Home LiteratureArticle Details
PMID: 3856849 Published · ppublish English Comparative Study Journal Article Research Support, U.S. Gov't, P.H.S.

Calmodulin accelerates the rate of polymerization of human platelet actin and alters the structural characteristics of actin filaments.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 82 ·No. 6 ·1985-03-00 ·Pages 1683-7

Piazza GA, Wallace RW

Abstract

Calmodulin stimulated the rate of Mg2+-induced polymerization of human platelet actin. The stimulatory effect was due to an increase in the nucleation phase of the reaction; there was no effect on the steady-state viscosity. The calmodulin antagonist trifluoperazine blocked the stimulatory effect of calmodulin. Addition of EGTA to the reaction mixture also stimulated the rate of actin polymerization; however, the effect of calmodulin on actin polymerization is not due to Ca2+ chelation, as is presumed to be the case for EGTA. Electron microscopy revealed structural differences in the filaments prepared in the presence of calmodulin as compared to those prepared with trifluoperazine. In the presence of calmodulin, the filaments were thicker, suggesting that they consisted of multiple actin polymers. In addition, numerous projections were present perpendicular to the filaments, as well as localized areas of filament bundling. It was not possible to demonstrate a direct interaction between calmodulin and actin, which raises the possibility that the calmodulin effect may be indirect through a calmodulin-binding protein or calmodulin-dependent enzyme. Regardless of whether calmodulin is acting directly or indirectly, these results provide evidence that calmodulin may play a regulatory role in either the polymerization of actin or in determining the structural characteristics of actin filaments.

