) and MBL-associated serine protease-2 and the influence of age, gender and physical exercise
Scand. J. Immunol.
66
458-464
2007
Homo sapiens
Schafranski, M.D.; Pereira Ferrari, L.; Scherner, D.; Torres, R.; de Messias-Reason, I.J.
Functional MASP2 gene polymorphism in patients with history of rheumatic fever
Hum. Immunol.
69
41-44
2008
Homo sapiens
Swierzko, A.S.; Cedzynski, M.; Domzalska-Popadiuk, I.; Macdonald, S.L.; Borkowska-Klos, M.; Atkinson, A.P.; Szala, A.; Jopek, A.; Jensenius, J.C.; Kawakami, M.; Szczapa, J.; Matsushita, M.; Szemraj, J.; Turner, M.L.; Kilpatrick, D.C.
Mannan-binding lectin-associated serine protease-2 (MASP-2) in a large cohort of neonates and its clinical associations
Mol. Immunol.
46
1696-1701
2009
Homo sapiens
Hamad, I.; Hunter, A.C.; Szebeni, J.; Moghimi, S.M.
Poly(ethylene glycol)s generate complement activation products in human serum through increased alternative pathway turnover and a MASP-2-dependent process
Mol. Immunol.
46
225-232
2008
Homo sapiens
Zehnder, A.; Fisch, U.; Hirt, A.; Niggli, F.K.; Simon, A.; Ozsahin, H.; Schlapbach, L.J.; Ammann, R.A.
Prognosis in pediatric hematologic malignancies is associated with serum concentration of mannose-binding lectin-associated serine protease-2 (MASP-2)
Pediatr. Blood Cancer
53
53-57
2009
Homo sapiens
Miller, C.; Wilgenbusch, S.; Michaels, M.; Chi, D.S.; Youngberg, G.; Krishnaswamy, G.
Molecular defects in the mannose binding lectin pathway in dermatological disease: Case report and literature review
Clin. Mol. Allergy
8
6-6
2010
Homo sapiens
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
Skjoedt, M.O.; Hummelshoj, T.; Palarasah, Y.; Honore, C.; Koch, C.; Skjodt, K.; Garred, P.
A novel mannose-binding lectin/ficolin-associated protein is highly expressed in heart and skeletal muscle tissues and inhibits complement activation
J. Biol. Chem.
285
8234-8243
2010
Homo sapiens
Thiel, S.; Kolev, M.; Degn, S.; Steffensen, R.; Hansen, A.G.; Ruseva, M.; Jensenius, J.C.
Polymorphisms in mannan-binding lectin (MBL)-associated serine protease 2 affect stability, binding to MBL, and enzymatic activity
J. Immunol.
182
2939-2947
2009
Homo sapiens
Brouwer, N.; Frakking, F.N.; van de Wetering, M.D.; van Houdt, M.; Hart, M.; Budde, I.K.; Strengers, P.F.; Laursen, I.; Houen, G.; Roos, D.; Jensenius, J.C.; Caron, H.N.; Dolman, K.M.; Kuijpers, T.W.
Mannose-binding lectin (MBL) substitution: recovery of opsonic function in vivo lags behind MBL serum levels
J. Immunol.
183
3496-3504
2009
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
Duncan, R.C.; Bergstroem, F.; Coetzer, T.H.; Blom, A.M.; Wijeyewickrema, L.C.; Pike, R.N.
Multiple domains of MASP-2, an initiating complement protease, are required for interaction with its substrate C4
Mol. Immunol.
49
593-600
2012
Homo sapiens
Novovic, S.; Andersen, A.M.; Ersb?ll, A.K.; Jorgensen, L.N.; Nielsen, H.J.; Jensenius, J.C.; Hansen, M.B.
Mannan-binding lectin and mannan-binding lectin-associated serine protease 2 in acute pancreatitis
Pancreas
40
1097-1102
2011
Homo sapiens
Keizer, M.P.; Pouw, R.B.; Kamp, A.M.; Patiwael, S.; Marsman, G.; Hart, M.H.; Zeerleder, S.; Kuijpers, T.W.; Wouters, D.
TFPI inhibits lectin pathway of complement activation by direct interaction with MASP-2
Eur. J. Immunol.
45
544-550
2015
Homo sapiens
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 (O00187)
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 (O00187)
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 (O00187)
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 (O00187)
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)
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)
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
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
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