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J Biol Chem, Vol. 273, Issue 28, 17531-17538, July 10, 1998
-Filamin Is a New Protein That Interacts with the
Cytoplasmic Tail of Glycoprotein Ib
,,
From the We have cloned and sequenced a 9.4-kilobase
cDNA specifying a new 280-kDa protein interacting with the
cytoplasmic tail of glycoprotein (Gp) Ib Cardeza Foundation for Hematologic Research,
and showing considerable
homology to actin-binding protein 280 (ABP-280) and chicken retinal
filamin. We term this protein human 
-filamin. The gene for
-filamin localizes to chromosome 3p14.3-p21.1. -Filamin mRNA
expression was observed in many tissues and in cultured human umbilical
vein endothelial cells (HUVECs); only minimal expression was detected
in platelets and the megakaryocytic cell line CHRF-288. Like ABP-280,
-filamin contains an NH2-terminal actin-binding
domain, a backbone of 24 tandem repeats, and two "hinge" regions. A
polyclonal antibody to the unique -filamin first hinge sequence
identifies a strong 280-kDa band in HUVECs but only a weak band in
platelets, and stains normal human endothelial cells in culture and
in situ. We have confirmed the interaction of -filamin
and GpIb in platelet and HUVEC lysates. In addition, using
two-hybrid analysis with deletion mutants, we have localized the
binding domain for GpIb in -filamin to residues 1862-2148, an
area homologous to the GpIb binding domain in ABP-280. -Filamin is a new member of the filamin family that may have significance for
GpIb function in endothelial cells and platelets.
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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