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Blood, Vol. 95 No. 1 (January 1), 2000:
pp. 198-204
From the Laboratory of Cellular Physiology and Immunology, The
Rockefeller University, New York, NY; and Merck Research Laboratory,
Department of Lipid Biochemistry, Rahway, NJ.
We have previously described a novel lipoprotein particle consisting
of phospholipids, apolipoprotein A-I (apoAI), lipopolysaccharide binding protein (LBP) and Factor H-related proteins (FHRP), and we
termed these particles FALP (FHRP-associated lipoprotein particles). Highly purified preparations of FALP contain variable amounts of an
unidentified polypeptide triplet of Mr ~85 000 (tp85). Here we
report that tp85 represents fragment D of fibrinogen, as confirmed by
N-terminal amino acid sequencing and Western blot analysis with an
antifibrinogen antibody. The physical association of fibrinogen with
other components of FALP in plasma was further confirmed by sandwich
ELISA by using monoclonal antibodies against apoAI, FHRP or LBP
to capture the particles and polyclonal antifibrinogen as the detecting
antibody. Furthermore, affinity chromatography with
anti-FHRP-1-specific IgG showed that fibrinogen is co-immunodepleted with FALP and approximately 17% of total plasma fibrinogen are bound
to FALP. LBP is a lipid transfer protein that moves lipopolysaccharide (LPS) to a binding site on CD14 or high-density lipoprotein (HDL). To
determine whether fibrinogen affects the lipid transfer activity of LBP
on FALP, this activity was measured in FALP prepared with and without
fibrinogen. Neither activity of LBP was affected by fibrinogen. The
abundance of FALP suggests, instead, an effect of FALP on the function
or clearance of fibrinogen or fragment D. (Blood. 2000;95:198-204)
This article has been cited by other articles:
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| Copyright © 2000 by American Society of Hematology Online ISSN: 1528-0020 | |||||||||
