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Titolo:
Structural requirements of echistatin for the recognition of alpha(v)beta(3) and alpha(5)beta(1) integrins
Autore:
Wierzbicka-Patynowski, I; Niewiarowski, S; Marcinkiewicz, C; Calvete, JJ; Marcinkiewicz, MM; McLane, MA;
Indirizzi:
Univ Delaware, McKinly Lab 057, Dept Med Technol, Newark, DE 19808 USA Univ Delaware Newark DE USA 19808 Dept Med Technol, Newark, DE 19808 USA Temple Univ, Dept Physiol, Philadelphia, PA 19140 USA Temple Univ Philadelphia PA USA 19140 Physiol, Philadelphia, PA 19140 USA Sol Sherry Thrombosis Res Ctr, Philadelphia, PA 19140 USA Sol Sherry Thrombosis Res Ctr Philadelphia PA USA 19140 hia, PA 19140 USA CSIC, Inst Biomed, Valencia 46010, Spain CSIC Valencia Spain 46010CSIC, Inst Biomed, Valencia 46010, Spain
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 53, volume: 274, anno: 1999,
pagine: 37809 - 37814
SICI:
0021-9258(199912)274:53<37809:SROEFT>2.0.ZU;2-I
Fonte:
ISI
Lingua:
ENG
Soggetto:
NUCLEAR-MAGNETIC-RESONANCE; GLUTATHIONE-S-TRANSFERASE; III CONNECTING SEGMENT; LIGAND-BINDING; SECONDARY STRUCTURE; VIPER VENOMS; GPIIB-IIIA; ALPHA-V-BETA-3 INTEGRINS; BETA(3) INTEGRIN; ESCHERICHIA-COLI;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
40
Recensione:
Indirizzi per estratti:
Indirizzo: McLane, MA Univ Delaware, McKinly Lab 057, Dept Med Technol, Newark, DE 19808 USA Univ Delaware Newark DE USA 19808 echnol, Newark, DE 19808 USA
Citazione:
I. Wierzbicka-Patynowski et al., "Structural requirements of echistatin for the recognition of alpha(v)beta(3) and alpha(5)beta(1) integrins", J BIOL CHEM, 274(53), 1999, pp. 37809-37814

Abstract

There are key differences between the amino acid residues of the RGD loopsand the C termini of echistatin, a potent antagonist of alpha(IIb)beta(3),alpha(v)beta(3) and alpha(5)beta(1), and eristostatin, a similar disintegrin selectively inhibiting alpha(IIb)beta(3),. In order to identify echistatin motifs required for selective recognition of alpha(v)beta(3) and alpha(5)beta(1) integrins, we expressed recombinant echistatin, eristostatin, and 15 hybrid molecules. We tested them for their ability to inhibit adhesion of different cell lines to fibronectin and von Willebrand factor and to express ligand-induced binding site epitope. The results showed that Asp(27) and Met(28) support recognition of both alpha(v)beta(3) and alpha(5)beta(1). Replacement of Met(28) with Asn completely abolished echistatin's ability to recognize each of the integrins, while replacement of Met(28) with Leu selectively decreased echistatin's ability to recognize alpha(5)beta(1) only. Eristostatin in which C-terminal WNG sequence was substituted with HKGPAT exhibited new activity with alpha(5)beta(1), which was 10-20-fold higher than that of wild type eristostatin, A hypothesis is proposed that the C terminus of echistatin interacts with separate sites on beta(1) and beta(3) integrin molecules.

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Documento generato il 09/07/20 alle ore 00:22:46