Steroid Hormones May Regulate Autophosphorylation of Adenosine‐3′,5′‐Monophosphate‐Dependent Protein Kinase in Target Tissues

Alice Liu, Ulrich WALTER, Paul GREENGARD

Research output: Contribution to journalArticle

40 Citations (Scopus)

Abstract

A protein in rat liver cytosol whose phosphorylation was regulated by hydrocortisone administration in vivo was tentatively identified as the regulatory subunit of a cAMP‐dependent protein kinase. Evidence that this protein, whose phosphorylation was regulated by steroid and cyclic AMP, is the regulatory subunit of type‐II cAMP‐dependent protein kinase included: (a) co‐purification of the steroid cAMP‐regulated protein and the regulatory subunit during DEAE‐cellulose, Sepharose‐4B, and hydroxylapatite column chromatography, (b) co‐migration of the two proteins on dodecyl sulfate/ polyacrylamide slab gels during the various steps of purification, (c) specific adsorption of the two proteins onto 8(6‐aminohexylamino)‐cAMP‐Sepharose 4B, and (d) a similar pattern of distribution of the two proteins in various subcellular fractions prepared from rat liver homogenate. By each of these criteria, it was found that the steroid/cAMP‐regulated protein present in rat liver cytosol behaved identically with the regulatory subunit of type‐II cAMP‐dependent protein kinase in that tissue. Results qualitatively similar to those obtained in the study of the effect of hydrocortisone on rat liver were also obtained in studies of the effects of other steroid hormones on other target tissues in the rat, including uterus (17β‐estradiol), ventral prostate and seminal vesicle (testosterone), and epididymal fat pad (hydrocortisone). The tentative identification of the steroid/cAMP‐regulated protein as the regulatory subunit of the type‐II cAMP‐dependent protein kinase in the cytosol of several tissues indicates that autophosphorylation of the regulatory subunit of type‐II protein kinase may be regulated by the steroid hormones. The fact that three different classes of steroid hormones appear to affect the phosphorylation of the regulatory subunit of type‐II cAMP‐dependent protein kinase in their target tissues raises the possibility that this common biochemical action may play an important role in the mechanism of steroid hormone action. It is also possible that this effect of the steroid hormones may provide it molecular basis for some of the known physiological interactions of the steroid hormones with those hormones that act through using cAMP its a second messenger.

Original languageEnglish (US)
Pages (from-to)539-548
Number of pages10
JournalEuropean Journal of Biochemistry
Volume114
Issue number3
DOIs
StatePublished - Jan 1 1981

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Steroid hormones
Protein Kinases
Steroids
Hormones
Tissue
Rats
Liver
Phosphorylation
Proteins
Hydrocortisone
Cytosol
Column chromatography
Second Messenger Systems
Durapatite
Subcellular Fractions
Cyclic AMP
Seminal Vesicles
Purification
Protein Subunits
Testosterone

All Science Journal Classification (ASJC) codes

  • Biochemistry

Cite this

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title = "Steroid Hormones May Regulate Autophosphorylation of Adenosine‐3′,5′‐Monophosphate‐Dependent Protein Kinase in Target Tissues",
abstract = "A protein in rat liver cytosol whose phosphorylation was regulated by hydrocortisone administration in vivo was tentatively identified as the regulatory subunit of a cAMP‐dependent protein kinase. Evidence that this protein, whose phosphorylation was regulated by steroid and cyclic AMP, is the regulatory subunit of type‐II cAMP‐dependent protein kinase included: (a) co‐purification of the steroid cAMP‐regulated protein and the regulatory subunit during DEAE‐cellulose, Sepharose‐4B, and hydroxylapatite column chromatography, (b) co‐migration of the two proteins on dodecyl sulfate/ polyacrylamide slab gels during the various steps of purification, (c) specific adsorption of the two proteins onto 8(6‐aminohexylamino)‐cAMP‐Sepharose 4B, and (d) a similar pattern of distribution of the two proteins in various subcellular fractions prepared from rat liver homogenate. By each of these criteria, it was found that the steroid/cAMP‐regulated protein present in rat liver cytosol behaved identically with the regulatory subunit of type‐II cAMP‐dependent protein kinase in that tissue. Results qualitatively similar to those obtained in the study of the effect of hydrocortisone on rat liver were also obtained in studies of the effects of other steroid hormones on other target tissues in the rat, including uterus (17β‐estradiol), ventral prostate and seminal vesicle (testosterone), and epididymal fat pad (hydrocortisone). The tentative identification of the steroid/cAMP‐regulated protein as the regulatory subunit of the type‐II cAMP‐dependent protein kinase in the cytosol of several tissues indicates that autophosphorylation of the regulatory subunit of type‐II protein kinase may be regulated by the steroid hormones. The fact that three different classes of steroid hormones appear to affect the phosphorylation of the regulatory subunit of type‐II cAMP‐dependent protein kinase in their target tissues raises the possibility that this common biochemical action may play an important role in the mechanism of steroid hormone action. It is also possible that this effect of the steroid hormones may provide it molecular basis for some of the known physiological interactions of the steroid hormones with those hormones that act through using cAMP its a second messenger.",
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Steroid Hormones May Regulate Autophosphorylation of Adenosine‐3′,5′‐Monophosphate‐Dependent Protein Kinase in Target Tissues. / Liu, Alice; WALTER, Ulrich; GREENGARD, Paul.

In: European Journal of Biochemistry, Vol. 114, No. 3, 01.01.1981, p. 539-548.

Research output: Contribution to journalArticle

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