Response of Rat Thyroid Oxidative Enzymes to TSH

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Abstract
Injected bovine TSH caused an increase in activity per mg protein of TPNH-cytochrome c reductase, isocitric dehydrogenase, glucose 6-phosphate dehydrogenase, and DPNH-DPIP reductase by 24 hr. and an increased total gland content of these enzymes at 72 hr. Gland weight, protein content, RNA, DPNH-cytochrome c reductase, and cytochrome c oxidase increased by 72 hr. but the changes were not significant at the p < . 05 level. Prior T4 administration diminished all these enzyme activities. The changes are thought to be caused by: proteolysis with a reduction to nonenzymatic protein; a possible shift of cell metabolism to biosynthetic activities; cell growth. The responses in respiratory enzyme activities do not occur as rapidly as do other TSH-mediated changes in cell metabolism and are most likely secondary to TSH-induced changes in energy utilization.

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