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Titolo:
Megakaryocyte hyperplasia and enhanced agonist-induced platelet activationin vasodilator-stimulated phosphoprotein knockout mice
Autore:
Hauser, W; Knobeloch, KP; Eigenthaler, M; Gambaryan, S; Krenn, V; Geiger, J; Glazova, M; Rohde, E; Horak, I; Walter, U; Zimmer, M;
Indirizzi:
Univ Wurzburg, Inst Klin Biochem & Pathobiochem, D-97080 Wurzburg, GermanyUniv Wurzburg Wurzburg Germany D-97080 iochem, D-97080 Wurzburg, Germany Univ Wurzburg, Inst Pathol, D-97080 Wurzburg, Germany Univ Wurzburg Wurzburg Germany D-97080 Pathol, D-97080 Wurzburg, Germany Forschungsinst Mol Pharmakol, Abt Mol Genet, D-12207 Berlin, Germany Forschungsinst Mol Pharmakol Berlin Germany D-12207 2207 Berlin, Germany Russian Acad Sci, IM Sechenov Evolutionary Physiol & Biochem Inst, St Petersburg 194223, Russia Russian Acad Sci St Petersburg Russia 194223 t Petersburg 194223, Russia
Titolo Testata:
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
fascicolo: 14, volume: 96, anno: 1999,
pagine: 8120 - 8125
SICI:
0027-8424(19990706)96:14<8120:MHAEAP>2.0.ZU;2-J
Fonte:
ISI
Lingua:
ENG
Soggetto:
DEPENDENT PROTEIN-KINASE; INTACT HUMAN PLATELETS; RICH FOCAL ADHESION; VASP IN-VITRO; LISTERIA-MONOCYTOGENES; PHOSPHORYLATION; DOMAIN; CELLS; LOCALIZATION; CYTOSKELETON;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
36
Recensione:
Indirizzi per estratti:
Indirizzo: Walter, U Univ Wurzburg, Inst Klin Biochem & Pathobiochem, Josef SchneiderStr 2, D-97080 Wurzburg, Germany Univ Wurzburg Josef Schneider Str 2 Wurzburg Germany D-97080 ny
Citazione:
W. Hauser et al., "Megakaryocyte hyperplasia and enhanced agonist-induced platelet activationin vasodilator-stimulated phosphoprotein knockout mice", P NAS US, 96(14), 1999, pp. 8120-8125

Abstract

Vasodilator-stimulated phosphoprotein (VASP), a substrate of cAMP- and cGMP-dependent protein kinases, is associated with focal adhesions, cell-cell contacts, microfilaments,and highly dynamic membrane regions. VASP, which is expressed in most cell types and in particularly high levels inhuman platelets, binds to profilin, zyxin, vinculin, F-actin, and the Listeria monocytogenes surface protein ActA. VASP is a member of the enabled (Ena)/VASP protein family and is thought to be involved in actin filament formation and integrin alpha(IIb)beta(3) inhibition in human platelets. To gain further insight into the in vivo function of this protein, VASP-deficient mice were generated by homologous recombination. VASP-/- mice demonstrated hyperplasia of megakaryocytes in bone marrow and spleen but exhibited no other macroscopic or microscopic abnormalities. Activation of platelets with thrombin induced a more than 2-fold higher surface expression of P-selectin and fibrinogen binding in VASP-deficient platelets in comparison to wild type. Thesedata support the concept that VASP is a negative modulator of platelet andintegrin alpha(IIb)beta(3) activation. Although the limited phenotypic differences between wild-type and VASP-/- mice suggested functional compensation of VASP by members of the Ena/VASP family, alterations in the expressionlevels of mammalian enabled (Mena) and Ena-VASP-like (Evl) protein were not detected. VASP-deficient mice may provide an interesting model system fordiseases in which enhanced platelet activation plays a major role.

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Documento generato il 28/11/20 alle ore 15:54:36