Abstract
The platelet GPIIb-IIIa heterodimer complex is essential for platelet aggregation and is a member of a family of adhesive protein receptors. GPIIb, the larger component of this complex, is composed of two disulfide-linked subunits: GPIIbα and GPHbβ. A cDNA expression library was constructed using mRNA from a human erythroleukemia (HEL) cell line expressing GPIIb-IIIa in λgt11, and the library was screened using a polyclonal antibody against GPIIb. Positive clones were isolated and a 3.3 kb cDNA clone was shown to contain DNA sequence information for the amino acids at the N-termini of both GPIIbα and GPIIbβ. The IIbα sequence begins 30 bp downstream from the 5′-end of the clone, while the IIbβ starts 700 bp upstream from the poly-A tail at the 3′-end of the clone. Northern blot analysis indicates a GPIIb mRNA of 4.1 kb. Analysis of the DNA sequence provides the first complete amino acid sequence for GPIIbα and GPIIbβ, including hydrophobic domains, glycosylation sites, and proline-rich areas. A 16.3 kb human genomic clone has been isolated; exons span at least 12 kb of this clone. Current studies are defining the intron-exon organization of the gene. These findings will allow a direct approach to analysis of the genetic defect(s) causing thrombasthenia, and may lead to means for prenatal diagnosis of this platelet defect.
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Heidenreich, R., Schwartz, E., Surrev, S. et al. CDNA AND GENOMIC CLONES FOR HUMAN PLATELET GLYCOPROTEIN lib (GPIIb). Pediatr Res 21 (Suppl 4), 290 (1987). https://doi.org/10.1203/00006450-198704010-00739
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DOI: https://doi.org/10.1203/00006450-198704010-00739