Detail of "5255-75-4"

Reference

Rapid, substrate-specific, and dose-dependent deactivation of liver cytosolic glutathione S-transferases in vivo by 1,1-dichloroethylene

Rapid, substrate-specific, and dose-dependent deactivation of liver cytosolic glutathione S-transferases in vivo by 1,1-dichloroethylene. Moslen, Mary Treinen; Reynolds, Edward S. (Dep. Pathol., Univ. Texas Med. Branch, Galveston, TX 77550, USA). Res. Commun. Chem. Pathol. Pharmacol., 47(1), 59-72 (English) 1985. CODEN: RCOCB8. ISSN: 0034-5164. DOCUMENT TYPE: Journal CA Section: 4 (Toxicology) The administration of 200 mg 1,1-dichloroethylene (DCE) [75-35-4]/kg to fasted rats rapidly decreased liver cytosolic glutathione S-transferase [50812-37-8] activities by 50% within 1 h. This early decrease was not assocd. with increased serum activities of this sol. enzyme and is considered due to the enzyme deactivation. The early decrease in enzyme activities was concomitant with a 75% depletion of cytosolic GSH [70-18-8] and preceded changes in cytochrome P 450 [9035-51-2] and the onset of liver cytotoxicity, both of which occurred abruptly between 2 and 3 h. Substantial changes in glutathione S-transferase activities at 4 h were produced only by severely hepatotoxic doses of DCE. The early decrease in hepatic glutathione S-transferase activities was selective for the substrates dichloronitrobenzene [27900-75-0], chlorodinitrobenzene [25567-67-3], and 1,2-epoxy-3-(p-nitrophenoxy)propane [5255-75-4] with apparent sparing of activity towards ethacrynic acid [58-54-8]. The rapid, selective, and dose-dependent deactivation of the hepatic glutathione S-transferase isoenzymes could be relevant to the catastrophic hepatotoxicity of DCE.

Reactivity of 12,13-epoxytrichothecenes with epoxide hydrolase, glutathione-S-transferase and glutathione

Reactivity of 12,13-epoxytrichothecenes with epoxide hydrolase, glutathione-S-transferase and glutathione. Nakamura, Yasuko; Ohta, Minoru; Ueno, Yoshio (Fac. Pharm. Sci., Tokyo Univ. Sci., Tokyo, Japan). Chem. Pharm. Bull., 25(12), 3410-14 (English) 1977. CODEN: CPBTAL. ISSN: 0009-2363. DOCUMENT TYPE: Journal CA Section: 4 (Toxicology) Interaction of the 12,13-epoxytrichothecenes and related mycotoxins with epoxide hydrolase [9048-63-9] and glutathione S-transferase (GSH-S-transferase) [50812-37-8] from rat liver was examd. in vitro. Neither hydrolysis of safrole oxide [7470-44-2] by the microsomal epoxide hydrolase nor conjugation of 2,3-epoxy-(p-nitrophenoxy)propane [5255-75-4] with glutathione [70-18-8] by the sol. GSH-S-transferase was interfered by the trichothecenes such as T-2 toxin [21259-20-1] and fusarenon-X [23255-69-8]. Gas-liq. chromatog. (GLC) anal. and colorimetric detn. of the residual GSH revealed that the trichothecenes were inert to the partilly purified GSH-S-transferase. In contrast to the trichothecenes, PR-toxin [56299-00-4], an epoxide mycotoxin from Penicillium roqueforti, and lactones such as patulin [149-29-1] and penicillic acid [90-65-3] from Penicillium and Aspergillus spp., were found to react nonenzymically with GSH in a molar ratio of 1:1.