Home LiteratureArticle Details
PMID: 4323789 Published · ppublish English Journal Article

Role of the receptor in the mechanism of action of adenosine 3':5'-cyclic monophosphate.

Gill GN, Garren LD

Abstract

Highly purified cAMP-dependent protein phosphokinase from adrenal-cortical tissue contains cAMP-receptor activity. In activating the kinase, cAMP binds to the receptor and causes it to dissociate from its complex with the kinase. The kinase, freed of receptor, is fully activated and no longer stimulable by cAMP. Kinase can be similarly activated by differentially denaturing the receptor with heat. Addition of receptor suppresses kinase activity; this suppression can be overcome by cAMP. After dissociation of receptor, two molecular forms of the activated kinase exist. The cAMP receptor thus functions as a repressor of the protein kinase; binding of cAMP to receptor causes it to dissociate from the kinase, which is then fully activated.

MeSH Terms
Adenine Nucleotides Adrenal Glands/analysis Animals Cattle Chemical Phenomena Chemistry Chromatography, DEAE-Cellulose Cyclic AMP/pharmacology Electrophoresis Hot Temperature In Vitro Techniques Phosphorus Isotopes Phosphotransferases/isolation & purification,pharmacology Protein Binding Proteins/isolation & purification,pharmacology Tritium Ultracentrifugation
Chemicals
Adenine Nucleotides Phosphorus Isotopes Proteins Tritium Cyclic AMP Phosphotransferases
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Gill G N
Garren L D
References (22)
22 references, click to expand
  1. A simple method for the preparation of 32-P-labelled adenosine triphosphate of high specific activity.
    Biochem J. 1964 Jan;90(1):147-9 PMID: 5832284
  2. Distinct subunits for the regulation and catalytic activity of aspartate transcarbamylase.
    Biochemistry. 1965 Jun;4(6):1054-62 PMID: 5320387
  3. An adenosine 3',5'-monophosphate-dependant protein kinase from rabbit skeletal muscle.
    J Biol Chem. 1968 Jul 10;243(13):3763-5 PMID: 4298072
  4. Size and charge isomer separation and estimation of molecular weights of proteins by disc gel electrophoresis.
    Arch Biochem Biophys. 1968 Jul;126(1):155-64 PMID: 5671059
  5. Histone phosphorylation: stimulation by adenosine 3',5'-monophosphate.
    Science. 1968 Nov 1;162(3853):579-80 PMID: 4303296
  6. On the mechanism of action of adrenocorticotropic hormone: the binding of cyclic-3',5'-adenosine monophosphate to an adrenal cortical protein.
    Proc Natl Acad Sci U S A. 1969 Jun;63(2):512-9 PMID: 4308274
  7. Protamine kinase from rainbow trout testis. Partial purification and characterization.
    J Biol Chem. 1970 Jan 25;245(2):425-34 PMID: 4312674
  8. Interconversion of phospho- and dephospho- forms of pig heart pyruvate dehydrogenase.
    Proc Natl Acad Sci U S A. 1970 Apr;65(4):947-54 PMID: 4314903
  9. A cyclic-3',5'-adenosine monophosphate dependent protein kinase from the adrenal cortex: comparison with a cyclic AMP binding protein.
    Biochem Biophys Res Commun. 1970 May 11;39(3):335-43 PMID: 4316205
  10. Cyclic AMP receptor protein of E. coli: its role in the synthesis of inducible enzymes.
    Proc Natl Acad Sci U S A. 1970 Jun;66(2):480-7 PMID: 4317918
  11. Cyclic nucleotide-dependent protein kinases. IV. Widespread occurrence of adenosine 3',5'-monophosphate-dependent protein kinase in various tissues and phyla of the animal kingdom.
    Proc Natl Acad Sci U S A. 1969 Dec;64(4):1349-55 PMID: 4393915
  12. ATP-dependent and cyclic AMP-dependent activation of rat adipose tissue lipase by protein kinase from rabbit skeletal muscle.
    Proc Natl Acad Sci U S A. 1970 Sep;67(1):290-5 PMID: 4318780
  13. Mechanism of activation by adenosine 3':5'-cyclic monophosphate of a protein phosphokinase from rabbit reticulocytes.
    Proc Natl Acad Sci U S A. 1970 Sep;67(1):408-14 PMID: 4318788
  14. An assay for adenosine 3',5'-cyclic monophosphate based on the association of the nucleotide with a partially purified binding protein.
    Biochemistry. 1970 Oct 13;9(21):4223-9 PMID: 4318805
  15. Mechanism of activation of catabolite-sensitive genes: a positive control system.
    Proc Natl Acad Sci U S A. 1970 May;66(1):104-10 PMID: 4320461
  16. Mode of action of adenosine 3',5'-cyclic phosphate on protein kinase from rat liver.
    Biochem Biophys Res Commun. 1970 Dec 9;41(5):1290-7 PMID: 4320718
  17. Inactivation of glycogen synthetase and activation of phosphorylase kinase by muscle adenosine 3',5'-monophosphate-dependent protein kinases.
    J Biol Chem. 1970 Dec 10;245(23):6317-28 PMID: 4320836
  18. Separation of regulatory and catalytic subunits of the cyclic 3',5'-adenosine monophosphate-dependent protein kinase(s) of rabbit skeletal muscle.
    Biochem Biophys Res Commun. 1971 Jan 22;42(2):187-94 PMID: 4322813
  19. Protein measurement with the Folin phenol reagent.
    J Biol Chem. 1951 Nov;193(1):265-75 PMID: 14907713
  20. Significance of heat-activated enzymes.
    Science. 1956 Jan 13;123(3185):50-3 PMID: 13281479
  21. A method for determining the sedimentation behavior of enzymes: application to protein mixtures.
    J Biol Chem. 1961 May;236:1372-9 PMID: 13767412
  22. STARCH-GEL ELECTROPHORESIS--APPLICATION TO THE CLASSIFICATION OF PITUITARY PROTEINS AND POLYPEPTIDES.
    Metabolism. 1964 Oct;13:SUPPL:985-1002 PMID: 14228777
Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
Published
1971-04-00
Pages
786-90
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC389043
Subset
IM
Analysis Services
Analysis Services

Contact

No. 2 Wenbo Road, Zhangqiu District, Jinan, Shandong

Qilu Normal University · Genelibs Bioinformatics Lab

750 Shunhua Rd, Jinan

2F, Bldg F, University Science Park

Tel: 0531-88819269

WeChat Official Account

Follow our WeChat subscription account for real-time updates and the latest in medical and biological research.


Business Email

E-mail: [email protected]