Skip to main content
NCBI home page
The Journal of Cell Biology logoLink to The Journal of Cell Biology
. 1980 Jul 1;86(1):280–285. doi: 10.1083/jcb.86.1.280

Low-temperature induction of calcium-dependent protein phosphorylation in blood platelets

PMCID: PMC2110668  PMID: 7419577

Abstract

Exposure to low temperature causes platelets to change shape in a manner similar to the shape change that precedes secretagogue-induced serotonin release. Previous studies have shown that two proteins, of approximately 20,000 and approximately 40,000 Mr, become phosphorylated before secretion. We have investigated whether low temperature can induce phosphorylation of these proteins and/or serotonin secretion. The data indicate that low-temperature-induced shape change has no requirement for extracellular calcium, whereas phosphorylation of the two proteins and subsequent serotonin release both have strong calcium requirements. Because cold treatment is thought to influence platelet shape through an effect on microtubules, the events in the shape change- release sequence would seem to be ordered as follows: microtubule disassembly leads to shape change leads to protein phosphorylation leads to secretion.

Full Text

The Full Text of this article is available as a PDF (620.6 KB).

Selected References

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

  1. Bennett W. F., Belville J. S., Lynch G. A study of protein phosphorylation in shape change and Ca++-dependent serotonin release by blood platelets. Cell. 1979 Dec;18(4):1015–1023. doi: 10.1016/0092-8674(79)90214-9. [DOI] [PubMed] [Google Scholar]
  2. Borisy G. G., Olmsted J. B., Marcum J. M., Allen C. Microtubule assembly in vitro. Fed Proc. 1974 Feb;33(2):167–174. [PubMed] [Google Scholar]
  3. Bouvier C. A., Gabbiani G., Ryan G. B., Badonnel M. C., Majno G., Lüscher E. F. Binding of anti-actin autoantibodies to platelets. Thromb Haemost. 1977 Apr 30;37(2):321–328. [PubMed] [Google Scholar]
  4. Daniel J. L., Holmsen H., Adelstein R. S. Thrombin-stimulated myosin phosphorylation in intact platelets and its possible involvement secretion. Thromb Haemost. 1977 Dec 15;38(4):984–989. [PubMed] [Google Scholar]
  5. Fox J. E., Say A. K., Haslam R. J. Subcellular distribution of the different platelet proteins phosphorylated on exposure of intact platelets to ionophore A23187 or to prostaglandin E1. Possible role of a membrane phosphopolypeptide in the regulation of calcium-ion transport. Biochem J. 1979 Dec 15;184(3):651–661. doi: 10.1042/bj1840651. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Gaskin F., Cantor C. R., Shelanski M. L. Biochemical studies on the in vitro assembly and disassembly of microtubules. Ann N Y Acad Sci. 1975 Jun 30;253:133–146. doi: 10.1111/j.1749-6632.1975.tb19197.x. [DOI] [PubMed] [Google Scholar]
  7. Greengard P. Phosphorylated proteins as physiological effectors. Science. 1978 Jan 13;199(4325):146–152. doi: 10.1126/science.22932. [DOI] [PubMed] [Google Scholar]
  8. Haslam R. J., Lynham J. A. Relationship between phosphorylation of blood platelet proteins and secretion of platelet granule constituents. I. Effects of different aggregating agents. Biochem Biophys Res Commun. 1977 Jul 25;77(2):714–722. doi: 10.1016/s0006-291x(77)80037-5. [DOI] [PubMed] [Google Scholar]
  9. Hathaway D. R., Adelstein R. S. Human platelet myosin light chain kinase requires the calcium-binding protein calmodulin for activity. Proc Natl Acad Sci U S A. 1979 Apr;76(4):1653–1657. doi: 10.1073/pnas.76.4.1653. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Henslee J. G., Srere P. A. Resolution of rat mitochondrial matrix proteins by two-dimensional polyacrylamide gel electrophoresis. J Biol Chem. 1979 Jun 25;254(12):5488–5497. [PubMed] [Google Scholar]
  11. Holmsen H. Biochemistry of the platelet release reaction. Ciba Found Symp. 1975;35:175–205. doi: 10.1002/9780470720172.ch9. [DOI] [PubMed] [Google Scholar]
  12. Kim Y. S., Padilla G. M. Determination of free Ca ion concentrations with an ion-selective electrode in the presence of chelating agents in comparison with calculated values. Anal Biochem. 1978 Sep;89(2):521–528. doi: 10.1016/0003-2697(78)90381-0. [DOI] [PubMed] [Google Scholar]
  13. Krebs E. G., Beavo J. A. Phosphorylation-dephosphorylation of enzymes. Annu Rev Biochem. 1979;48:923–959. doi: 10.1146/annurev.bi.48.070179.004423. [DOI] [PubMed] [Google Scholar]
  14. Lyons R. M., Atherton R. M. Characterization of a platelet protein phosphorylated during the thrombin-induced release reaction. Biochemistry. 1979 Feb 6;18(3):544–552. doi: 10.1021/bi00570a025. [DOI] [PubMed] [Google Scholar]
  15. Lyons R. M., Stanford N., Majerus P. W. Thrombin-induced protein phosphorylation in human platelets. J Clin Invest. 1975 Oct;56(4):924–936. doi: 10.1172/JCI108172. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Tilney L. G., Hiramoto Y., Marsland D. Studies on the microtubules in heliozoa. 3. A pressure analysis of the role of these structures in the formation and maintenance of the axopodia of Actinosphaerium nucleofilum (Barrett). J Cell Biol. 1966 Apr;29(1):77–95. doi: 10.1083/jcb.29.1.77. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. White J. G., Gerrard J. M. Interaction of microtubules and microfilaments in platelet contractile physiology. Methods Achiev Exp Pathol. 1979;9:1–39. [PubMed] [Google Scholar]
  18. White J. G., Krivit W. An ultrastructural basis for the shape changes induced in platelets by chilling. Blood. 1967 Nov;30(5):625–635. [PubMed] [Google Scholar]
  19. ZUCKER M. B., BORRELLI J. Reversible alterations in platelet morphology produced by anticoagulants and by cold. Blood. 1954 Jun;9(6):602–608. [PubMed] [Google Scholar]

Articles from The Journal of Cell Biology are provided here courtesy of The Rockefeller University Press

RESOURCES