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 TYPE-X

被引:62
作者
HAYWARD, CPM
HASSELL, JA
DENOMME, GA
RACHUBINSKI, RA
BROWN, C
KELTON, JG
机构
[1] MCMASTER UNIV,DEPT MED,HAMILTON,ON L8N 3Z5,CANADA
[2] MCMASTER UNIV,DEPT BIOCHEM,HAMILTON,ON L8N 3Z5,CANADA
[3] MCMASTER UNIV,INST MOLEC BIOL & BIOTECHNOL,HAMILTON,ON L8N 3Z5,CANADA
[4] CANADIAN RED CROSS BLOOD TRANSFUS SERV,HAMILTON CTR,HAMILTON,ON L8N 3Z5,CANADA
关键词
D O I
10.1074/jbc.270.31.18246
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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 lambda 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, carboxyl-terminal domains of several other trimeric proteins, including complement Clq and collagens type VIII and X.
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收藏
页码:18246 / 18251
页数:6
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