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J. Biol. Chem., Vol. 262, Issue 18, 8476-8482, Jun, 1987
M Poncz, R Eisman, R Heidenreich, SM Silver, G Vilaire, S Surrey, E Schwartz and JS Bennett
The platelet membrane glycoprotein IIb X IIIa heterodimer complex (GPIIb X
IIIa) is the platelet receptor for adhesive proteins, containing binding
sites for fibrinogen, von Willebrand factor, and fibronectin on activated
platelets. GPIIb X IIIa also appears to be a member of a family of membrane
adhesive protein receptors that plays a major role in cell-cell and
cell-matrix interactions. GPIb is the larger component of this platelet
receptor and is composed of two disulfide-linked subunits. In this report
we describe the analysis of cDNA clones for human GPIIb that were isolated
from a lambda gt11 expression library prepared using RNA from HEL cells. A
total of 3.3 kilobases of cDNA was sequence, revealing a continuous open
reading frame encoding both GPIIb subunits. The cDNA encodes 1039 amino
acids: 137 constituting the smaller subunit, 871 constituting the larger
subunit, and 30 constituting an NH2-terminal signal peptide. No homology
was found between the larger and smaller subunits. The smaller subunit
contains a 26-residue hydrophobic sequence near its COOH terminus that
represents a potential transmembrane domain. Four stretches of 12 amino
acids present in the larger subunit are homologous to the calcium binding
sites of calmodulin and troponin C. Northern blot analysis using HEL cell
RNA indicated that the mature mRNA coding for GPIIb is 4.1 kilobases in
size. A comparison of the GPIIb coding region with available cDNA sequences
of the alpha-chains of the vitronectin and fibronectin receptors revealed
41% DNA homology and 74% and 63% amino acid homology, respectively. Our
data establish the amino acid sequence for the human platelet glycoprotein
IIb and provide additional evidence for the existence of a family of
cellular adhesion protein receptors.
Structure of the platelet membrane glycoprotein IIb. Homology to the alpha subunits of the vitronectin and fibronectin membrane receptors
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