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The localization of heparin-binding fragments on human C4b-binding protein.

M Hessing, R A Vlooswijk, T M Hackeng, D Kanters and B N Bouma
J Immunol January 1, 1990, 144 (1) 204-208;
M Hessing
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R A Vlooswijk
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T M Hackeng
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D Kanters
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B N Bouma
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Abstract

C4b-binding protein (C4BP) is a multimeric plasma protein, which regulates the classical pathway of the C system. C4BP interacts with C C4b on a domain located in a 48-kDa chymotryptic fragment. We now demonstrate that C4BP contains heparin-binding fragments, which are located within the C4b binding domain. We have used an assay using heparin coupled to Sepharose CL-6B to show that 125I-C4BP binds to heparin in a time-dependent, saturable, and reversible manner. Binding could be inhibited by purified 48-kDa fragments and direct binding on the 48-kDa fragments to heparin-Sepharose was demonstrated by SDS-PAGE. mAb against native C4BP and the isolated 160-kDa central core fragment were evaluated for their ability to block the binding of 125I-C4BP to heparin and C4b. The relative efficacy of mAb against intact C4BP in blocking C4BP binding to heparin-Sepharose was similar to that for blocking 125I-C4BP binding to C4b. In addition, heparin blocked the binding of 125I-C4BP to C4b and vice versa. It is therefore likely that the heparin-binding fragments are localized on or close to the C4b-binding site of C4BP.

  • Copyright © 1990 by American Association of Immunologists
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The Journal of Immunology
Vol. 144, Issue 1
1 Jan 1990
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The localization of heparin-binding fragments on human C4b-binding protein.
M Hessing, R A Vlooswijk, T M Hackeng, D Kanters, B N Bouma
The Journal of Immunology January 1, 1990, 144 (1) 204-208;

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The localization of heparin-binding fragments on human C4b-binding protein.
M Hessing, R A Vlooswijk, T M Hackeng, D Kanters, B N Bouma
The Journal of Immunology January 1, 1990, 144 (1) 204-208;
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Print ISSN 0022-1767        Online ISSN 1550-6606