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Titolo:
Identification and role of thiols in Toxoplasma gondii egress
Autore:
Stommel, EW; Cho, ES; Steide, JA; Seguin, R; Barchowsky, A; Schwartzman, JD; Kasper, LH;
Indirizzi:
Dartmouth Hitchcock Med Ctr, Dartmouth Med Sch, Dept Med, Neurol Sect, Lebanon, NH 03756 USA Dartmouth Hitchcock Med Ctr Lebanon NH USA 03756 t, Lebanon, NH 03756 USA Dartmouth Med Sch, Dept Microbiol, Lebanon, NH 03756 USA Dartmouth Med Sch Lebanon NH USA 03756 t Microbiol, Lebanon, NH 03756 USA Dartmouth Med Sch, Dept Pharmacol, Lebanon, NH 03756 USA Dartmouth Med Sch Lebanon NH USA 03756 t Pharmacol, Lebanon, NH 03756 USA Dartmouth Med Sch, Dept Pathol, Lebanon, NH 03756 USA Dartmouth Med Sch Lebanon NH USA 03756 Dept Pathol, Lebanon, NH 03756 USA McGill Univ, Montreal Neurol Inst, Neuroimmunol Unit, Montreal, PQ H3A 2B4, Canada McGill Univ Montreal PQ Canada H3A 2B4 Unit, Montreal, PQ H3A 2B4, Canada
Titolo Testata:
EXPERIMENTAL BIOLOGY AND MEDICINE
fascicolo: 3, volume: 226, anno: 2001,
pagine: 229 - 236
SICI:
1535-3702(200103)226:3<229:IAROTI>2.0.ZU;2-K
Fonte:
ISI
Lingua:
ENG
Soggetto:
NUCLEOSIDE TRIPHOSPHATE HYDROLASE; PARASITOPHOROUS VACUOLE; GLUTATHIONE; CELLS; FIBROBLASTS; ACTIVATION; SECRETION; PARASITES; INVASION; EXIT;
Keywords:
Toxoplasma gondii; Ca2+; nucleoside triphosphate hydrolase; n-acetyl-cysteine; glutathione; glutathione s-transferase; glutaredoxin; thioredoxin;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
24
Recensione:
Indirizzi per estratti:
Indirizzo: Stommel, EW Dartmouth Hitchcock Med Ctr, Dartmouth Med Sch, Dept Med, Neurol Sect, Lebanon, NH 03756 USA Dartmouth Hitchcock Med Ctr Lebanon NH USA 03756 NH 03756 USA
Citazione:
E.W. Stommel et al., "Identification and role of thiols in Toxoplasma gondii egress", EXP BIOL ME, 226(3), 2001, pp. 229-236

Abstract

The nucleoside triphosphate hydrolase of Toxoplasma gondii is a potent apyrase that is secreted into the parasitophorous vacuole where it appears to be essentially inactive in an oxidized form. Recent evidence shows that nucleoside triphosphate hydrolase can be activated by dithiothreitol in vivo. On reduction of the enzyme, there is a rapid depletion of host cell ATP. Previous results also demonstrate a dithiothreitol induced egress of parasites from the host cell with a concurrent Ca2+ flux, postulated to be a consequence of the release of ATP-dependent Ca2+ stores within the tubulovesicular network of the parasitophorous vacuole, Reduction of the nucleoside triphosphate hydrolase appears crucial for its activation; however, the exact mechanism of reduction/activation has not been determined. Using a variety oftechniques, we slow here that glutathione promoters activate a Ca2+ flux and decrease ATP levels in infected human fibroblasts, We further show the in vitro activation of nucleoside triphosphate hydrolase by endogenous reducing agents, one of which we postulate might be secreted into the PV by T. gondii. Our findings suggest that the reduction of the parasite nucleoside triphosphate hydrolase, and ultimately parasite egress, is under the controlof the parasites themselves.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/04/20 alle ore 08:40:58