NDLI: Mechanism of complement-dependent haemolysis via the lectin pathway: role of the complement regulatory proteins

Content Provider	PubMed Central
Author	Suankratay, C. Mold, C. Zhang, Y. Lint, T. F. Gewurz, H.
Copyright Year	1999
Abstract	Mannan-binding lectin (MBL) is an acute phase protein which activates the classical complement pathway at the level of C4 and C2 via two novel serine proteases homologous to C1r and C1s. We recently reported that haemolysis via this lectin pathway requires alternative pathway amplification. The present experiments sought to establish the basis for this requirement, and hence focused on the activity and regulation of the C3 convertases. Complement activation was normalized between the lectin and classical pathways such that identical amounts of bound C4 and of haemolytically active C4,2 sites were present on the indicator cells. Under these conditions, there was markedly less haemolysis, associated with markedly less C3 and C5 deposited, via the lectin pathway than via the classical pathway, particularly when alternative pathway recruitment was blocked by depletion of factor D. Lectin pathway activation was associated with enhanced binding in the presence of MBL of complement control proteins C4bp and factor H to C4b and C3b, respectively, with decreased stability of the C3-converting enzyme C4b,2a attributable to C4bp. Immunodepletion of C4bp and/or factor H increased lectin pathway haemolysis and allowed lysis to occur in absence of the alternative pathway. Thus, the lectin pathway of humans is particularly susceptible to the regulatory effects of C4bp and factor H, due at least in part to MBL enhancement of C4bp binding to C4b and factor H binding to C3b.
Related Links	http://dx.doi.org/10.1046/j.1365-2249.1999.00998.x
Ending Page	448
Page Count	7
Starting Page	442
File Format	PDF
ISSN	00099104
e-ISSN	13652249
Journal	Clinical and Experimental Immunology
Issue Number	3
Volume Number	117
Language	English
Publisher	Blackwell Science Inc
Publisher Date	1999-09-01
Access Restriction	Open
Rights Holder	Blackwell Science Inc
Subject Keyword	Immunology Immunology and Allergy Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Immunology and Allergy Immunology

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