Abstract
Publisher Summary This chapter reviews the current understanding of the biosynthesis and structure of glycoprotein (GP) IIb-IIIa and its function in platelet adhesion, aggregation, and anchorage-dependent signaling. The genes for GP IIb and GP IIIa are closely linked within a 260 kb segment of DNA on the long arm of chromosome 17, with the IIIa gene situated 5' to that of IIb. Although derived from separate mRNA transcripts, the two proteins are coordinately expressed in normal and abnormal states. Pluripotential K562 cells synthesize GP IIb-IIIa during phorbol ester-induced differentiation, and this is because of increased transcription of mRNA for GP IIb and IIIa rather than to a change in mRNA stability. Full synchronization of GP IIb-IIIa expression occurs after translation of the proteins; both proteins must enter the endoplasmic reticulum in order for the heterodimer complex to form and to eventually be transported to the surface membrane of the cell. The chapter also summarizes recent studies pertaining to the molecular basis of Glanzmann's thrombasthenia and the pathogenesis of GP IIb-IIIa dysfunction in other clinical disorders.
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