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J. Biol. Chem., Vol. 269, Issue 26, 17424-17427, Jul, 1994
M Yagi, S Edelhoff, CM Disteche and GJ Roth
Human platelet glycoprotein Ib beta (GPIb beta) (M(r) 22,000) is part of
the GPIb-V-IX system that constitutes the receptor for von Willebrand
factor and mediates platelet adhesion in the arterial circulation. The four
members of the receptor (GPs Ib alpha, Ib beta, V, and IX) share structural
and functional features. Individually, GPIb beta contributes to surface
expression of the receptor and participates in transmembrane signaling
through phosphorylation of its intracellular domain. To define the
structure of the GPIb beta gene, a cosmid clone from a human genomic
library was analyzed. The transcriptional start site was located by both
primer extension and the "anchored" polymerase chain reaction. Similar to
the genes for Ib alpha, V, and IX, the Ib beta gene is compact with a
single 274-base intron inserted into the 5' end of the open reading frame.
The 5'-flanking region of the gene contains both GATA and ets sites that
are also found in the 5' promoter regions of other described
megakaryocyte/platelet genes. The GPIb beta gene was localized to
chromosome 22q11.2 by fluorescence in situ hybridization. The GPIb beta
gene has a simple structure, similar to that of other described
megakaryocyte/platelet genes, including those of the GPIb-V-IX system.
Structural characterization and chromosomal location of the gene encoding human platelet glycoprotein Ib beta
Hematology Section, Seattle Veterans Administration Medical Center, Washington 98108.
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