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Blood, Vol. 92 No. 4 (August 15), 1998:
pp. 1268-1276
A Novel Human Actin-Binding Protein Homologue That Binds to
Platelet Glycoprotein Ib
Wen-feng Xu,
Zhi-wei Xie,
Dominic W. Chung, and
Earl W. Davie
From the Department of Biochemistry, University of Washington,
Seattle, WA.
Glycoprotein (GP)Ib-IX-V is one of the major transmembrane complexes
present on the platelet surface. Its extracellular domain binds von
Willebrand factor (vWF) and thrombin, while its intracellular domain
associates tightly with the cytoskeleton through the actin-binding protein (ABP)-280, also known as filamin. In the present study, a
full-length cDNA coding for a human ABP homologue has been cloned and
sequenced. This protein was identified by the yeast two-hybrid screening procedure via its interaction with the intracellular domain
of GPIb . Initially, a 1.3-kb partial cDNA was isolated from a
megakaryocyte-like cell line (K562) cDNA library followed by a
full-length cDNA of 9.4 kb that was identified in a human placenta
library. The full-length cDNA encoded a protein of 2,578 amino acids
with a calculated molecular weight of 276 kD (ABP-276). The amino
terminal 248 amino acids contained an apparent actin binding domain
followed by 24 tandem repeats each containing about 96 amino acids. The
amino acid sequence of the protein shared a high degree of homology
with human endothelial ABP-280 (70% identity) and chicken filamin
(83% identity). However, the 32 amino acid Hinge I region in ABP-280
that contains a calpain cleavage site conferring flexibility on the
molecule, was absent in the homologue. An isoform containing a 24 amino
acid insertion with a unique sequence at the missing Hinge I region was
also identified (ABP-278). This isoform resulted from alternative RNA
splicing. ABP-276 and/or ABP-278 were present in all tissues
examined, but the relative amount varied in that some tissue contained
both forms, while other tissue contained predominately one or the
other.
© 1998 by The American Society of Hematology.
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