Heat shock protein-70 induction mediates luteal regression in the rat

Molecular Endocrinology
A KhannaH R Behrman

Abstract

Induction of heat shock protein 70 (HSP-70) is associated with inhibition of hormone-sensitive steroidogenesis and interruption of cholesterol translocation to or into the mitochondria. A number of pharmacological and physiological inhibitors of luteal cell function stimulate HSP-70 synthesis via activation of the heat shock transcription factor (HSF). In the present study we address the following questions: 1) is HSP-70 synthesis increased during prostaglandin F2 alpha (PGF2 alpha)-induced luteolysis or natural luteal regression? 2) Does blocking HSP-70 synthesis reverse the inhibition of hormone-sensitive steroidogenesis induced by heat stress and PGF2 alpha? Gel-retardation assays demonstrated HSF activation within 7.5 min after PGF2 alpha (400 micrograms) administered in vivo. Western blotting revealed HSP-70 synthesis by 1 h with higher levels seen at 2 h. The stress response was similarly activated during natural regression of the corpus luteum in rats. Gel retardation assays demonstrated maximal HSF activation 10 days after ovulation. Western blotting showed that HSP-70 levels increased dramatically on this same day and were sustained for several days after the initiation of luteal regression. Inhibition of HSP-70 synthe...Continue Reading

Citations

Jul 23, 2013·The Journal of Clinical Investigation·Alison S CareSarah A Robertson
Nov 11, 2008·Reproduction in Domestic Animals = Zuchthygiene·N R SalvettiH H Ortega
Dec 20, 2011·The Journal of Obstetrics and Gynaecology Research·Eunkuk ParkJong-Phil Chu
Nov 2, 2006·Endocrine Reviews·Carlos StoccoGeula Gibori

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