show all | hide all No of entries

Information on EC 3.4.21.104 - mannan-binding lectin-associated serine protease-2 and Organism(s) Homo sapiens and UniProt Accession O00187

for references in articles please use BRENDA:EC3.4.21.104
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
Specify your search results
Select one or more organisms in this record:
This record set is specific for:
Homo sapiens
UNIPROT: O00187 not found.
Word Map
The taxonomic range for the selected organisms is: Homo sapiens
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, mbp-associated serine protease, ccp1-ccp2-sp, mannan-binding lectin-associated serine protease 2, mannose-binding lectin-associated serine protease-2, mannan-binding lectin associated serine protease-2, mannose-binding lectin-associated serine protease 2, mbp-associated serine protease-2, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CCP1-CCP2-SP
247
complement control protein-like domain 1-complement control protein-like domain-2-serine protease, catalytic segment of MASP-2
Mannan-binding lectin associated serine protease-2
247
-
mannan-binding lectin-associated serine protease
247
-
mannan-binding lectin-associated serine protease 2
247
-
mannan-binding lectin-associated serine protease-2
278886
-
mannose-binding lectin-associated serine protease 2
247
-
mannose-binding lectin-associated serine protease-2
247
-
Map19
MASP
247
-
MASP-2
MBL-associated serine protease
247
-
MBL-associated serine protease 2
247
-
MBL-associated serine protease-2
247
-
MBL-MASP
247
-
MBL/ficolin-associated serine protease
247
-
MBP-associated serine protease
247
-
MBP-associated serine protease 2
247
-
S01.229
247
Merops ID
REACTION
REACTION DIAGRAM
COMMENTARY hide
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)
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CAS REGISTRY NUMBER
COMMENTARY hide
214915-16-9
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
benzyloxycarbonyl-Gly-Arg-S-benzyl + H2O
?
show the reaction diagram
-
-
-
-
?
complement component C2 + H2O
?
show the reaction diagram
complement component C4 + H2O
?
show the reaction diagram
complement component C4 + H2O
complement component C4b
show the reaction diagram
-
37°C
-
-
?
4,4'-dithiopyridine + H2O
?
show the reaction diagram
-
-
-
?
Abz-GLQRALEI-Lys(Dnp)-NH2 + H2O
?
show the reaction diagram
-
-
-
-
?
Abz-SLGRKIQI-Lys(Dnp)-NH2 + H2O
?
show the reaction diagram
-
-
-
-
?
alpha-N-benzyloxycarbonyl-L-lysine thiobenzyl ester + H2O
?
show the reaction diagram
-
-
-
?
C1-inhibitor P4-P1 fragment + H2O
?
show the reaction diagram
-
-
-
-
?
C1-inhibitor P4-P4' fragment + H2O
?
show the reaction diagram
-
-
-
-
?
complement component C2 + H2O
2 fragments of complement component C2
show the reaction diagram
complement component C2 + H2O
?
show the reaction diagram
complement component C2 + H2O
complement component C2a + complement component C2b
show the reaction diagram
-
-
-
?
complement component C2 + H2O
complement component C2b + ?
show the reaction diagram
-
-
-
-
?
complement component C2 P4-P1 fragment + H2O
?
show the reaction diagram
-
-
-
-
?
complement component C2 P4-P4' fragment + H2O
?
show the reaction diagram
-
-
-
-
?
complement component C3 + H2O
?
show the reaction diagram
complement component C3 + H2O
complement component C3b + ?
show the reaction diagram
-
-
-
-
?
complement component C3i + H2O
?
show the reaction diagram
-
-
-
?
complement component C4 + H2O
2 fragments of complement C4
show the reaction diagram
complement component C4 + H2O
?
show the reaction diagram
complement component C4 + H2O
complement component C4-alpha + complement component C4-alpha'
show the reaction diagram
-
-
-
?
complement component C4 + H2O
complement component C4b + ?
show the reaction diagram
-
-
-
-
?
complement component C4 P4-P1 fragment + H2O
?
show the reaction diagram
-
-
-
-
?
complement component C4 P4-P4' fragment + H2O
?
show the reaction diagram
-
-
-
-
?
factor XIII + H2O
factor XIIIa + ?
show the reaction diagram
-
-
-
-
?
fibrinogen + H2O
fibrin + ?
show the reaction diagram
-
-
-
-
?
Ile-Ala-Arg 4-nitroanilide + H2O
?
show the reaction diagram
-
-
-
?
N-acetylglycine-L-lysine methyl ester + H2O
?
show the reaction diagram
-
-
-
?
N-alpha-benzyloxycarbonyl-L-lysine thiobenzyl ester + H2O
?
show the reaction diagram
-
-
-
-
?
N-carboxybenzoylglycine-L-arginine thiobenzyl ester + H2O
?
show the reaction diagram
-
-
-
?
