Comparison of cDNA-derived protein sequences of the human fibronectin and vitronectin receptor. cap alpha. -subunits and platelet glycoprotein IIb
The fibronectin receptor (FnR), the vitronectin receptor (VnR), and the platelet membrane glycoprotein (GP) IIb-IIIa complex are members of a family of cell adhesion receptors, which consist of noncovalently associated ..cap alpha..- and ..beta..-subunits. The present study was designed to compare the cDNA-derived protein sequences of the ..cap alpha..-subunits of human FnR, VnR, and platelet GP IIb. cDNA clones for the ..cap alpha..-subunit of the FnR (FnR/sub ..cap alpha../) were obtained from a human umbilical vein endothelial (HUVE) cell library by using an oligonucleotide probe designed from a peptide sequence of platelet GP IIb. cDNA clones for platelet GP IIb were isolated from a cDNA expression library of human erythroleukemia cells by using antibodies. cDNA clones of the VnR ..cap alpha..-subunit (VnR/sub ..cap alpha../) were obtained from the HUVE cell library by using an oligonucleotide probe from the partial cDNA sequence for the VnR/sub ..cap alpha../. Translation of these sequences showed that the FNR/sub ..cap alpha../, the VnR/sub ..cap alpha../, and GP IIb are composed of disulfide-linked large (858-871 amino acids) and small (137-158 amino acids) chains that are posttranslationally processed from a single mRNA. A single hydrophobic segment located near the carboxyl terminus of each small chain appears to be a transmembrane domain. The large chains appear to be entirely extracellular, and each contains four repeated putative Ca/sup 2 +/-binding domains of about 30 amino acids that have sequence similarities to other Ca/sup 2 +/-binding proteins. The identity among the protein sequences of the three receptor ..cap alpha..-subunits ranges from 36.1% to 44.5%, with the Ca/sup 2 +/-binding domains having the greatest homology. These proteins apparently evolved by a process of gene duplication.
- Research Organization:
- Univ. of California, San Francisco
- OSTI ID:
- 5303932
- Journal Information:
- Biochemistry; (United States), Vol. 26:25
- Country of Publication:
- United States
- Language:
- English
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