Comparison of cDNA-derived protein sequences of the human fibronectin and vitronectin receptor. cap alpha. -subunits and platelet glycoprotein IIb

Journal Article · Tue Dec 15 04:00:00 EST 1987 · Biochemistry; (United States)

OSTI ID:5303932

Fitzgerald, L A; Poncz, M; Steiner, B; Rall, Jr, S C; Bennett, J S; Phillips, D R

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), Journal Name: Biochemistry; (United States) Vol. 26:25; ISSN BICHA
• Country of Publication: United States
• Language: English

Related Subjects

550201* -- Biochemistry-- Tracer Techniques
59 BASIC BIOLOGICAL SCIENCES
AMINO ACID SEQUENCE
BETA DECAY RADIOISOTOPES
BETA-MINUS DECAY RADIOISOTOPES
BIOLOGICAL MATERIALS
BLOOD
BLOOD CELLS
BLOOD COAGULATION FACTORS
BLOOD PLATELETS
BODY FLUIDS
CARBOHYDRATES
CARBON 14 COMPOUNDS
COAGULANTS
DAYS LIVING RADIOISOTOPES
DNA
DNA SEQUENCING
DRUGS
GLUCOPROTEINS
HEMATOLOGIC AGENTS
ISOTOPES
LABELLED COMPOUNDS
LIGHT NUCLEI
MATERIALS
MEMBRANE PROTEINS
MOLECULAR STRUCTURE
NUCLEI
NUCLEIC ACIDS
ODD-ODD NUCLEI
OLIGONUCLEOTIDES
ORGANIC COMPOUNDS
PHOSPHORUS 32
PHOSPHORUS ISOTOPES
PROTEINS
RADIOISOTOPES
RECEPTORS
RECOMBINANT DNA
SACCHARIDES
STRUCTURAL CHEMICAL ANALYSIS