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Titolo:
Identification of triadin 1 as the predominant triadin isoform expressed in mammalian myocardium
Autore:
Kobayashi, YM; Jones, LR;
Indirizzi:
Indiana Univ, Sch Med, Krannert Inst Cardiol, Indianapolis, IN 46202 USA Indiana Univ Indianapolis IN USA 46202 ardiol, Indianapolis, IN 46202 USA Indiana Univ, Sch Med, Dept Med, Indianapolis, IN 46202 USA Indiana Univ Indianapolis IN USA 46202 pt Med, Indianapolis, IN 46202 USA Indiana Univ, Sch Med, Dept Biochem & Mol Biol, Indianapolis, IN 46202 USAIndiana Univ Indianapolis IN USA 46202 l Biol, Indianapolis, IN 46202 USA
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 40, volume: 274, anno: 1999,
pagine: 28660 - 28668
SICI:
0021-9258(19991001)274:40<28660:IOT1AT>2.0.ZU;2-2
Fonte:
ISI
Lingua:
ENG
Soggetto:
JUNCTIONAL SARCOPLASMIC-RETICULUM; CORE-GLYCOSYLATION EFFICIENCY; CANINE CARDIAC CALSEQUESTRIN; AMINO-ACID SEQUENCE; SKELETAL-MUSCLE; RYANODINE RECEPTOR; BIOCHEMICAL-CHARACTERIZATION; DIHYDROPYRIDINE RECEPTOR; IMPORTANT DETERMINANT; GLYCOPROTEIN TRIADIN;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
29
Recensione:
Indirizzi per estratti:
Indirizzo: Jones, LR Indiana Univ, Sch Med, Krannert Inst Cardiol, 1111 W Tenth St, Indianapolis, IN 46202 USA Indiana Univ 1111 W Tenth St Indianapolis IN USA 46202 46202 USA
Citazione:
Y.M. Kobayashi e L.R. Jones, "Identification of triadin 1 as the predominant triadin isoform expressed in mammalian myocardium", J BIOL CHEM, 274(40), 1999, pp. 28660-28668

Abstract

Triadin is an integral membrane protein of sarcoplasmic reticulum shown tointeract with the ryanodine receptor/Ca2+ release channel, junctin, and calsequestrin. Several triadin isoforms have been postulated to exist in cardiac muscle, but to date none has been conclusively identified. Here, we show that only triadin 1 is significantly expressed. We cloned and sequenced cDNAs encoding canine cardiac triadin 1 and 3 but found no evidence for triadin 2. From deduced primary structures, antibodies against domains common to all triadins and an antibody against the unique C terminus of triadin 1 were raised. All antibodies detected two prominent proteins of molecular masses 35 and 40 kDa on immunoblots from cardiac microsomes, including the antibody that recognizes only triadin 1. The 40-kDa mobility form was shown tocorrespond to the glycosylated form of triadin 1, not a distinct triadin 2isoform as previously hypothesized. Confirming this, overexpression of triadin 1 in transgenic mouse hearts produced both the 35-kDa deglycosylated and the 40-kDa glycosylated mobility forms. The glycosylation site of triadin 1 was localized to asparagine residue 75, and its bitopic arrangement in the membrane was confirmed. Although a 92-kDa immunoreactive protein could be tentatively identified in myocardium as triadin 3, its expression level was insignificant (less than or equal to 5%) compared with that of triadin 1. We conclude that triadin 1 is the triadin isoform most likely to play a role in Ca2+ release in heart.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 07/07/20 alle ore 14:54:48