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Titolo:
BIOCHEMICAL-CHARACTERIZATION AND MOLECULAR-CLONING OF CARDIAC TRIADIN
Autore:
GUO W; JORGENSEN AO; JONES LR; CAMPBELL KP;
Indirizzi:
UNIV IOWA,COLL MED,DEPT PHYSIOL & BIOPHYS,HOWARD HUGHES MED INST,400 ECKSTEIN MED RES BLDG IOWA CITY IA 52242 UNIV IOWA,COLL MED,DEPT PHYSIOL & BIOPHYS,HOWARD HUGHES MED INST IOWACITY IA 52242 UNIV TORONTO,DEPT ANAT & CELL BIOL TORONTO ON M5S 1A8 CANADA INDIANA UNIV,SCH MED,KRANNERT INST CARDIOL INDIANAPOLIS IN 46202 INDIANA UNIV,SCH MED,DEPT MED INDIANAPOLIS IN 46202
Titolo Testata:
The Journal of biological chemistry
fascicolo: 1, volume: 271, anno: 1996,
pagine: 458 - 465
SICI:
0021-9258(1996)271:1<458:BAMOCT>2.0.ZU;2-I
Fonte:
ISI
Lingua:
ENG
Soggetto:
RETICULUM GLYCOPROTEIN TRIADIN; SARCOPLASMIC-RETICULUM; VENTRICULAR MUSCLE; ULTRASTRUCTURAL-LOCALIZATION; CALCIUM RELEASE; CALSEQUESTRIN; RYANODINE; PROTEIN; RECEPTOR; CHANNEL;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
28
Recensione:
Indirizzi per estratti:
Citazione:
W. Guo et al., "BIOCHEMICAL-CHARACTERIZATION AND MOLECULAR-CLONING OF CARDIAC TRIADIN", The Journal of biological chemistry, 271(1), 1996, pp. 458-465

Abstract

Triadin is an intrinsic membrane protein first identified in the skeletal muscle junctional sarcoplasmic reticulum and is considered to play an important role in excitation-contraction coupling, Using polyclonal antibodies to skeletal muscle triadin, me have identified and characterized three isoforms in rabbit cardiac muscle. The cDNAs encoding these three isoforms of triadin have been isolated by reverse transcription-polymerase chain reaction and cDNA library screening. The deducedamino acid sequences show that these proteins are identical in their N-terminal sequences, whereas the C-terminal sequences are distinct from each other and from that of skeletal muscle triadin. Based upon both the amino acid sequences and biochemical analysis, all three triadinisoforms share similar membrane topology with skeletal muscle triadin. Immunofluorescence staining of rabbit cardiac muscle with antibodiespurified from the homologous region of triadin shows that cardiac triadin is primarily confined to the I-band region of cardiac myocytes, where the junctional and corbular sarcoplasmic reticulum is located, Furthermore, we demonstrate that the conserved region of the luminal domain of triadin is able to bind both the ryanodine receptor and calsequestrin in cardiac muscle. These results suggest that triadin colocalizes with and binds to the ryanodine receptor and calsequestrin and carries out a function in the lumen of the junctional sarcoplasmic reticulum that is important for both skeletal and cardiac muscle excitation-contraction coupling.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 02/07/20 alle ore 21:53:17