Skip to main content
NCBI home page
Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1975 Jun;72(6):2256–2259. doi: 10.1073/pnas.72.6.2256

Changes in relative levels of guanosine-3':5'-monophosphate-dependent and adenosine-3':5'-monophosphate-dependent protein kinases in lung, heart, and brain of developing guinea pigs.

J F Kuo
PMCID: PMC432736  PMID: 166381

Abstract

Canges in relative levels of protein kinases (ATP:protein phosphotransferase, EC 2.7.1.37) stimulated by either guanosine 3':5'-monophosphate (cyclic-GMP) or adenosine 3':5'-monophosphate (cyclic-AMP) were examined in extracts of the lung, heart, brain, and liver from guinea pigs at various stages of development. The level of cyclic-GMP-dependent protein kinase in the fetal lung, which was found to be the highest of any mammalian tissue samples examined, declined during development. On the other hand, the level of cyclic-AMP-dependent protein kinase in the same extracts, which was initially lower than that of the cyclic-GMP-dependent enzyme, increased during development and reached a level higher than that of the cyclic-GMP-dependent enzyme when the animals reached maturity. This reciprocal change in level of the two classes of protein kinases in developing lung was demonstrated further by chromatographing the extracts on Sephadex G-200 and quantitating the activity of the isolated enzymes. A decrease in the ratio of the two classes of protein kinases qualitatively similar to that seen in the lung was also noted in the developing heart. An increase in the ratio of the enzymes, however, was seen in the developing brain. Unlike in the lung, heart, and brain, no change in relative level and ratio of the enzymes was noted in liver during development. These results suggest that a balance between the effects of cyclic-GMP-dependent and cyclic-AMP-dependent protein kinases may be important in normal development of certain tissues.

Full text

PDF
2256

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Appleman M. M., Birnbaumer L., Torres H. N. Factors affecting the activity of muscle glycogen synthetase. 3. The reaction with adenosine triphosphate Mg++, and cyclic 3'5'-adenosine monophosphate. Arch Biochem Biophys. 1966 Sep 26;116(1):39–43. doi: 10.1016/0003-9861(66)90009-9. [DOI] [PubMed] [Google Scholar]
  2. Davis C. Abortion counseling; what we need to know and why. J Pract Nurs. 1975 Jun;25(6):16-7, 34. [PubMed] [Google Scholar]
  3. Frank W. Cyclic 3':5' AMP and cell proliferation in cultures of embryonic rat cells. Exp Cell Res. 1972 Mar;71(1):238–241. doi: 10.1016/0014-4827(72)90287-x. [DOI] [PubMed] [Google Scholar]
  4. Goldberg N. D., O'Dea R. F., Haddox M. K. Cyclic GMP. Adv Cyclic Nucleotide Res. 1973;3:155–223. [PubMed] [Google Scholar]
  5. Hadden J. W., Hadden E. M., Haddox M. K., Goldberg N. D. Guanosine 3':5'-cyclic monophosphate: a possible intracellular mediator of mitogenic influences in lymphocytes. Proc Natl Acad Sci U S A. 1972 Oct;69(10):3024–3027. doi: 10.1073/pnas.69.10.3024. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Kuo J. F. Divergent actions of protein kinase modulator in regulating mammalian cyclic GMP-dependent and cyclic AMP-dependent protein kinases. Metabolism. 1975 Mar;24(3):321–329. doi: 10.1016/0026-0495(75)90113-4. [DOI] [PubMed] [Google Scholar]
  7. Kuo J. F., Greengard P. 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):1349–1355. doi: 10.1073/pnas.64.4.1349. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Kuo J. F., Greengard P. Cyclic nucleotide-dependent protein kinases. VI. Isolation and partial purification of a protein kinase activated by guanosine 3',5'-monophosphate. J Biol Chem. 1970 May 25;245(10):2493–2498. [PubMed] [Google Scholar]
  9. Kuo J. F. Guanosine 3':5'-monophosphate-dependent protein kinases in mammalian tissues. Proc Natl Acad Sci U S A. 1974 Oct;71(10):4037–4041. doi: 10.1073/pnas.71.10.4037. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Kuo J. F., Kuo W. N. Regulation by beta-adrenergic receptor and muscarinic cholinergic receptor activation of intracellular cyclic AMP and cyclic GMP levels in rat lung slices. Biochem Biophys Res Commun. 1973 Dec 10;55(3):660–665. doi: 10.1016/0006-291x(73)91195-9. [DOI] [PubMed] [Google Scholar]
  11. Kuo J. F., Wyatt G. R., Greengard P. Cyclic nucleotide-dependent protein kinases. IX. Partial purification and some properties of guanosine 3',5'-monophosphate-dependent and adenosine 3',5'-monophosphate-dependent protein kinases from various tissues and species of Arthropoda. J Biol Chem. 1971 Dec 10;246(23):7159–7167. [PubMed] [Google Scholar]
  12. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  13. Ryan W. L., Heidrick M. L. Role of cyclic nucleotides in cancer. Adv Cyclic Nucleotide Res. 1974;4(0):81–116. [PubMed] [Google Scholar]
  14. Stoner J. S., Manganiello V. C., Vaughan M. Guanosine cyclic 3',5'-monophosphate and guanylate cyclase activity in guinea pig lung: effects of acetylcholine and cholinesterase inhibitors. Mol Pharmacol. 1974 Jan;10(1):155–161. [PubMed] [Google Scholar]
  15. Voorhees J. J., Duell E. A., Stawiski M., Harrell E. R. Cyclic nucleotide metabolism in normal and proliferating epidermis. Adv Cyclic Nucleotide Res. 1974;4(0):117–162. [PubMed] [Google Scholar]
  16. Walsh D. A., Ashby C. D., Gonzalez C., Calkins D., Fischer E. H. Krebs EG: Purification and characterization of a protein inhibitor of adenosine 3',5'-monophosphate-dependent protein kinases. J Biol Chem. 1971 Apr 10;246(7):1977–1985. [PubMed] [Google Scholar]

Articles from Proceedings of the National Academy of Sciences of the United States of America are provided here courtesy of National Academy of Sciences

RESOURCES