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Titolo:
Platelet HDL3 binding sites are not related to integrin alpha(IIb)beta(3) (GPIIb-IIIa)
Autore:
Pedreno, J; de Castellarnau, C; Masana, L;
Indirizzi:
Univ Rovira & Virgili, Unitat Recerca Lipids & Arteriosclerosi, Fac Med, Tarragona, Spain Univ Rovira & Virgili Tarragona Spain lerosi, Fac Med, Tarragona, Spain Hosp Santa Cruz & San Pablo, Inst Recerca, Barcelona, Spain Hosp Santa Cruz & San Pablo Barcelona Spain t Recerca, Barcelona, Spain
Titolo Testata:
ATHEROSCLEROSIS
fascicolo: 1, volume: 154, anno: 2001,
pagine: 23 - 29
SICI:
0021-9150(200101)154:1<23:PHBSAN>2.0.ZU;2-J
Fonte:
ISI
Lingua:
ENG
Soggetto:
HUMAN-BLOOD PLATELETS; RECEPTOR; LDL; AGGREGATION; INHIBITION; MECHANISMS; SECRETION; PROTEINS;
Keywords:
platelets; HDL3; Glanzmann's thrombasthenia; integrin alpha(IIb)beta(3);
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Clinical Medicine
Life Sciences
Citazioni:
30
Recensione:
Indirizzi per estratti:
Indirizzo: Pedreno, J Univ Rovira & Virgili, Unitat Recerca Lipids & Arteriosclerosi,Fac Med, Sant Llorenc 21 Reus, Tarragona, Spain Univ Rovira & Virgili SantLlorenc 21 Reus Tarragona Spain in
Citazione:
J. Pedreno et al., "Platelet HDL3 binding sites are not related to integrin alpha(IIb)beta(3) (GPIIb-IIIa)", ATHEROSCLER, 154(1), 2001, pp. 23-29

Abstract

Early studies considered that fibrinogen receptor (glycoprotein [GP] IIb-IIIa or platelet integrin alpha (IIb)beta (3)) is the binding site for low-density lipoprotein (LDL) and high-density lipoprotein type 3 (HDL3). Recentdata, however, do not support the hypothesis that the binding of LDL to human intact resting platelets is related to integrin alpha (IIb)beta (3). Inthis study we present evidence that platelet integrin alpha (IIb)beta (3) is also not involved in the interaction of HDL3 and human intact resting platelets. Firstly, specific ligands for platelet integrin alpha (IIb)beta (3) such as fibrinogen, vitronectin, von Willebrand factor and fibronectin, were unable to inhibit the binding of HDL3 to intact resting platelets. Secondly, the HDL3 binding characteristics (K-d and B-max values), the activation of protein kinase C (PKC) and the inhibition of thrombin-induced inositoltriphosphate (IP3) formation and calcium (Ca2+) mobilization mediated by HDL3 particles were similar in platelets from control subjects and patients with type I and type II Glanzmann's thrombasthenia, which are characterizedby total and partial lack of GPIIb-IIIa and fibrinogen, respectively. In contrast, nitrosylation of tyrosine residues of HDL3 by tetranitromethane fully abolished both the ability of particles to interact with its specific binding sites and the functional effects. Thirdly, polyclonal antibodies against the GPIIb-IIIa complex (edu-3 and 5B12), human antiserums against platelet alloantigens (anti-Bak(a/B) and anti-PLA1/2), anti-integrin subunits (anti-alpha (v) and anti-beta (3)), and a wide panel of monoclonal antibodies (mAbs) against well-known epitopes of GPIIb (M3, M4, M5, M6, M8 and M95-2b) and GPIIIa (P23-7, P33, P37, P40, and P97) did not affect the binding ofHDL3 particles to human intact resting platelets. Overall results show that neither the GPIIb-IIIa complex nor GPIIb or GPIIIa individually are the membrane binding proteins for HDL3 on intact resting platelets. (C) 2001 Elsevier Science Ireland Ltd. All rights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 18/01/20 alle ore 01:50:38