MeSH Terms
Actins/blood Blood Platelets/drug effects,metabolism Calcium/blood Calmodulin/pharmacology Humans In Vitro Techniques Polymers/metabolism Protein Conformation/drug effects
Chemicals
Actins Calmodulin Polymers Calcium
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Piazza G A
Wallace R W
References (40)
40 references, click to expand
  1. Cleavage of structural proteins during the assembly of the head of bacteriophage T4.
    Nature. 1970 Aug 15;227(5259):680-5 PMID: 5432063
  2. Mechanism of activation of a cyclic adenosine 3':5'-monophosphate phosphodiesterase from bovine heart by calcium ions. Identification of the protein activator as a Ca2+ binding protein.
    J Biol Chem. 1973 Sep 10;248(17):5950-5 PMID: 4353626
  3. Cyclic 3',5'-nucleotide phosphodiesterase. Distribution and developmental changes of the enzyme and its protein activator in mammalian tissues and cells.
    Biochim Biophys Acta. 1974 Apr 25;341(2):402-11 PMID: 4365089
  4. Cyclic 3':5'-nucleotide phosphodiesterase. Purification, characterization, and active form of the protein activator from bovine brain.
    J Biol Chem. 1974 Aug 10;249(15):4943-54 PMID: 4367813
  5. Protein activator of cyclic 3':5'-nucleotide phosphodiesterase of bovine or rat brain also activates its adenylate cyclase.
    Biochem Biophys Res Commun. 1975 Oct 6;66(3):1055-62 PMID: 170936
  6. Cyclic 3':5'-nucleotide phosphodiesterase. Ca2+ confers more helical conformation to the protein activator.
    J Biol Chem. 1976 Jul 25;251(14):4193-8 PMID: 180019
  7. Structural similarities between the Ca2+-dependent regulatory proteins of 3':5'-cyclic nucleotide phosphodiesterase and actomyosin ATPase.
    J Biol Chem. 1976 Aug 10;251(15):4501-13 PMID: 181375
  8. Direct evidence for intracellular divalent cation redistribution associated with platelet shape change.
    Biochem Biophys Res Commun. 1976 Jul 12;71(1):362-70 PMID: 786285
  9. Comparative biochemistry of non-muscle actins.
    J Biol Chem. 1977 Nov 25;252(22):8300-9 PMID: 144137
  10. Ca2+-dependent regulator. Production and characterization of a monospecific antibody.
    J Biol Chem. 1978 Oct 25;253(20):7515-21 PMID: 212426
  11. Platelet alpha-granule proteins: studies on release and subcellular localization.
    Blood. 1979 Apr;53(4):604-18 PMID: 426909
  12. Human erythrocyte Ca2+-Mg2+-ATPase: mechanism of stimulation by Ca2+.
    Arch Biochem Biophys. 1979 Apr 15;194(1):165-70 PMID: 156003
  13. 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):1653-7 PMID: 156362
  14. Rabbit skeletal muscle F-actin can be stable at low ionic strength, provided trace amounts of Ca2+ are absent.
    Biochim Biophys Acta. 1979 Apr 25;577(2):267-72 PMID: 110352
  15. Reorganization of actin in platelets stimulated by thrombin as measured by the DNase I inhibition assay.
    Proc Natl Acad Sci U S A. 1979 Dec;76(12):6376-80 PMID: 118466
  16. Platelet phosphorylase kinase activity and its regulation by the calcium-dependent regulatory protein, calmodulin.
    Biochim Biophys Acta. 1980 Mar 14;612(1):50-5 PMID: 7362832
  17. Brush-border calmodulin. A major component of the isolated microvillus core.
    J Cell Biol. 1980 Jun;85(3):916-23 PMID: 6893051
  18. Calmodulin-binding proteins of the microfilaments present in isolated brush borders and microvilli of intestinal epithelial cells.
    J Biol Chem. 1980 Nov 25;255(22):10551-4 PMID: 7430135
  19. Effects of trace amounts of Ca2+ and Mg2+ on the polymerization of actin.
    Biochim Biophys Acta. 1981 Jan 30;667(1):139-42 PMID: 6783113
  20. Changes in the cytoskeletal structure of human platelets following thrombin activation.
    J Biol Chem. 1981 Jul 10;256(13):6927-32 PMID: 6894599
  21. Platelet calcium-dependent proteins: identification and localization of the calcium-dependent regulator, calmodulin, in platelets.
    Am J Hematol. 1981 Jun;10(4):359-67 PMID: 7018228
  22. Proteins associated with cytoplasmic actin.
    Cell. 1981 Sep;25(3):587-90 PMID: 7285114
  23. Purification of a calmodulin-binding protein from chicken gizzard that interacts with F-actin.
    Proc Natl Acad Sci U S A. 1981 Sep;78(9):5652-5 PMID: 6946503
  24. Platelet and leucocyte calmodulins: isolation and characterisation.
    Eur J Biochem. 1981 Nov;120(2):303-8 PMID: 6274636
  25. Silver stain for proteins in polyacrylamide gels: a modified procedure with enhanced uniform sensitivity.
    Anal Biochem. 1981 Nov 1;117(2):307-10 PMID: 6172996
  26. Calmodulin and the cell cycle: involvement in regulation of cell-cycle progression.
    Cell. 1982 Jan;28(1):41-50 PMID: 7066986
  27. Actin-binding proteins--regulators of cell architecture and motility.
    Nature. 1982 Apr 29;296(5860):811-6 PMID: 7200195
  28. Actin polymerization and its regulation by proteins from nonmuscle cells.
    Physiol Rev. 1982 Apr;62(2):672-737 PMID: 6280220
  29. Two opposing effects of calmodulin on microtubule assembly depend on the presence of microtubule-associated proteins.
    J Biol Chem. 1982 Jun 10;257(11):6306-10 PMID: 6804463
  30. An F-actin- and calmodulin-binding protein from isolated intestinal brush borders has a morphology related to spectrin.
    Cell. 1982 Apr;28(4):843-54 PMID: 7201352
  31. Erythroid spectrin, brain fodrin, and intestinal brush border proteins (TW-260/240) are related molecules containing a common calmodulin-binding subunit bound to a variant cell type-specific subunit.
    Proc Natl Acad Sci U S A. 1982 Jul;79(13):4002-5 PMID: 6955786
  32. Actin polymerization induced by calspectin, a calmodulin-binding spectrin-like protein.
    FEBS Lett. 1982 Nov 8;148(2):221-5 PMID: 7152018
  33. The role of calmodulin in hemostasis.
    Prog Hemost Thromb. 1982;6:25-61 PMID: 6300965
  34. Regulation of calcium accumulation and efflux from platelet vesicles. Possible role for cyclic-AMP-dependent phosphorylation and calmodulin.
    Biochim Biophys Acta. 1983 Jun 23;731(3):456-64 PMID: 6134552
  35. Assay of calmodulin by Ca2+-dependent phosphodiesterase.
    Methods Enzymol. 1983;102:39-47 PMID: 6316081
  36. Calmodulin-binding proteins that interact with actin filaments in a Ca2+-dependent flip-flop manner: survey in brain and secretory tissues.
    Proc Natl Acad Sci U S A. 1983 Nov;80(22):6868-71 PMID: 6316332
  37. Actin filament content and organization in unstimulated platelets.
    J Cell Biol. 1984 Jun;98(6):1985-91 PMID: 6233292
  38. Presence of calmodulin in human platelet cytoskeletons and its concentration change upon activation of platelets.
    Biochim Biophys Acta. 1984 Sep 28;801(2):290-7 PMID: 6148109
  39. Specific cleavage of calmodulin-binding proteins by low Ca2+-requiring form of Ca2+-activated neutral protease in human platelets.
    Biochem Int. 1983 Jun;6(6):767-75 PMID: 6091657
  40. ELECTRON MICROSCOPE STUDIES ON THE STRUCTURE OF NATURAL AND SYNTHETIC PROTEIN FILAMENTS FROM STRIATED MUSCLE.
    J Mol Biol. 1963 Sep;7:281-308 PMID: 14064165
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
DOI
10.1073/pnas.82.6.1683
Published
1985-03-00
Pages
1683-7
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC397336
Subset
IM
Grants
NCI NIH HHS · CA 13148 · United States
NHLBI NIH HHS · HL29766 · United States
External Links
PubMed source DOI: 10.1073/pnas.82.6.1683 PMC Full Text View journal details
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]

Copyright © 2026.Genelibs Jinan Honghui Biotechnology Co., Ltd. 鲁ICP备20007159号-2