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Titolo:
Binding of ADAM12, a marker of skeletal muscle regeneration, to the muscle-specific actin-binding protein, alpha-actinin-2, is required for myoblast fusion
Autore:
Galliano, MF; Huet, C; Frygelius, J; Polgren, A; Wewer, UM; Engvall, E;
Indirizzi:
La Jolla Canc Res Ctr, Burnham Inst, La Jolla, CA 92037 USA La Jolla Canc Res Ctr La Jolla CA USA 92037 Inst, La Jolla, CA 92037 USA Univ Copenhagen, Inst Mol Pathol, DK-2100 Copenhagen, Denmark Univ Copenhagen Copenhagen Denmark DK-2100 , DK-2100 Copenhagen, Denmark
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 18, volume: 275, anno: 2000,
pagine: 13933 - 13939
SICI:
0021-9258(20000505)275:18<13933:BOAAMO>2.0.ZU;2-K
Fonte:
ISI
Lingua:
ENG
Soggetto:
ADAM-12 MELTRIN-ALPHA; NECROSIS-FACTOR-ALPHA; METALLOPROTEASE-DISINTEGRIN; SECRETASE CLEAVAGE; CYTOPLASMIC DOMAIN; MEMBRANE-PROTEINS; CELL-ADHESION; FAMILY; EXPRESSION; PRECURSOR;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
39
Recensione:
Indirizzi per estratti:
Indirizzo: Engvall, E La Jolla Canc Res Ctr, Burnham Inst, 10901 N Torrey Pines Rd, La Jolla, CA92037 USA La Jolla Canc Res Ctr 10901 N Torrey Pines Rd La JollaCA USA 92037
Citazione:
M.F. Galliano et al., "Binding of ADAM12, a marker of skeletal muscle regeneration, to the muscle-specific actin-binding protein, alpha-actinin-2, is required for myoblast fusion", J BIOL CHEM, 275(18), 2000, pp. 13933-13939

Abstract

ADAM12 belongs to the transmembrane metalloprotease ADAM ("a disintegrin and metalloprotease") family. ADAM12 has been implicated in muscle cell differentiation and fusion, but its precise function remains unknown. Here, we show that ADAM12 is dramatically up-regulated in regenerated, newly formed fibers in vivo. In C2C12 cells, ADAM12 is expressed at low levels in undifferentiated myoblasts and is transiently up-regulated at the onset of differentiation when myoblasts fuse into multinucleated myotubes, whereas other ADAMs, such as ADAMs 9, 10, 15, 17, and 19, are expressed at all stages of differentiation. Using the yeast two-hybrid screen, we found that the muscle-specific alpha-actinin-2 strongly binds to the cytoplasmic tail of ADAM12. In vitro binding assays with GST fusion proteins confirmed the specific interaction. The major binding site for alpha-actinin-2 was mapped to a shortsequence in the membrane-proximal region of ADAM12 cytoplasmic tail; a second binding site was identified in the membrane-distal region. Co-immunoprecipitation experiments confirm the in vivo association of ADAM12 cytoplasmic domain with alpha-actinin-2. Overexpression of the entire cytosolic ADAM12 tail acted in a dominant negative fashion by inhibiting fusion of C2C12 cells, whereas expression of a cytosolic ADAM12 lacking the major alpha-actinin-2 binding site had no effect on cell fusion. Our results suggest that interaction of ADAM12 with alpha-actinin-2 is important for ADAM12 function.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/04/20 alle ore 08:35:45