N-tert-butyloxycarbonyl-L-Leu-Gly-L-Arg-7-amido-4-methylcoumarin + H2O
tert-butyloxycarbonyl-L-Leu-Gly-L-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
Nalpha-benzoyl-L-arginine ethyl ester + H2O
?
show the reaction diagram
-
-
-
?
Nalpha-carbobenzoxy-L-lysine-4-nitrophenyl ester + H2O
?
show the reaction diagram
-
-
-
?
p-tosyl-L-arginine methyl ester + H2O
?
show the reaction diagram
-
-
-
?
Phe-Gly-Arg-7-amido-4-methylcoumarin + H2O
Phe-Gly-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
recombinant enzyme, low activity
-
-
?
Phe-Ser-Arg-7-amido-4-methylcoumarin + H2O
Phe-Ser-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
recombinant enzyme, low activity
-
-
?
Protein + H2O
?
show the reaction diagram
prothrombin + H2O
thrombin + ?
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
complement component C2 + H2O
2 fragments of complement component C2
show the reaction diagram
complement component C2 + H2O
?
show the reaction diagram
-
-
-
-
?
complement component C4 + H2O
2 fragments of complement C4
show the reaction diagram
complement component C4 + H2O
?
show the reaction diagram
factor XIII + H2O
factor XIIIa + ?
show the reaction diagram
-
-
-
-
?
fibrinogen + H2O
fibrin + ?
show the reaction diagram
-
-
-
-
?
Protein + H2O
?
show the reaction diagram
prothrombin + H2O
thrombin + ?
show the reaction diagram
-
-
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
-
enables dimerization
CaCl2
-
5 mM
NaCl
-
140 mM
additional information
no induction by Na+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
complement C1 inhibitor
-
-
-
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
-
alpha-2-Macroglobulin
-
anti-thrombin III
-
recombinant enzyme, inhibition only in presence of heparin
-
benzyloxycarbonyl-D-Phe-Pro-methoxypropylboroglycinepinanediol ester
-
-
C1 inhibitor
-
C1-inhibitor
-
cyclic sunflower MASP inhibitor-1
-
-
Kunitz-type inhibitor tissue factor pathway inhibitor
-
selective inhbitor 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
-
L-Glu-Gly-L-Arg-chloromethylketone
-
-
pefabloc
-
i.e. 4-(2-aminoethyl)-benzenesulphonyl fluoride
PefablocSC
-
irreversible inhibition
sunflower MASP inhibitor-1
-
i.e. GICSRSLPPICIPD
sunflower MASP inhibitor-2
-
i.e. GYCSRSYPPYCIPD
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
mannose-binding lectin
-
-
-
ficolin
-
-
-
H-ficolin
-
-
-
L-ficolin
-
-
-
M-ficolin
-
-
-
mannan-binding lectin
-
mannose-binding lectin
-
-
-
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
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0052 - 0.0092
complement C2
-
0.000085 - 0.0028
complement C4
-
0.123
C1-inhibitor P4-P1 fragment, C1-inhibitor P4-P4' fragment
-
pH 7.4, 37°C
-
4 - 6.5
complement C2
-
1.6 - 74
complement C4
-
0.015
complement component C2 P4-P1 fragment
-
pH 7.4, 37°C
-
0.173
complement component C2 P4-P4' fragment
-
pH 7.4, 37°C
-
0.0579
Complement component C4
-
catalytic MASP-2 fragment CCP1–CCP2–SP, in 0.05 M Tris–HCl, 0.15 M NaCl, 0.2% (w/v) PEG 8000, 0.02% (w/v) NaN3, pH 7.4 at 37°C
-
0.0155
complement component C4 P4-P1 fragment
-
pH 7.4, 37°C
-
0.271
complement component C4 P4-P4' fragment
-
pH 7.4, 37°C
-
6.7
N-acetylglycine-L-lysine methyl ester
-
pH 7.4, 30°C
40
N-carboxybenzoylglycine-L-arginine thiobenzyl ester
-
pH 7.4, 30°C
4.4
Nalpha-benzoyl-L-arginine ethyl ester
-
pH 7.4, 30°C
2.8
p-tosyl-L-arginine methyl ester
-
pH 7.4, 30°C
additional information
additional information
kinetics
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5.1 - 5.6
complement C2
-
0.026 - 3.2
complement C4
-
1.27
Abz-GLQRALEI-Lys(Dnp)-NH2
-
catalytic MASP-2 fragment CCP1–CCP2–SP, in 0.05 M Tris–HCl, 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 CCP1–CCP2–SP, in 0.05 M Tris–HCl, 0.15 M NaCl, 0.2% (w/v) PEG 8000, 0.02% (w/v) NaN3, pH 7.4 at 37°C
0.25
C1-inhibitor P4-P1 fragment
-
pH 7.4, 37°C
-
0.3 - 35.32
C1-inhibitor P4-P4' fragment
-
1.9 - 4.9
complement C2
-
0.9 - 2.2
complement C4
-
3.7 - 31.86
complement component C2 P4-P1 fragment
-
99.58
complement component C2 P4-P4' fragment
-
pH 7.4, 37°C
-
4.54
complement component C4 P4-P1 fragment
-
pH 7.4, 37°C
-
0.04 - 9.35
complement component C4 P4-P4' fragment
-
133
N-acetylglycine-L-lysine methyl ester
-
pH 7.4, 30°C
12.7
N-carboxybenzoylglycine-L-arginine thiobenzyl ester
-
pH 7.4, 30°C
2.4
Nalpha-benzoyl-L-arginine ethyl ester
-
pH 7.4, 30°C
7.1
p-tosyl-L-arginine methyl ester
-
pH 7.4, 30°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
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
-
0.0000088
C1-inhibitor 2
-
37°C, pH 7.4
-
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 hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.5
assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 9
-
-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.43
-
calculated from nucleotide sequence
