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Titolo:
Protein interaction studies of MAGP-1 with tropoelastin and fibrillin-1
Autore:
Jensen, SA; Reinhardt, DP; Gibson, MA; Weiss, AS;
Indirizzi:
Univ Sydney, Dept Biochem G08, Sydney, NSW 2006, Australia Univ Sydney Sydney NSW Australia 2006 em G08, Sydney, NSW 2006, Australia Med Univ Lubeck, Dept Med Mol Biol, D-23538 Lubeck, Germany Med Univ Lubeck Lubeck Germany D-23538 Mol Biol, D-23538 Lubeck, Germany Univ Adelaide, Dept Pathol, Adelaide, SA 5005, Australia Univ Adelaide Adelaide SA Australia 5005 ol, Adelaide, SA 5005, Australia
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 43, volume: 276, anno: 2001,
pagine: 39661 - 39666
SICI:
0021-9258(20011026)276:43<39661:PISOMW>2.0.ZU;2-Q
Fonte:
ISI
Lingua:
ENG
Soggetto:
ELASTIN-ASSOCIATED MICROFIBRILS; GLYCOPROTEIN-1 MAGP-1; TERMINAL DOMAIN; CALCIUM; BINDS; TRANSGLUTAMINASE; COACERVATION; ORGANIZATION; EXPRESSION; COLLAGEN;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
28
Recensione:
Indirizzi per estratti:
Indirizzo: Weiss, AS Univ Sydney, Dept Biochem G08, Sydney, NSW 2006, Australia Univ Sydney Sydney NSW Australia 2006 dney, NSW 2006, Australia
Citazione:
S.A. Jensen et al., "Protein interaction studies of MAGP-1 with tropoelastin and fibrillin-1", J BIOL CHEM, 276(43), 2001, pp. 39661-39666

Abstract

Elastic fibers consist primarily of an amorphous elastin core associated with microfibrils, 10-12 nm in diameter, containing fibrillins and microfibril-associated glycoproteins (MAGPs). To investigate the interaction of MAGP-1 with tropoelastin and fibrillin-1, we expressed human MAGP-1 as a T7-tagfusion protein in Escherichia coli. Refolding of the purified protein produced a soluble form of MAGP-1 that displayed saturable binding to tropoelastin. Fragments of tropoelastin corresponding to the N-terminal, C-terminal,and central regions of the molecule were used to characterize the MAGP-1 binding site. Cleavage of tropoelastin with kallikrein, which cleaves after Arg(515) in the central region of the molecule, disrupted the interaction, suggesting that the separated N- and C-terminal fragments were insufficientto determine MAGP-1 binding to intact tropoelastin. In addition, no evidence of an interaction was observed between MAGP-1 and a tropoelastin construct consisting of domains 17-27 that brackets the kallikrein cleavage site, suggesting a complex mechanism of interaction be. tween the two molecules. Binding of MAGP-1 was also tested with overlapping recombinant fibrillin-1 fragments. MAGP-1 bound to a region at the N terminus of fibrillin-1 in a calcium-dependent manner. In summary, these results suggest a model for the interaction of elastin with the microfibrillar scaffold.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 10/07/20 alle ore 00:09:17