Information on EC 3.4.21.104 - mannan-binding lectin-associated serine protease-2

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.4.21.104
-
RECOMMENDED NAME
GeneOntology No.
mannan-binding lectin-associated serine protease-2
-
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
cleavage of C-N-linkage
hydrolysis of peptide bond
CAS REGISTRY NUMBER
COMMENTARY hide
214915-16-9
-
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
-
MASP-2 is the initiating protease of the lectin pathway
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
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
-
-
-
?
benzyloxycarbonyl-Gly-Arg-S-benzyl + 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
-
-
-
-
?
C2 complement component + H2O
?
show the reaction diagram
-
-
-
-
?
C4 complement component + 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
-
37°C
-
-
?
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-Pro-Arg-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
-
?
Phe-Ser-Arg-7-amido-4-methylcoumarin + H2O
Phe-Ser-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
recombinant enzyme, low activity
-
-
?
plasminogen + H2O
plasmin + propeptide of thrombin
show the reaction diagram
prekallikrein + H2O
kallikrein + propeptide of thrombin
show the reaction diagram
Protein + H2O
?
show the reaction diagram
prothrombin + H2O
thrombin + ?
show the reaction diagram
-
-
-
-
?
prothrombin + H2O
thrombin + propeptide of thrombin
show the reaction diagram
Val-Leu-Lys-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
C2 complement component + H2O
?
show the reaction diagram
-
-
-
-
?
C4 complement component + 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 C2b + ?
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 C4b + ?
show the reaction diagram
Q3V5Q0
-
-
-
?
factor XIII + H2O
factor XIIIa + ?
show the reaction diagram
-
-
-
-
?
fibrinogen + H2O
fibrin + ?
show the reaction diagram
-
-
-
-
?
plasminogen + H2O
plasmin + propeptide of thrombin
show the reaction diagram
-
activation
-
-
?
prekallikrein + H2O
kallikrein + propeptide of thrombin
show the reaction diagram
-
activation
-
-
?
Protein + H2O
?
show the reaction diagram
prothrombin + H2O
thrombin + ?
show the reaction diagram
-
-
-
-
?
prothrombin + H2O
thrombin + propeptide of thrombin
show the reaction diagram
-
activation of thrombin covalentyl bound to a bacterial cell surface
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CaCl2
-
5 mM
NaCl
-
140 mM
additional information
no induction by Na+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
alpha-2-Macroglobulin
-
anti-thrombin III
-
recombinant enzyme, inhibition only in presence of heparin
-
benzyloxycarbonyl-D-Phe-Pro-methoxypropylboroglycinepinanediol ester
-
-
-
C1 inhibitor
-
C1-inhibitor
-
complement 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
-
-
myelin basic protein
-
no activity with substrate C4-component of the enzyme complexed with myelin basic protein before activation of the complex by binding to a suitable carbohydrate ligand
-
pefabloc
-
i.e. 4-(2-aminoethyl)-benzenesulphonyl fluoride
PefablocSC
-
irreversible inhibition
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
-
sunflower MASP inhibitor-1
-
i.e. GICSRSLPPICIPD
sunflower MASP inhibitor-2
-
i.e. GYCSRSYPPYCIPD
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ficolin
-
ficolins
-
are pattern recognition proteins acting in innate immunity, and triggering the activation of the lectin complement pathway through MBL-associated serine proteases
-
H-ficolin
-
-
-
L-ficolin
-
-
-
M-ficolin
-
-
-
mannan-binding lectin
-
mannose-binding lectin
-
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.123
C1-inhibitor P4-P1 fragment, C1-inhibitor P4-P4' fragment
-
pH 7.4, 37°C
-
0.0052 - 6.5
complement C2
-
0.000085 - 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
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.27
Abz-GLQRALEI-Lys(Dnp)-NH2
Homo sapiens
-
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
Homo sapiens
-
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
Homo sapiens
-
pH 7.4, 37°C
-
0.3 - 35.32
C1-inhibitor P4-P4' fragment
-
1.9 - 5.6
complement C2
-
0.026 - 3.2
complement C4
-
3.7 - 31.86
complement component C2 P4-P1 fragment
-
99.58
complement component C2 P4-P4' fragment
Homo sapiens
-
pH 7.4, 37°C
-
4.54
complement component C4 P4-P1 fragment
Homo sapiens
-
pH 7.4, 37°C
-
