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Jens Christian Jensenius

MASP-2, the C3 convertase generating protease of the MBLectin complement activating pathway

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MASP-2, the C3 convertase generating protease of the MBLectin complement activating pathway. / Vorup-Jensen, T; Jensenius, Jens Christian; Thiel, S.

In: Immunobiology, Vol. 199, No. 2, 1998, p. 348-57.

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@article{2e36ee52d8f94f48a3d9dc8ce474f189,
title = "MASP-2, the C3 convertase generating protease of the MBLectin complement activating pathway",
abstract = "Mannan-binding lectin (MBL) activates the complement system through cleavage of C4 and C2. Until recently it was thought that only one serine protease in complex with MBL (MBL-associated serine protease, MASP) mediates complement activation, but with the finding of a second MBL-associated serine protease, MASP-2, the activation process appears more elaborate, possibly resembling that of the C1 complex. The two MASPs share the domain organisation of C1r and C1s and it may be speculated that interaction between the two MASPs is required for complement activation in the same manner as with the C1 proteases. We have demonstrated that MASP-2 is a C4 cleaving component of the MBL/MASP complex. By analogy, one may thus speculate that, upon binding of MBL to carbohydrate, MASP-1 autoactivates and then activates MASP-2, but there is as yet no evidence for this. The components of C1 are present in serum in approximately equimolar amounts, whereas MASP-1 is in large excess over MBL. Pairwise comparison of the four proteases shows the primary structures to be approximately 40% identical. Phylogenetic analysis indicates that MASP-2 is closer to C1r and C1s than is MASP-1, but no particular association between MASP-2 and the C4 cleaving enzyme, C1s, can be deduced from sequence comparison.",
keywords = "Animals, Carrier Proteins, Cattle, Collectins, Complement Activation, Complement C1r, Complement C1s, Complement C2, Complement C3-C5 Convertases, Complement C4, Enzyme Activation, Evolution, Molecular, Humans, Macromolecular Substances, Mannose-Binding Protein-Associated Serine Proteases, Phylogeny, Protein Conformation, Sequence Homology, Amino Acid, Serine Endopeptidases, Structure-Activity Relationship, Vertebrates",
author = "T Vorup-Jensen and Jensenius, {Jens Christian} and S Thiel",
year = "1998",
language = "English",
volume = "199",
pages = "348--57",
journal = "Immunobiology",
issn = "0171-2985",
publisher = "Elsevier GmbH - Urban und Fischer",
number = "2",

}

RIS

TY - JOUR

T1 - MASP-2, the C3 convertase generating protease of the MBLectin complement activating pathway

AU - Vorup-Jensen, T

AU - Jensenius, Jens Christian

AU - Thiel, S

PY - 1998

Y1 - 1998

N2 - Mannan-binding lectin (MBL) activates the complement system through cleavage of C4 and C2. Until recently it was thought that only one serine protease in complex with MBL (MBL-associated serine protease, MASP) mediates complement activation, but with the finding of a second MBL-associated serine protease, MASP-2, the activation process appears more elaborate, possibly resembling that of the C1 complex. The two MASPs share the domain organisation of C1r and C1s and it may be speculated that interaction between the two MASPs is required for complement activation in the same manner as with the C1 proteases. We have demonstrated that MASP-2 is a C4 cleaving component of the MBL/MASP complex. By analogy, one may thus speculate that, upon binding of MBL to carbohydrate, MASP-1 autoactivates and then activates MASP-2, but there is as yet no evidence for this. The components of C1 are present in serum in approximately equimolar amounts, whereas MASP-1 is in large excess over MBL. Pairwise comparison of the four proteases shows the primary structures to be approximately 40% identical. Phylogenetic analysis indicates that MASP-2 is closer to C1r and C1s than is MASP-1, but no particular association between MASP-2 and the C4 cleaving enzyme, C1s, can be deduced from sequence comparison.

AB - Mannan-binding lectin (MBL) activates the complement system through cleavage of C4 and C2. Until recently it was thought that only one serine protease in complex with MBL (MBL-associated serine protease, MASP) mediates complement activation, but with the finding of a second MBL-associated serine protease, MASP-2, the activation process appears more elaborate, possibly resembling that of the C1 complex. The two MASPs share the domain organisation of C1r and C1s and it may be speculated that interaction between the two MASPs is required for complement activation in the same manner as with the C1 proteases. We have demonstrated that MASP-2 is a C4 cleaving component of the MBL/MASP complex. By analogy, one may thus speculate that, upon binding of MBL to carbohydrate, MASP-1 autoactivates and then activates MASP-2, but there is as yet no evidence for this. The components of C1 are present in serum in approximately equimolar amounts, whereas MASP-1 is in large excess over MBL. Pairwise comparison of the four proteases shows the primary structures to be approximately 40% identical. Phylogenetic analysis indicates that MASP-2 is closer to C1r and C1s than is MASP-1, but no particular association between MASP-2 and the C4 cleaving enzyme, C1s, can be deduced from sequence comparison.

KW - Animals

KW - Carrier Proteins

KW - Cattle

KW - Collectins

KW - Complement Activation

KW - Complement C1r

KW - Complement C1s

KW - Complement C2

KW - Complement C3-C5 Convertases

KW - Complement C4

KW - Enzyme Activation

KW - Evolution, Molecular

KW - Humans

KW - Macromolecular Substances

KW - Mannose-Binding Protein-Associated Serine Proteases

KW - Phylogeny

KW - Protein Conformation

KW - Sequence Homology, Amino Acid

KW - Serine Endopeptidases

KW - Structure-Activity Relationship

KW - Vertebrates

M3 - Journal article

C2 - 9777418

VL - 199

SP - 348

EP - 357

JO - Immunobiology

JF - Immunobiology

SN - 0171-2985

IS - 2

ER -