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Volume 270,
Number 31,
Issue of August 04, pp. 18246-18251, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
The cDNA
Sequence of Human Endothelial Cell Multimerin
A UNIQUE PROTEIN WITH RGDS, COILED-COIL, AND EPIDERMAL GROWTH
FACTOR-LIKE DOMAINS AND A CARBOXYL TERMINUS SIMILAR TO THE GLOBULAR
DOMAIN OF COMPLEMENT C1q AND COLLAGENS TYPE VIII AND X
(Received for publication, May 17, 1995)
Catherine P. M.
Hayward
,
John A.
Hassell
,
Gregory
A.
Denomme
,
Richard A.
Rachubinski
,
Claudia
Brown
,
John G.
Kelton
Multimerin is a massive, soluble protein found in platelets and
in the endothelium of blood vessels. Multimerin is composed of varying
sized, disulfide-linked multimers, the smallest of which is a
homotrimer. Multimerin is a factor V/Va-binding protein and may
function as a carrier protein for platelet factor V. The cDNA for human
multimerin was isolated from gt11 endothelial cell libraries using
antibodies, and the isolated cDNA clones were used to obtain the full
sequence. The full-length multimerin cDNA was 4.2 kilobase pairs.
Northern analyses identified a 4.7-kilobase transcript in cultured
endothelial cells, a megakaryocytic cell line, platelets, and highly
vascular tissues. The multimerin cDNA can encode a protein of 1228
amino acids with the probable signal peptide cleavage site between
amino acids 19 and 20. The protein is predicted to be hydrophilic and
to contain 23 N-glycosylation sites. The adhesive motif RGDS
(Arg-Gly-Asp-Ser) and an epidermal growth factor-like domain were
identified. Sequence searches indicated that multimerin is a unique
protein. Analyses identified probable coiled-coil structures in the
central portion of the multimerin sequence. Additionally, the
carboxyl-terminal region of multimerin resembles the globular,
non-collagen-like, carboxylterminal domains of several other trimeric
proteins, including complement C1q and collagens type VIII and X.

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Copyright © 1995 by the American Society for Biochemistry and Molecular Biology.
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