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Titolo:
Skeletal muscle cell hypertrophy induced by inhibitors of metalloproteases; myostatin as a potential mediator
Autore:
Huet, C; Li, ZF; Liu, HZ; Black, RA; Galliano, MF; Engvall, E;
Indirizzi:
Burnham Inst, La Jolla, CA 92037 USA Burnham Inst La Jolla CA USA 92037Burnham Inst, La Jolla, CA 92037 USA Hop Debrousse, INRA, INSERM, U418, F-69322 Lyon, France Hop Debrousse Lyon France F-69322 RA, INSERM, U418, F-69322 Lyon, France Immunex Res & Dev Corp, Res Adm, Seattle, WA 98101 USA Immunex Res & Dev Corp Seattle WA USA 98101 es Adm, Seattle, WA 98101 USA CHU Purpan, CNRS, UPR 2163, F-31059 Toulouse 03, France CHU Purpan Toulouse France 03 NRS, UPR 2163, F-31059 Toulouse 03, France
Titolo Testata:
AMERICAN JOURNAL OF PHYSIOLOGY-CELL PHYSIOLOGY
fascicolo: 5, volume: 281, anno: 2001,
pagine: C1624 - C1634
SICI:
0363-6143(200111)281:5<C1624:SMCHIB>2.0.ZU;2-Z
Fonte:
ISI
Lingua:
ENG
Soggetto:
TUMOR-NECROSIS-FACTOR; GROWTH-FACTOR-BETA; AMYLOID PRECURSOR PROTEIN; ALPHA-SECRETASE CLEAVAGE; MESSENGER-RNA EXPRESSION; FACTOR BINDING-PROTEINS; TRANS-GOLGI NETWORK; DISINTEGRIN-METALLOPROTEASE; MATRIX METALLOPROTEINASES; TGF-BETA;
Keywords:
metalloendopeptidases; protease inhibitor; growth and differentiation factor-8;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
80
Recensione:
Indirizzi per estratti:
Indirizzo: Engvall, E Burnham Inst, 10901 N Torrey Pines Rd, La Jolla, CA 92037 USA Burnham Inst 10901 N Torrey Pines Rd La Jolla CA USA 92037 USA
Citazione:
C. Huet et al., "Skeletal muscle cell hypertrophy induced by inhibitors of metalloproteases; myostatin as a potential mediator", AM J P-CELL, 281(5), 2001, pp. C1624-C1634

Abstract

Cell growth and differentiation are controlled in many tissues by paracrine factors, which often require proteolytic processing for activation. Metalloproteases of the metzincin family, such as matrix metalloproteases and ADAMs, recently have been shown to be involved in the shedding of growth factors, cytokines, and receptors. In the present study, we show that hydroxamate-based inhibitors of metalloproteases (HIMPs), such as TAPI and BB-3103, increase the fusion of C2C12 myoblasts and provoke myotube hypertrophy. HIMPs did not seem to effect hypertrophy via proteins that have previously been shown to regulate muscle growth in vitro, such as insulin-like growth factor-I, calcineurin, and tumor necrosis factor-alpha. Instead, the proteolytic maturation of myostatin (growth differentiation factor-8) seemed to be reduced in C2C12 cells treated with HIMPs, as suggested by the presence of nonprocessed myostatin precursor only in hypertrophic myotubes. Myostatin isa known negative regulator of skeletal muscle growth, belonging to the transforming growth factor-beta /bone morphogenetic protein superfamily. Theseresults indicate that metalloproteases are involved in the regulation of skeletal muscle growth and differentiation, that the proteolytic maturation of myostatin in C2C12 cells may be directly or indirectly linked to the activity of some unidentified HIMP-sensitive metalloproteases, and that the lack of myostatin processing on HIMP treatment may be a mediator of myotube hypertrophy in this in vitro model.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 31/03/20 alle ore 10:30:19