Loading…
The mechanism of carbohydrate-mediated complement activation by the serum mannan-binding protein
Serum mannan-binding protein (S-MBP), a lectin specific for mannose and N-acetylglucosamine, was documented to activate complement through the classical pathway. In this study, we examined the mechanism that initiates this activation. By a passive hemolysis test using sheep erythrocytes coated with...
Saved in:
Published in: | The Journal of biological chemistry 1990-02, Vol.265 (4), p.1980-1984 |
---|---|
Main Authors: | , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
Summary: | Serum mannan-binding protein (S-MBP), a lectin specific for mannose and N-acetylglucosamine, was documented to activate complement
through the classical pathway. In this study, we examined the mechanism that initiates this activation. By a passive hemolysis
test using sheep erythrocytes coated with yeast mannan, the activation of complement by human S-MBP was shown to proceed in
the absence of C1q. The following binding studies using 125I-labeled C1r2s2 and C1s indicated that the activated form of C1r2s2
bound to S-MBP located on the surface of the cells with high affinity. The binding of C1s to the cell-bound S-MBP require
the presence of C1r, suggesting that C1r2s2 binds to S-MBP through C1r. The activation of C1s from a proenzyme to a protease
was mediated by cell-bound S-MBP in the presence of C1r and the activated protease remained associated with the cells and
was not released into the medium. The activation of complement with S-MBP was a solid phase event and did not proceed in a
fluid phase. On the basis of these results, it was concluded that S-MBP is responsible for the initiation of carbohydrate-mediated
complement activation as C1q does in immune complex-mediated complement activation. |
---|---|
ISSN: | 0021-9258 1083-351X |
DOI: | 10.1016/s0021-9258(19)39928-4 |