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Titolo:
Effects of the extracellular matrix on lumican expression in rat aortic smooth muscle cells in vitro
Autore:
Qin, HJ; Ishiwata, T; Asano, G;
Indirizzi:
Nippon Med Coll, Dept Pathol, Bunkyo Ku, Tokyo 1138602, Japan Nippon Med Coll Tokyo Japan 1138602 hol, Bunkyo Ku, Tokyo 1138602, Japan
Titolo Testata:
JOURNAL OF PATHOLOGY
fascicolo: 5, volume: 195, anno: 2001,
pagine: 604 - 608
SICI:
0022-3417(200112)195:5<604:EOTEMO>2.0.ZU;2-7
Fonte:
ISI
Lingua:
ENG
Soggetto:
KERATAN SULFATE PROTEOGLYCAN; ARTERIAL INJURY; PROTEINS; COLLAGEN; DECORIN; GROWTH; PROLIFERATION; ENDOTHELIUM; PHENOTYPE; BIGLYCAN;
Keywords:
lumican; fibronectin; laminin; integrin receptor; smooth muscle cells;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Clinical Medicine
Life Sciences
Citazioni:
25
Recensione:
Indirizzi per estratti:
Indirizzo: Ishiwata, T Nippon Med Coll, Dept Pathol, Bunkyo Ku, 1-1-5 Sendagi, Tokyo 1138602, Japan Nippon Med Coll 1-1-5 Sendagi Tokyo Japan 1138602 8602, Japan
Citazione:
H.J. Qin et al., "Effects of the extracellular matrix on lumican expression in rat aortic smooth muscle cells in vitro", J PATHOLOGY, 195(5), 2001, pp. 604-608

Abstract

Lumican is a small leucine-rich proteoglycan (SLRP), which contributes to cell migration, tissue hydration, and collagen fibrillogenesis. Whether lumican is localized in rat muscle cells (SMCs) and what its relationships might be to other extracellular components have not yet been elucidated. In this study, using reverse transcription-polymerase chain reaction (RT-PCR), competitive RT-PCR, and western blot, lumican messenger ribonucleic acid (mRNA) was expressed in cultured rat aortic SMCs. SMCs cultured in serum-free medium showed four bands at 68, 62, 50, and 37 kD. The 68 and 62 kD bands corresponded to proteoglycan, the 50 kD band to glycoprotein, and the 37 kD band to the core protein form of lumican. The relationships of lumican to fibronectin and laminin were also investigated. The lumican mRNA level in SMCs cultured on fibronectin was highest at day 1, but it increased at day 3 in SMCs cultured on laminin. On the fibronectin or laminin-coated plates, SMCs, expressed only the 68 and 62 kD bands, corresponding to proteoglycan. Pretreatment with anti-beta1 integrin receptor antibody revealed a decreasein the proteoglycan forms of lumican protein and an additional two bands at 50 and 37 kD, indicating glycoprotein and the core protein of lumican. These results show that lumican was synthesized in cultured rat aortic SMCs as proteoglycan, glycoprotein, and core protein. The extracellular matrix (ECM) affected lumican protein production and restricted the lumican protein form to proteoglycan via the beta1 integrin receptor in SMCs. Copyright (C)2001 John Wiley & Sons, Ltd.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/12/20 alle ore 19:30:58