Regulation of cardiac protein balance by hydrocortisone: interaction with insulin.

E. E. Griffin, K. Wildenthal

Research output: Contribution to journalArticle

Abstract

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)
JournalThe American journal of physiology
Volume234
Issue number3
StatePublished - Mar 1978

Fingerprint

Hydrocortisone
Insulin
Proteins
Proteolysis
Hexosaminidases
Fetal Heart
Branched Chain Amino Acids
Cathepsin D
Organ Culture Techniques
Creatine Kinase
Steroids
Hormones
Enzymes

ASJC Scopus subject areas

  • Medicine(all)

Cite this

Regulation of cardiac protein balance by hydrocortisone : interaction with insulin. / Griffin, E. E.; Wildenthal, K.

In: The American journal of physiology, Vol. 234, No. 3, 03.1978.

Research output: Contribution to journalArticle

@article{57a38ad4153c41c1862ff0897894424a,
title = "Regulation of cardiac protein balance by hydrocortisone: interaction with insulin.",
abstract = "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.",
author = "Griffin, {E. E.} and K. Wildenthal",
year = "1978",
month = "3",
language = "English (US)",
volume = "234",
journal = "American Journal of Physiology - Heart and Circulatory Physiology",
issn = "0363-6135",
publisher = "American Physiological Society",
number = "3",

}

TY - JOUR

T1 - Regulation of cardiac protein balance by hydrocortisone

T2 - interaction with insulin.

AU - Griffin, E. E.

AU - Wildenthal, K.

PY - 1978/3

Y1 - 1978/3

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=19244369695&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=19244369695&partnerID=8YFLogxK

M3 - Article

C2 - 629346

VL - 234

JO - American Journal of Physiology - Heart and Circulatory Physiology

JF - American Journal of Physiology - Heart and Circulatory Physiology

SN - 0363-6135

IS - 3

ER -