ROLE OF HYDROGEN PEROXIDE AND GLUTATHIONE IN GLUCOSE OXIDATION BY THYROID

被引：11

作者：

BENARD, B

DEGROOT, LJ

机构：

[1] Department of Medicine, Faculté de Médecine de Sherbrooke, Sherbrooke, Que.

[2] Thyroid Study Unit, University of Chicago School of Medicine, Chicago, IL

来源：

BIOCHIMICA ET BIOPHYSICA ACTA | 1969年 / 184卷 / 01期

基金：

英国医学研究理事会;

关键词：

D O I：

10.1016/0304-4165(69)90097-X

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Catalase depressed the 14CO2 yield from [I-14C]glucose in vitro in both TSH-stimulated and unstimulated thyroid slices. This observation was specific for the enzyme and seemed related to its action on H2O2, since H2O2 in the presence of GSH induced a significant stimulation of the hexose monophosphate shunt in thyroid homogenates. This effect of H2O2 and glutathione was specifically linked to the increased reoxidation of NADPH to NADP+, as measured by the spectrophotometric disappearance of the pyridine nucleotide at 340 mμ. These results offered proof for glutathione peroxidation in thyroid and suggested a role of glutathione in regulating thyroid hexose monophosphate shunt activity. It is postulated that the increased hexose monophosphate shunt activity induced by TSH could be at least partially related to H2O2 production in the course of colloid droplet or phagosome formation. © 1969.

引用

页码：48 / &

共 15 条

[1] GLUCOSE-6-PHOSPHATE DEHYDROGENASE AND DETOXIFICATION OF HYDROGEN PEROXIDE IN HUMAN ERYTHROCYTES [J].