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Titolo:
Glycoprotein Ib/IX/V binding to the membrane skeleton maintains shear-induced platelet aggregation
Autore:
Christodoulides, N; Feng, SJ; Resendiz, JC; Berndt, MC; Kroll, MH;
Indirizzi:
Vet Affairs Med Ctr, Hematol Oncol Sect, Houston, TX 77030 USA Vet AffairsMed Ctr Houston TX USA 77030 ncol Sect, Houston, TX 77030 USA Baylor Coll Med, Houston, TX 77030 USA Baylor Coll Med Houston TX USA 77030 ylor Coll Med, Houston, TX 77030 USA Rice Univ, Houston, TX 77030 USA Rice Univ Houston TX USA 77030Rice Univ, Houston, TX 77030 USA Baker Med Res Inst, Prahran, Vic 3181, Australia Baker Med Res Inst Prahran Vic Australia 3181 rahran, Vic 3181, Australia
Titolo Testata:
THROMBOSIS RESEARCH
fascicolo: 2, volume: 102, anno: 2001,
pagine: 133 - 142
SICI:
0049-3848(20010415)102:2<133:GIBTTM>2.0.ZU;2-O
Fonte:
ISI
Lingua:
ENG
Soggetto:
IB-IX COMPLEX; VONWILLEBRAND-FACTOR; BLOOD-PLATELETS; ACTIN POLYMERIZATION; CYTOPLASMIC DOMAIN; VWF MULTIMERS; STRESS; CYTOSKELETON; FILAMENTS;
Keywords:
shear stress; glycoprotein Ib; von willebrand factor; signal transduction; actin; platelet aggregation;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
20
Recensione:
Indirizzi per estratti:
Indirizzo: Kroll, MH Vet Affairs Med Ctr, Hematol Oncol Sect, 111H,2002 Holcombe Blvd, Houston,TX 77030 USA Vet Affairs Med Ctr 111H,2002 Holcombe Blvd Houston TX USA 77030
Citazione:
N. Christodoulides et al., "Glycoprotein Ib/IX/V binding to the membrane skeleton maintains shear-induced platelet aggregation", THROMB RES, 102(2), 2001, pp. 133-142

Abstract

The extracellular domain of glycoprotein (Gp) Ib alpha serves as the von Willebrand factor (vWf) receptor that triggers shear stress-dependent platelet aggregation. Its intracellular domain associates with actin-binding protein-280 (filamin la) that binds directly to filamentous actin, thereby linking the membrane skeleton to GpIb alpha. We examined the functional significance of GpIb alpha interactions with actin during platelet aggregation in response to 120 dyn/ cm(2) shear stress. Lysates of resting and sheared platelets were centrifuged at similar to 13,000 x g for 15 min, and GpIb alphawas immunoprecipitated from the lysate supernatant. CpIb alpha and coimmunoprecipitated proteins were separated by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) and immunoblotted with antibodies specific for GpIb alpha and actin. We observed a significant increase in the amounts of actin coimmunoprecipitating with CpIb alpha: as platelets aggregatedin response to shear stress. Actin/GpIb alpha interactions reached a maximum after 90 s of sheer stress. Monoclonal antibody(mAb) blockade of vWf binding to GpIb alpha inhibited shear stress-induced platelet aggregation and actin associating with GpIb alpha. Pretreatment of platelets with cytochalasin D resulted in the inhibition of actin binding to GpIb alpha, in shearedplatelets and in an increase in the rate and magnitude of platelet disaggregation. These data indicate that shear stress causes changes in the association between GpIb alpha and the actin-based membrane skeleton. The increased interaction between GpIb alpha and the actin-based membrane skeleton results from shear-induced vWf binding to GpIb alpha and is mechanoprotective in that it maintains shear-induced aggregation of activated platelets. (C) 2001 Elsevier Science Ltd. All rights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 26/01/20 alle ore 22:46:41