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Microheterogeneity of type II cAMP-dependent protein kinase in various mammalian species and tissues.
Abstract: Excluding autophosphorylated species, at least six forms of the regulatory subunit of type II cAMP-dependent protein kinase (RII) from various mammalian tissues were identified by sodium dodecyl sulfate (SDS) gel electrophoresis of purified samples and of crude preparations photoaffinity labeled with 8-azido[32P] cAMP and by gel filtration. After autophosphorylation some heart RII forms termed type IIA (bovine, porcine, equine, and dog) shifted to a more slowly migrating band on SDS gels while others termed type IIB (rat, guinea pig, rabbit, and monkey) did not detectably shift. Both subclasses of RII exhibited variation in apparent Mr on SDS gels. Bovine and porcine heart nonautophosphorylated RII had Mr 56,000 and the autophosphorylated RII had Mr 58,000, while dog and equine heart RII had Mr 54,000 and 56,000 while rabbit and guinea pig heart RII had Mr 52,000. More than one RII was found in different tissues of the same species. Rabbit skeletal muscle contained a Mr 56,000 IIB form. Bovine lung contained almost equal amounts of a IIA form apparently identical to that of bovine heart and a Mr 52,000 IIB form similar to that which predominated in bovine brain. Rat adipose tissue, brain, and monkey heart contained predominantly a Mr 51,000 IIB form. The rat liver Mr 56,000 IIB form chromatographed differently from all other RII tested by gel filtration. Several lines of evidence indicated that the various forms of RII were not derived from one another through proteolysis or other processes. Each of the type II forms rapidly incorporated 0.3-1.0 mol of 32P per mol of subunit when incubated with [gamma-32P]ATP and C subunit. Four of the forms tested were similar in the cAMP concentration dependence for activation of their corresponding holoenzymes and inhibited C subunit about equally. Each exhibited two components of [3H]cAMP dissociation, indicating two intrachain cAMP-binding sites, and the dissociation rates for the respective sites were similar.
Publication Date: 1984-08-25 PubMed ID: 6088506 The Equine Research Bank provides access to a large database of publicly available scientific literature. Inclusion in the Research Bank does not imply endorsement of study methods or findings by Mad Barn.
- Comparative Study
- Journal Article
- Research Support
- Non-U.S. Gov't
- Research Support
- U.S. Gov't
- P.H.S.
Summary
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This research investigates the microheterogeneity of type II cAMP-dependent protein kinase, a protein regulating enzyme, in different mammalian species and tissues. The study identified at least six forms of the enzyme, presenting variations across species and having two cAMP-binding sites exhibiting similar dissociation rates.
Objective of the Research
- The research aimed to investigate the variability and specific forms of type II cAMP-dependent protein kinase (an enzyme responsible for protein regulation) in various mammalian species and tissues.
Identification of Variations
- Using sodium dodecyl sulfate gel electrophoresis and gel filtration, the researchers identified at least six forms excluding autophosphorylated ones, of type II cAMP-dependent protein kinase, also known as RII, from various mammalian tissues.
- The researchers found variations in the molecular weight (Mr) of non-autophosphorylated and autophosphorylated forms of RII. They discovered different forms within different tissues of the same species. For instance, rabbit skeletal muscle exhibited a 56,000 Mr IIB form, whereas bovine lung contained equal amounts of a IIA form similar to bovine heart and a 52,000 Mr IIB form similar to bovine brain.
Analysis of Variations and Protein Regulation
- The study concluded that due to the distinctive manner in the chromatic behavior of the type II forms of the enzyme, they likely do not derive from each other through proteolysis or other processes.
- The researchers also revealed that each type II form rapidly incorporated 0.3-1.0 mol of 32P per mol of subunit upon incubating with [gamma-32P]ATP and C subunit, supporting their individual functionality.
- All forms also demonstrated two components of cAMP dissociation, suggesting two intrachain cAMP-binding sites. The dissociation rates for each site were quite similar, implying uniform functionality across all type II forms in the regulation of cAMP.
- Furthermore, it was established that different forms were similar in the cAMP concentration required for activating their respective holoenzymes, showing similar inhibition of the C subunit.
Implication of the Study
- By identifying the unique forms and understanding their regulation mechanisms, the research broadens the understanding of cAMP-dependent protein kinases, their operation, differences in its types, and the role in various tissue types across different species. This knowledge could potentially aid future studies aimed at leveraging these enzymes’ functionality for various therapeutic applications.
Cite This Article
APA
Robinson-Steiner AM, Beebe SJ, Rannels SR, Corbin JD.
(1984).
Microheterogeneity of type II cAMP-dependent protein kinase in various mammalian species and tissues.
J Biol Chem, 259(16), 10596-10605.
Publication
Researcher Affiliations
MeSH Terms
- Adipose Tissue / enzymology
- Animals
- Brain / enzymology
- Cattle
- Cyclic AMP / pharmacology
- Cyclic GMP / pharmacology
- Dogs
- Erythrocebus patas
- GTP-Binding Proteins
- Horses
- Liver / enzymology
- Lung / enzymology
- Macromolecular Substances
- Molecular Weight
- Muscles / enzymology
- Myocardium / enzymology
- Organ Specificity
- Protein Kinases / analysis
- Rabbits
- Rats
- Receptors, Cell Surface / analysis
- Species Specificity
- Swine
Grant Funding
- AM 15988 / NIADDK NIH HHS
Citations
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- Pidoux G, Witczak O, Jarnæss E, Myrvold L, Urlaub H, Stokka AJ, Küntziger T, Taskén K. Optic atrophy 1 is an A-kinase anchoring protein on lipid droplets that mediates adrenergic control of lipolysis. EMBO J 2011 Oct 7;30(21):4371-86.
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- Pariset C, Feinberg J, Dacheux JL, Oyen O, Jahnsen T, Weinman S. Differential expression and subcellular localization for subunits of cAMP-dependent protein kinase during ram spermatogenesis. J Cell Biol 1989 Sep;109(3):1195-205.
- Lawrence JC Jr, Hiken JF, Inkster M, Scott CW, Mumby MC. Insulin stimulates the generation of an adipocyte phosphoprotein that is isolated with a monoclonal antibody against the regulatory subunit of bovine heart cAMP-dependent protein kinase. Proc Natl Acad Sci U S A 1986 Jun;83(11):3649-53.
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