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Titolo:
Identification, characterization, and functional analysis of heart-specific myosin light chain phosphatase small subunit
Autore:
Arimura, T; Suematsu, N; Zhou, YB; Nishimura, J; Satoh, S; Takeshita, A; Kanaide, H; Kimura, A;
Indirizzi:
Tokyo Med & Dent Univ, Med Res Inst, Div Adult Dis, Div Mol Pathogenesis,Chiyoda Ku, Tokyo 1010062, Japan Tokyo Med & Dent Univ Tokyo Japan 1010062iyoda Ku, Tokyo 1010062, Japan Kyushu Univ, Grad Sch Med Sci, Dept Cardiovasc Med, Fukuoka 8128582, JapanKyushu Univ Fukuoka Japan 8128582 Cardiovasc Med, Fukuoka 8128582, Japan Kyushu Univ, Fac Med, Angiocardiol Res Inst, Div Mol Cardiol, Fukuoka 8128582, Japan Kyushu Univ Fukuoka Japan 8128582 iv Mol Cardiol, Fukuoka 8128582, Japan Tokyo Med & Dent Univ, Med Res Inst, Etiol & Pathogenesis Res Unit, Tokyo 1010062, Japan Tokyo Med & Dent Univ Tokyo Japan 1010062 Res Unit, Tokyo 1010062, Japan
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 9, volume: 276, anno: 2001,
pagine: 6073 - 6082
SICI:
0021-9258(20010302)276:9<6073:ICAFAO>2.0.ZU;2-Q
Fonte:
ISI
Lingua:
ENG
Soggetto:
SMOOTH-MUSCLE MYOSIN; KINASE-RELATED PROTEIN; PORCINE RENAL-ARTERY; REGULATORY SUBUNIT; MOLECULAR-CLONING; CA2+ SENSITIVITY; CALCIUM SENSITIVITY; TARGET SUBUNIT-1; BINDING PROTEIN; CARDIAC-CELLS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
53
Recensione:
Indirizzi per estratti:
Indirizzo: Kimura, A Tokyo Med & Dent Univ, Med Res Inst, Div Adult Dis, Div Mol Pathogenesis,Chiyoda Ku, 2-3-10 Kandasurugadai, Tokyo 1010062, Japan Tokyo Med & Dent Univ 2-3-10 Kandasurugadai Tokyo Japan 1010062
Citazione:
T. Arimura et al., "Identification, characterization, and functional analysis of heart-specific myosin light chain phosphatase small subunit", J BIOL CHEM, 276(9), 2001, pp. 6073-6082

Abstract

Myosin light chain phosphatase consists of three subunits, a 38-kDa catalytic subunit, a large 110-130-kDa myosin binding subunit, and a small subunit of 20-21 kDa. The catalytic subunit and the large subunit have been well characterized. The small subunit has been cloned and studied from smooth muscle, but little is known about its function and specificity in the other muscles such as cardiac muscle. In this study, cDNAs for heart-specific small subunit isoforms, hHS-M-21, were isolated and characterized. Evidence wasobtained from an analysis of genome to suggest that the small subunit was the product of the same gene as the large subunit. Using permeabilized renal artery preparation and permeabilized cardiac myocytes, it was shown that the small subunit increased sensitivity to Ca2+ in muscle contraction. It was also shown using an overlay assay that hHS-M-21 bound the large subunit. Mapping experiments demonstrated that the binding domain and the domain involved in the increasing Ca2+ sensitivity mapped to the same N-terminal region of hHS-M-21. These observations suggest that the heart-specific small subunit hHS-M-21 plays a regulatory role in cardiac muscle contraction by its binding to the large subunit.

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Documento generato il 25/11/20 alle ore 01:34:05