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
increased MASP-2 expression in comparison with normal tissue
Manually annotated by BRENDA team
additional information
-
enzyme content in plasma of blood donors during 1 year, overview
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
-
MASP-2 is associated with mannan-binding lectin II
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
metabolism
-
MASP-2 is the initiating protease of the lectin pathway
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
Sequence
MASP2_HUMAN
686
0
75702
Swiss-Prot
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
29000
-
29000 + 60000, chimera C1s(MASP-2SP), SDS-PAGE
44000
-
x * 44000, mutant MASP-2 CCP1-CCP2-SP R444Q, SDS-PAGE
45000
-
x * 45000, SDS-PAGE
74000
-
2 * 74000, SDS-PAGE
74150
-
monomer, calculated from amino acid sequence
75100
-
x * 75100, SDS-PAGE
78000
-
x * 78000, chimera C1s(MASP-2CCP1/2), SDS-PAGE
28000
-
1 * 45000 + 1 * 28000, SDS-PAGE, reducing conditions
29000
-
calculated molecular mass of the MASP-2 CUB-EGF fragment in the presence of Ca2+
31000
44000
-
x * 44000, MASP-2 CCP1-CCP2-SP form, SDS-PAGE
45000
-
1 * 45000 + 1 * 28000, SDS-PAGE, reducing conditions
50000
-
x * 75000, full-length proenzyme, SDS-PAGE, x * 50000, A-chain of the enzyme, SDS-PAGE
52000
-
1 * 52000 + 1 * 31000, SDS-PAGE
66000
-
1 * 66000, heavy subunit, + 1 * 31000, light subunit, SDS-PAGE
70000
-
SDS-PAGE, proenzyme form
74150
-
calculated from nucleotide sequence
75000
-
x * 75000, full-length proenzyme, SDS-PAGE, x * 50000, A-chain of the enzyme, SDS-PAGE
76000
77000
-
MASP-2, gel filtration
80000
-
SDS-PAGE, non-reducing conditions
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
dimer
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
no glycoprotein
-
-
proteolytic modification
additional information
-
no sites for N-linked glycosylation
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
-
zymogen and the activated form, 2.4 A resolution
-
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 hide
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
MASP-2 CCP1-CCP2-SP R444Q
-
lower KM-value for complement C4
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
S195A
-
inactive
V377A
-
the mutant cleaves complement component C4 with an activity comparable to wild type MASP-2
additional information
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5
-
wild-type zymogen MASP-2
665655
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
48.2
-
Tm for the zymogen of mutant MASP-2 CCP1-CCP2-SP R444Q
50.8
-
Tm for the active fragment of mutant MASP-2 CCP1-CCP2-SP R444Q
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
enzyme is stable during at least 10 freeze-thaw cycles
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 4°C, and room temperature, 30 days, stable at
-
37°C, loss of about 95% activity within 30 days
-
enzyme activity is decreased due to aging, loss of 90% activity after 48-120 h
-
PURIFICATION/commentary
ORGANISM
UNIPROT
LITERATURE
chimeric proteins C1s(MASP-2CCP1/2) and C1s(MASP-2SP)
-
from serum by sequential affinity chromatography, separation from serum mannose-binding protein MBP in presence of EDTA
-
mannan-agarose column chromatography
-
mature protein and truncated fragments
-
MBL-derivatized Sepharose column chromatography
-
Q-Sepharose column chromatography
-
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 in Escherichia coli
-
expression in HEK-293F FreeStyle cells
-
expressed in a baculovirus/insect cell system
-
expressed in CHO cells
-
expressed in Escherichia coli BL21Star(DE3) pLysS cells
-
expressed in HEK293 cells
-
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 and truncated fragments of the catalytic region
-
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
-
mature protein and truncated fragments
-
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 hide
LITERATURE
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
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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, Homo sapiens (O00187)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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, Homo sapiens (O00187)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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, Homo sapiens (O00187)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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, Mus musculus (Q91WP0), Rattus norvegicus
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Wallis, R.
Interactions between mannose-binding lectin and MASPs during complement activation by the lectin pathway
Immunobiology
212
289-299
2007
Homo sapiens
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
Select items on the left to see more content.