Regulation of cardiac protein balance by hydrocortisone: Interaction with insulin

E. E. Griffin, K. Wildenthal

Research output: Contribution to journalArticlepeer-review

20 Scopus citations


In fetal mouse hearts in organ culture the rate of protein synthesis was substantially reduced and the rate of protein degradation slightly increased by hydrocortisone in the absence of insulin, but in the presence of insulin the steroid caused a small increase in protein synthesis and a significant reduction in protein degradation. Hydrocortisone promoted the net uptake (or reduced the net release) of branched-chain amino acids independent of insulin and independent of simultaneous changes in protein balance. The specific activities of the lysosomal enzymes cathepsin D and glucosaminidase were reduced by hydrocortisone in all media, whereas the specific activity of creatine kinase increased when the medium contained insulin but decreased in the absence of insulin. It is concluded that hydrocortisone regulates cardiac protein balance via alterations both in synthesis and in degradation. Some of the hormone's myocardial effects are influenced by insulin so that hydrocortisone is anabolic in its presence but catabolic in its absence.

Original languageEnglish (US)
Pages (from-to)E306-E313
JournalAmerican Journal of Physiology Endocrinology Metabolism and Gastrointestinal Physiology
Issue number3
StatePublished - Jan 1 1978

ASJC Scopus subject areas

  • General Medicine


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