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Titolo:
Processing of beta-dystroglycan by matrix metalloproteinase disrupts the link between the extracellular matrix and cell membrane via the dystroglycancomplex
Autore:
Yamada, H; Saito, F; Fukuta-Ohi, H; Zhong, D; Hase, A; Arai, K; Okuyama, A; Maekawa, R; Shimizu, T; Matsumura, K;
Indirizzi:
Teikyo Univ, Sch Med, Dept Neurol & Neurosci, Tokyo 1738605, Japan Teikyo Univ Tokyo Japan 1738605 Neurol & Neurosci, Tokyo 1738605, Japan Banyu Tsukuba Res Inst, Tsukuba, Ibaraki 3002611, Japan Banyu Tsukuba Res Inst Tsukuba Ibaraki Japan 3002611 araki 3002611, Japan Shionogi & Co Ltd, Shionogi Res Labs, Osaka 5530002, Japan Shionogi & Co Ltd Osaka Japan 5530002 ogi Res Labs, Osaka 5530002, Japan
Titolo Testata:
HUMAN MOLECULAR GENETICS
fascicolo: 15, volume: 10, anno: 2001,
pagine: 1563 - 1569
SICI:
0964-6906(20010715)10:15<1563:POBBMM>2.0.ZU;2-#
Fonte:
ISI
Lingua:
ENG
Soggetto:
DYSTROPHIN-ASSOCIATED PROTEINS; CONGENITAL MUSCULAR-DYSTROPHY; GLYCOPROTEIN-COMPLEX; PERIPHERAL-NERVE; SARCOGLYCAN COMPLEX; ALPHA-DYSTROGLYCAN; LAMININ; RECEPTOR; DEFICIENCY; EXPRESSION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
43
Recensione:
Indirizzi per estratti:
Indirizzo: Matsumura, K Teikyo Univ, Sch Med, Dept Neurol & Neurosci, Tokyo 1738605, Japan Teikyo Univ Tokyo Japan 1738605 rosci, Tokyo 1738605, Japan
Citazione:
H. Yamada et al., "Processing of beta-dystroglycan by matrix metalloproteinase disrupts the link between the extracellular matrix and cell membrane via the dystroglycancomplex", HUM MOL GEN, 10(15), 2001, pp. 1563-1569

Abstract

The dystroglycan complex is a membrane-spanning complex composed of two subunits, alpha- and beta -dystroglycan. alpha -dystroglycan is a cell surface peripheral membrane protein which binds to the extracellular matrix (ECM), whereas beta -dystroglycan is an integral membrane protein which anchors alpha -dystroglycan to the cell membrane. The dystroglycan complex providesa tight link between the ECM and cell membrane. Dysfunction of the dystroglycan complex has commonly been implicated in the molecular pathogenesis ofsevere forms of hereditary neuromuscular diseases, including Duchenne muscular dystrophy, Fukuyama-type congenital muscular dystrophy and sarcoglycanopathy (LGMD2C, -D, -E and -F). To begin to clarify the pathway by which the dysfunction of the dystroglycan complex could lead to muscle cell degeneration, we investigated the proteolytic processing of the dystroglycan complex in this study. We demonstrate that (i) a 30 kDa fragment of beta -dystroglycan is expressed in peripheral nerve, kidney, lung and smooth muscle, but not skeletal muscle, cardiac muscle or brain, and (ii) this fragment is the product of proteolytic processing of the extracellular domain of beta -dystroglycan by the membrane-associated matrix metalloproteinase (MMP) activity. Importantly, furthermore, we demonstrate that this processing disintegrates the dystroglycan complex. Our results indicate that the processing ofbeta -dystroglycan by MMP causes the disruption of the link between the ECM and cell membrane via the dystroglycan complex, which could have profoundeffects on cell viability. Based on these and previously reported findings, we propose a hypothesis that this processing may play a crucial role in the molecular pathogenesis of sarcoglycanopathy.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 02/12/20 alle ore 15:34:37