0.04 - 9.35
complement component C4 P4-P4' fragment
-
133
N-acetylglycine-L-lysine methyl ester
Homo sapiens
-
pH 7.4, 30°C
12.7
N-carboxybenzoylglycine-L-arginine thiobenzyl ester
Homo sapiens
-
pH 7.4, 30°C
2.4
Nalpha-benzoyl-L-arginine ethyl ester
Homo sapiens
-
pH 7.4, 30°C
7.1
p-tosyl-L-arginine methyl ester
Homo sapiens
-
pH 7.4, 30°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
0.058
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
-
0.00103
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
7.5
-
assay at
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
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
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
28000
-
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
66000
-
1 * 66000, heavy subunit, + 1 * 31000, light subunit, SDS-PAGE
70000
-
SDS-PAGE, proenzyme form
75000
-
x * 75000, full-length proenzyme, SDS-PAGE, x * 50000, A-chain of the enzyme, SDS-PAGE
75100
-
x * 75100, SDS-PAGE
77000
-
MASP-2, gel filtration
78000
-
x * 78000, chimera C1s(MASP-2CCP1/2), SDS-PAGE
80000
-
SDS-PAGE, non-reducing conditions
87000
-
x * 87000, proenzyme form, SDS-PAGE, 1 * 52000, heavy enzyme chain, active enzyme form, SDS-PAGE
90000
-
SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
-
-
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
-
-
no glycoprotein
-
-
proteolytic modification
additional information
-
no sites for N-linked glycosylation
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
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
-
hanging drop vapor diffusion method in the presence of Ca2+
-
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
-
MASP-2K mutant, inhibited in autoproteolytic activation, by affinity chromatography on an myelin basic protein-resin
-
mature protein and truncated fragments
-
MBL-derivatized Sepharose column chromatography
-
Ni-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)
secreted recombinant catalytically active and inactive wild-type and mutant MASP-2 zymogens from CHO cell culture medium
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in a baculovirus/insect cell system
-
expressed in Chinese hamster ovary cells, recombinant wild type rat MASP-2 is toxic to producing Chinese hamster ovary cells and autoactivates during biosynthesis
-
expressed in CHO cells
-
expressed in Escherichia coli BL21Star(DE3) pLysS cells
-
expressed in HEK293 cells
-
expression in Escherichia coli
-
expression in HEK-293F FreeStyle cells
-
expression of catalytically active and inactive wild-type and mutant MASP-2 zymogens in CHO cells, enzyme secretion
-
expression of mutant enzyme R424K in CHO 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
expression using a Drosophila melanogaster expression system, C4-cleavage activity reconstitution of the enzyme-deficient mutant by addition of recombinant enzyme to deficient serum
-
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 genetic structure, overview
-
MASP-2 promoter sequence analysis, phylogenetic analysis, expression regulation involves Stat3 and StatB, Stat3 is more important, overview
MASP2, DNA and amino acid sequence determination and anaylsis, phylogenetic analysis, MASP2 arose before the emergence of bony fish
mature protein and truncated fragments
-
the MASP-2 catalytic SP-domain is encoded by a single exon, evolutionary aspects, overview
ENGINEERING
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)
H155R
-
the mutant cleaves complement component C4 slightly better than the wild type MASP-2
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
P126L
-
the mutant cleaves complement component C4 with an activity comparable to wild type MASP-2
R103C
-
found in 2% of studied North Africans, not found in Sub-Saharans and Spaniards
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
R84Q
-
found in 13.33% of studied Sub-Saharans, 1% of studied North Africans, not found in Spaniards
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
S613A
-
site-directed mutagenesis, the mutant zymogen cannot autoactivate and is secreted in the zymogen form
additional information
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
combination of isolated MASP and MBP restores the complex and the complement activating activity
-
reconstitution of the MBL-MASP-sMAP complex using recombinant proteins, overview
-
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