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Titolo:
Expression of endoplasmic reticulum stress proteins during skeletal muscledisuse atrophy
Autore:
Hunter, RB; Mitchell-Felton, H; Essig, DA; Kandarian, SC;
Indirizzi:
Boston Univ, Dept Hlth Sci, Boston, MA 02215 USA Boston Univ Boston MA USA 02215 Univ, Dept Hlth Sci, Boston, MA 02215 USA Geneva Coll, Dept Biol, Beaver Falls, PA 15010 USA Geneva Coll Beaver Falls PA USA 15010 pt Biol, Beaver Falls, PA 15010 USA
Titolo Testata:
AMERICAN JOURNAL OF PHYSIOLOGY-CELL PHYSIOLOGY
fascicolo: 4, volume: 281, anno: 2001,
pagine: C1285 - C1290
SICI:
0363-6143(200110)281:4<C1285:EOERSP>2.0.ZU;2-K
Fonte:
ISI
Lingua:
ENG
Soggetto:
HEME OXYGENASE-1 GENE; CALCIUM-PUMP; TRANSCRIPTIONAL ACTIVATION; SARCOPLASMIC-RETICULUM; OXIDATIVE STRESS; CELL-DEATH; CA2+; APOPTOSIS; IMMOBILIZATION; BCL-2;
Keywords:
unloading; sarcoplasmic reticulum; heme oxygenase; CHOP/GADD-153; vinculin; 78-kDa glucose-regulated protein; calreticulin; calsequestrin; calcium; inositol trisphosphate receptor; protein kinase R;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
30
Recensione:
Indirizzi per estratti:
Indirizzo: Kandarian, SC Boston Univ, Dept Hlth Sci, 635 Commonwealth Ave,Rm 443, Boston, MA 02215 USA Boston Univ 635 Commonwealth Ave,Rm 443 Boston MA USA 02215
Citazione:
R.B. Hunter et al., "Expression of endoplasmic reticulum stress proteins during skeletal muscledisuse atrophy", AM J P-CELL, 281(4), 2001, pp. C1285-C1290

Abstract

Disuse atrophy of skeletal muscle leads to an upregulation of genes encoding sarcoplasmic reticulum (SR) calcium-handling proteins. Because many of the proteins that are induced with endoplasmic reticulum (ER) stress are ER calcium-handling proteins, we sought to determine whether soleus muscle atrophy was associated with a prototypical ER stress response. Seven days of rat hindlimb unloading did not alter expression of ubiquitous ER stress proteins such as Grp78, calreticulin, and CHOP/GADD-153, nor other proteins that have been shown to be activated by ER stressors such as vinculin, the type I D-myo-inositol 1,4,5-trisphosphate receptor, or protein kinase R, a eukaryotic initiation factor 2 alpha kinase. On the other hand, expression of heme oxygenase-1 (HO-1), an antioxidant ER stress protein, was significantly increased 2.2-fold. In addition, unloading led to an increase in calsequestrin, the muscle-specific SR calcium-binding protein, at both the mRNA (68%) and protein (24%) levels. Although disuse atrophy is associated with a significant remodeling of muscle-specific proteins controlling SR calcium flux, it is not characterized by a prototypical ER stress response. However, the upregulation of HO-1 may indicate ER adaptation to oxidative stress during muscle unloading.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 06/04/20 alle ore 08:24:13