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Research Article Free access | 10.1172/JCI113277

Platelet glycoprotein IIb. Chromosomal localization and tissue expression.

P F Bray, J P Rosa, G I Johnston, D T Shiu, R G Cook, C Lau, Y W Kan, R P McEver, and M A Shuman

Department of Medicine, University of California, San Francisco 94143.

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Department of Medicine, University of California, San Francisco 94143.

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Department of Medicine, University of California, San Francisco 94143.

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Department of Medicine, University of California, San Francisco 94143.

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Department of Medicine, University of California, San Francisco 94143.

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Department of Medicine, University of California, San Francisco 94143.

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Department of Medicine, University of California, San Francisco 94143.

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Department of Medicine, University of California, San Francisco 94143.

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Department of Medicine, University of California, San Francisco 94143.

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Published December 1, 1987 - More info

Published in Volume 80, Issue 6 on December 1, 1987
J Clin Invest. 1987;80(6):1812–1817. https://doi.org/10.1172/JCI113277.
© 1987 The American Society for Clinical Investigation
Published December 1, 1987 - Version history
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Abstract

The GPIIb-IIIa complex functions as a receptor for cytoadhesive proteins on the platelet surface. Both GPIIb and GPIIIa are synthesized by a human erythroleukemia (HEL) cell line. We isolated several cDNA clones by screening a HEL cell cDNA library with an oligonucleotide derived from amino acid sequence of GPIIb. Nucleotide and amino acid sequences were determined from 703 bp of one of these clones. Amino acid sequence of purified platelet GPIIb peptides confirmed the identity of the clone. The cDNA encodes the carboxyl terminus of the large (alpha) subunit of GPIIb and all of the smaller (beta) subunit of GPIIb. By hybridizing the cDNA directly to chromosomes separated by dual laser chromosome sorting, the gene for GPIIb was mapped to chromosome 17. Northern blot analysis showed a approximately 3.4-kb GPIIb mRNA in HEL cells. We also compared the amino acid sequences determined from eight additional platelet GPIIb peptides with the derived amino acids from a published HEL cell GPIIb cDNA, and the platelet and HEL cell proteins appear to be the same. Despite previous reports that vascular endothelial cells and monocytes contain GPIIb, no GPIIb mRNA was observed in either type of cell. Thus, GPIIb appears to be specific for the platelet-megakaryocyte membrane and is distinct from the alpha subunits of the adhesion receptors in other normal tissues.

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