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Titolo:
Molecular characterization of L-amino acid oxidase from Agkistrodon halys blomhoffii with special reference to platelet aggregation
Autore:
Takatsuka, H; Sakurai, Y; Yoshioka, A; Kokubo, T; Usami, Y; Suzuki, M; Matsui, T; Titani, K; Yagi, H; Matsumoto, M; Fujimura, Y;
Indirizzi:
Nara Med Univ, Dept Blood Transfus Med, Kashihara, Nara 6348522, Japan Nara Med Univ Kashihara Nara Japan 6348522 Kashihara, Nara 6348522, Japan Fujita Hlth Univ, Inst Comprehens Med Sci, Toyoake, Aichi 4701192, Japan Fujita Hlth Univ Toyoake Aichi Japan 4701192 oyoake, Aichi 4701192, Japan Gifu Pharmaceut Coll, Dept Publ Hlth Pharm, Gifu 5028585, Japan Gifu Pharmaceut Coll Gifu Japan 5028585 Hlth Pharm, Gifu 5028585, Japan Nara Med Univ, Dept Pediat, Kashihara, Nara 6348522, Japan Nara Med Univ Kashihara Nara Japan 6348522 Kashihara, Nara 6348522, Japan
Titolo Testata:
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEIN STRUCTURE AND MOLECULAR ENZYMOLOGY
fascicolo: 1-2, volume: 1544, anno: 2001,
pagine: 267 - 277
SICI:
0167-4838(20010112)1544:1-2<267:MCOLAO>2.0.ZU;2-1
Fonte:
ISI
Lingua:
ENG
Soggetto:
SNAKE-VENOM; HYDROGEN-PEROXIDE; GLYCOPROTEIN IB; PURIFICATION; APOPTOSIS; JARARACA; BLOOD;
Keywords:
L-amino acid oxidase; snake venom; purification; cDNA cloning; platelet aggregation;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
24
Recensione:
Indirizzi per estratti:
Indirizzo: Fujimura, Y Nara Med Univ, Dept Blood Transfus Med, Kashihara, Nara 6348522, Japan Nara Med Univ Kashihara Nara Japan 6348522 ara 6348522, Japan
Citazione:
H. Takatsuka et al., "Molecular characterization of L-amino acid oxidase from Agkistrodon halys blomhoffii with special reference to platelet aggregation", BBA-PROT ST, 1544(1-2), 2001, pp. 267-277

Abstract

L-Amino acid oxidase (LAO, EC 1.4.3.2) is widely distributed in snake venom, and induces apoptosis in vascular endothelial cells, causing prolonged bleeding from vessel walls at bite sites. The effect of snake venom LAOs on platelet function is controversial. Further, we have little information on their structural characterization. We purified M (mamushi)LAO, a single-chain glycoprotein with a molecular mass of 60 kDa and a pI of 4.9, from Agkistrodon halys blomhoffii (Japanese mamushi) venom, and determined the N-terminal and several internal amino acid sequences of this enzyme. Molecular cloning based on these data was conducted to elucidate its full-length cDNA structure (2192 nucleotides), which includes a putative 18 amino acid residue signal peptide and a 504 residue mature subunit. The predicted M-LAO translation product shares 87.35% identity with that of Crotalus adamanteus (Southeastern diamondback rattlesnake) LAG. M-LAO, up to a final concentrationof 2.6 muM, inhibited both agonist- and shear stress-induced platelet aggregation (SIPA) dose-dependently. In agonist-induced platelet aggregation, M-LAO predominantly inhibited the second aggregation, but with a marginal inhibition of the first. In SIPA, the inhibition was more dramatic under low-shear stress than high-shear stress, and was enhanced by the presence of L-leucine, a substrate of this enzyme. Catalase, a H2O2 scavenger, totally quenched such enhancement. These results suggest that M-LAO inhibits the interaction between activated platelet integrin alpha IIb/beta3 and fibrinogen through the continuous generation of H2O2, and may contribute to prolonged bleeding from the vessels at snake bite sites. (C) 2001 Elsevier Science B.V. All rights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/04/20 alle ore 02:09:18