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J. Biol. Chem., Vol. 276, Issue 34, 32129-32135, August 24, 2001
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From the Section of Nephrology, Department of Medicine, The
University of Chicago, Chicago, Illinois 60637
Complement-coated particles interact with
specific immune adherence receptors (IAR). In primates, this function
is served by complement receptor 1 (CR1) on erythrocytes. In contrast,
rodent platelets bear IAR distinct from CR1, the identity of which was studied here. A 150-kDa C3b-binding protein was isolated from rat
platelets, which had immunochemical and biochemical identity to plasma
factor H. Immunofluorescence microscopy and flow cytometry demonstrated
that factor H was present on the surface of rat and mouse platelets,
which could be removed by treatment with neuraminidase. Sheep
erythrocytes bearing C3b underwent immune adherence with rat and mouse
platelets, which was blocked with anti-factor H F(ab')2 antibodies, but not with antibodies binding
to the complement regulator, Crry, on the platelet surface. By
reverse transcription-polymerase chain reaction using rat
platelet RNA and primers designed from mouse factor H, a 472-base pair
product was generated that was identical in sequence to that produced
from rat liver RNA. The translated protein product was 85% similar to
mouse liver factor H. The 3'-nucleotide sequence from platelets
predicted a soluble factor H protein. By Northern analysis, liver and
platelets had identically sized factor H mRNA. Thus, rat and
mouse platelets have a membrane protein with characteristics of factor
H that is linked via sialic acid residues and functions as the IAR.
Whether platelet factor H is acquired by passive adsorption from sera and/or is produced by platelets remains to be determined.
A Protein with Characteristics of Factor H Is
Present on Rodent Platelets and Functions as the Immune Adherence
Receptor*
§,, and
*
This work was supported by National Institutes of Health
Grants R01DK48173 and R01DK55357 and a chapter grant from the Arthritis Foundation, Greater Chicago Chapter.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Supported by National Institutes of Health Training Grant T32DK07510.
§
To whom correspondence should be addressed: The University of
Chicago, Section of Nephrology, 5841 S. Maryland Ave., MC5100, Chicago,
IL 60637. Tel.: 773-702-4796; Fax: 773-702-5818; E-mail: jalexand@medicine.uchicago.edu.
Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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