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Titolo:
MOLECULAR-CLONING OF THE CDNA-ENCODING HUMAN SKELETAL-MUSCLE TRIADIN AND ITS LOCALIZATION TO CHROMOSOME 6Q22-6Q23
Autore:
TASKE NL; EYRE HJ; OBRIEN RO; SUTHERLAND GR; DENBOROUGH MA; FOSTER PS;
Indirizzi:
AUSTRALIAN NATL UNIV,JOHN CURTIN SCH MED RES,DIV BIOCHEM & MOLEC BIOLCANBERRA ACT 0200 AUSTRALIA AUSTRALIAN NATL UNIV,JOHN CURTIN SCH MED RES,DIV BIOCHEM & MOLEC BIOLCANBERRA ACT 0200 AUSTRALIA WOMENS & CHILDRENS HOSP,CTR MED GENET,DEPT CYTOGENET & MOLEC GENET ADELAIDE SA AUSTRALIA
Titolo Testata:
European journal of biochemistry
fascicolo: 1, volume: 233, anno: 1995,
pagine: 258 - 265
SICI:
0014-2956(1995)233:1<258:MOTCHS>2.0.ZU;2-Y
Fonte:
ISI
Lingua:
ENG
Soggetto:
CALCIUM-RELEASE CHANNEL; RETICULUM GLYCOPROTEIN TRIADIN; PURIFIED RYANODINE RECEPTOR; JUNCTIONAL FOOT PROTEIN; SARCOPLASMIC-RETICULUM; DIHYDROPYRIDINE RECEPTOR; ULTRASTRUCTURAL-LOCALIZATION; COMPLEMENTARY-DNA; DYSGENIC MUSCLE; CALSEQUESTRIN;
Keywords:
TRIADIN; EXCITATION CONTRACTION COUPLING; SKELETAL MUSCLE; MALIGNANT HYPERTHERMIA; CHROMOSOME 6;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
39
Recensione:
Indirizzi per estratti:
Citazione:
N.L. Taske et al., "MOLECULAR-CLONING OF THE CDNA-ENCODING HUMAN SKELETAL-MUSCLE TRIADIN AND ITS LOCALIZATION TO CHROMOSOME 6Q22-6Q23", European journal of biochemistry, 233(1), 1995, pp. 258-265

Abstract

We have cloned and sequenced the cDNA encoding triadin, a junctional terminal cisternae protein from human skeletal muscle. The cDNA, 2941 base pairs, in length, encodes a protein of 729 amino acids with a predicted molecular mass of 81545 Da. Hydropathy analysis indicates that triadin of human skeletal muscle has the same topology in the myoplasmic, transmembrane and sarcoplasmic reticulum luminal domains as that of triadin from rabbit skeletal muscle, The number and relative position of potential modulation sites are also conserved between the human and rabbit proteins. The cDNA sequence of the predicted sarcoplasmic reticulum luminal domain of human triadin diverged from that of rabbit, with an observed similarity of 82%, translating to an identity of 77% in amino acid sequence. Two insertions of 9 and 12 residues in the amino acid sequence were observed in the predicted luminal domain of triadin, although the structural and functional consequences of such insertions are expected to be minimal. Using fluorescence in situ hybridisation, we have assigned the gene encoding human triadin to the long armof chromosome 6 in the region 6q22-6q23. Our structural analysis of human triadin supports a central role for this protein in the mechanismof skeletal muscle excitation/contraction coupling.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 07/07/20 alle ore 12:18:59