Compartmentation of the type I regulatory subunit of cAMP-dependent protein kinase in cardiac ventricular muscle

Archives of Biochemistry and Biophysics
C A ReinitzJ B Shabb

Abstract

The species-dependent compartmentation of type I cAMP-dependent protein kinase (PKA I) and its dissociated regulatory subunit (RI) was examined in the heart by biochemical and immunohistochemical means. PKA I and RI were resolved from type II cAMP-dependent protein kinase and its regulatory subunit by DEAE-Sephacel chromatography of the supernatant and Triton X-100 soluble particulate fractions of heart homogenates. The relative amounts of holoenzymes and subunits were determined by cAMP-binding, protein kinase, 8-N3-[32P]cAMP photoaffinity labeling, and Western blot assays. Rat, rabbit, and guinea pig hearts all contained PKA I to varying degrees, but only in the supernatant fractions. Significant amounts of dissociated RI were found in the supernatant fractions, and to a lesser extent the particulate fractions, of these species. In contrast, though no PKA I was detected in the supernatant or particulate fractions of pig and beef heart, half of the cAMP-binding activity in the particulate fraction was attributed to RI. The results suggest that RI may associate with membrane fractions when it is not associated with the PKA catalytic subunit. Immunohistochemical studies of tissue sections from pig, beef, and rat cardiac ventricl...Continue Reading

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Citations

May 3, 2008·Cancer Research·Elise MeoliConstantine A Stratakis
Mar 21, 2003·Proceedings of the National Academy of Sciences of the United States of America·Stefan KammererAndreas Braun
Nov 6, 2004·Proceedings of the National Academy of Sciences of the United States of America·Junko KurokawaRobert S Kass
Feb 14, 2020·FASEB Journal : Official Publication of the Federation of American Societies for Experimental Biology·Víctor Cilleros-MañéMaria Angel Lanuza
Jun 29, 2002·Molecular and Cellular Endocrinology·M KovoN Dekel

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