|
|
 Previous Article | Table of Contents | Next Article 
Assembly and GPIIIa content of cytoskeletal core in platelets agglutinated
with bovine von Willebrand factor
EG Puszkin, EA Mauss and MB Zucker
Department of Pathology, Montefiore Medical Center, Albert Einstein College
of Medicine, Bronx, NY 10467.
The association between occupancy of the von Willebrand factor (vWf)
receptor glycoprotein (GP) Ib, agglutination, and the assembly and
composition of the cytoskeletal core was studied in 125I-surface- labeled
aspirin-treated washed platelets. Binding of ligands to GPIIb- IIIa and
platelet aggregation were abolished by addition of EDTA. Platelet
agglutination induced by bovine vWf generated a complete cytoskeletal core
(Triton-insoluble residue), shown by sodium dodecyl sulfate polyacrylamide
gel electrophoresis (SDS-PAGE) to be composed of actin-binding protein
(ABP) (260 Kd), 235-Kd protein, myosin heavy chain (200 Kd), alpha-actinin
(100 Kd), and actin (43 Kd). In addition, autoradiography of the gels
showed a 125I 105-Kd GP, identified by immunoblot as GPIIIa, as well as
GPIb, GPIIb, and another band at 87 Kd, probably GPIV. Neither cytoskeletal
assembly nor GPIIa incorporation was altered if calpain was inhibited with
leupeptin. Platelet suspensions exposed to bovine vWf without stirring (ie,
nonagglutinated) or platelets in which agglutination was inhibited with ADP
showed smaller cytoskeletons with little ABP, 235 Kd protein, and
alpha-actinin. Autoradiographs showed mainly GPIb. Cytochalasin D (CD) and
monobromobimane (MB) enhanced agglutination and prevented the inhibitory
action of ADP on bovine vWf-induced platelet agglutination. CD markedly
inhibited the assembly of the cytoskeletal core as well as GPIIIa
retention, whereas MB resulted in a large Triton-insoluble residue which
contained GPIIIa. Thus, development of a platelet cytoskeletal core is
apparently not required for agglutination, but when a cytoskeletal core is
assembled in agglutinated platelets, GPIIIa is retained.
Volume 76,
Issue 8,
pp. 1572-1579,
10/15/1990
Copyright © 1990 by The American Society of Hematology
 CiteULike  Connotea  Del.icio.us  Digg  Reddit  Technorati What's this?
This article has been cited by other articles:
|
|
|
|
 
R. J. Bodnar, X. Xi, Z. Li, M. C. Berndt, and X. Du
Regulation of Glycoprotein Ib-IX-von Willebrand Factor Interaction by cAMP-dependent Protein Kinase-mediated Phosphorylation at Ser 166 of Glycoprotein Ibbeta
J. Biol. Chem.,
November 27, 2002;
277(49):
47080 - 47087.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
S. L. Cranmer, P. Ulsemer, B. M. Cooke, H. H. Salem, C. de la Salle, F. Lanza, and S. P. Jackson
Glycoprotein (GP) Ib-IX-transfected Cells Roll on a von Willebrand Factor Matrix under Flow. IMPORTANCE OF THE GPIb/ACTIN-BINDING PROTEIN (ABP-280) INTERACTION IN MAINTAINING ADHESION UNDER HIGH SHEAR
J. Biol. Chem.,
March 5, 1999;
274(10):
6097 - 6106.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
G. D. Englund, R. J. Bodnar, Z. Li, Z. M. Ruggeri, and X. Du
Regulation of von Willebrand Factor Binding to the Platelet Glycoprotein Ib-IX by a Membrane Skeleton-dependent Inside-out Signal
J. Biol. Chem.,
May 11, 2001;
276(20):
16952 - 16959.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
