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PMID: 156362 Published · ppublish English Journal Article

Human platelet myosin light chain kinase requires the calcium-binding protein calmodulin for activity.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 76 ·No. 4 ·1979-04-00 ·Pages 1653-7

Hathaway DR, Adelstein RS

Abstract

In an actomyosin fraction isolated from human platelets, phosphorylation of the 20,000-dalton light chain of myosin is stimulated by calcium and the calcium-binding protein calmodulin. The enzyme catalyzing this phosphorylation has been isolated by using calmodulin-affinity chromatography. Platelet myosin light chain kinase activity was monitored throughout the isolation procedures by using the 20,000-dalton smooth muscle myosin light chain purified from turkey gizzards as substrate. The partially purified myosin kinase requires both calcium and calmodulin for activity and has a specific activity of 3.1 mumol of phosphate transferred to the 20,000-dalton light chain per mg of kinase per min under optimal assay conditions. Km values determined for ATP and myosin light chains are 121 microM and 18 microM, respectively. Of several substrates surveyed as phosphate acceptors (alpha-casein, histone II-A, phosphorylase b, protamine, histone V-S, and phosvitin), only the 20,000-dalton myosin light chain is phosphorylated at a significant rate. These results suggest that platelet myosin light chain kinase is a calcium-dependent enzyme and that the requirement for calcium is mediated by the calcium-binding protein calmodulin.

MeSH Terms
Actomyosin/blood Adenosine Triphosphatases/blood Blood Platelets/metabolism Calmodulin/pharmacology Carrier Proteins/pharmacology Egtazic Acid/pharmacology Humans Kinetics Macromolecular Substances Molecular Weight Myosins/blood,isolation & purification Phosphorylation
Chemicals
Calmodulin Carrier Proteins Macromolecular Substances Egtazic Acid Actomyosin Adenosine Triphosphatases Myosins
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Hathaway D R
Adelstein R S
References (34)
34 references, click to expand
  1. Phosphorylation of platelet myosin increases actin-activated myosin ATPase activity.
    Nature. 1975 Aug 14;256(5518):597-8 PMID: 170529
  2. Effect of phosphorylation of smooth muscle myosin on actin activation and Ca2+ regulation.
    Proc Natl Acad Sci U S A. 1977 Jan;74(1):129-33 PMID: 189302
  3. Troponin C like protein of blood platelets.
    FEBS Lett. 1977 Aug 15;80(2):308-12 PMID: 196934
  4. Phosphodiesterase protein activator mimics red blood cell cytoplasmic activator of (Ca2+-Mg2+)ATPase.
    Biochem Biophys Res Commun. 1977 Aug 22;77(4):1203-9 PMID: 197955
  5. Partial purification of the Ca2+-Mg2+ ATPase activator from human erythrocytes: its similarity to the activator of 3':5' - cyclic nucleotide phosphodiesterase.
    Biochem Biophys Res Commun. 1977 Aug 22;77(4):1210-6 PMID: 197956
  6. Purification of cyclic 3',5'-nucleotide phosphodiesterase inhibitory protein by affinity chromatography on activator protein coupled to Sepharose.
    Biochemistry. 1978 Jan 10;17(1):120-6 PMID: 201280
  7. Modulator protein as a component of the myosin light chain kinase from chicken gizzard.
    Biochemistry. 1978 Jan 24;17(2):253-8 PMID: 202300
  8. The modulator-dependent protein kinase. A multifunctional protein kinase activatable by the Ca2+-dependent modulator protein of the cyclic nucleotide system.
    J Biol Chem. 1978 May 25;253(10):3387-90 PMID: 206540
  9. Control of microtubule assembly-disassembly by calcium-dependent regulator protein.
    Proc Natl Acad Sci U S A. 1978 Aug;75(8):3771-5 PMID: 211505
  10. Identification of the Ca2+-dependent modulator protein as the fourth subunit of rabbit skeletal muscle phosphorylase kinase.
    FEBS Lett. 1978 Aug 15;92(2):287-93 PMID: 212300
  11. Calmodulin and myosin light-chain kinase of rabbit fast skeletal muscle.
    Biochem J. 1979 Apr 1;179(1):89-97 PMID: 224861
  12. 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):714-22 PMID: 332167
  13. Electrophoretic analysis of the major polypeptides of the human erythrocyte membrane.
    Biochemistry. 1971 Jun 22;10(13):2606-17 PMID: 4326772
  14. Molecular control mechanisms in muscle contraction.
    Physiol Rev. 1973 Jul;53(3):612-73 PMID: 4577547
  15. Cleavage of structural proteins during the assembly of the head of bacteriophage T4.
    Nature. 1970 Aug 15;227(5259):680-5 PMID: 5432063
  16. An electrophoretic study of the low-molecular-weight components of myosin.
    Biochem J. 1970 Aug;119(1):31-8 PMID: 5485752
  17. Calcium-binding subunit of myosin light chain kinase.
    J Biochem. 1977 Jul;82(1):287-9 PMID: 561063
  18. Thrombin-stimulated myosin phosphorylation in intact platelets and its possible involvement secretion.
    Thromb Haemost. 1977 Dec 15;38(4):984-9 PMID: 579699
  19. Stimulation of brain membrane protein phosphorylation by calcium and an endogenous heat-stable protein.
    Nature. 1978 Feb 2;271(5644):478-9 PMID: 628428
  20. A Ca2+-and modulator-dependent myosin light chain kinase from non-muscle cells.
    Biochem Biophys Res Commun. 1978 Dec 29;85(4):1352-9 PMID: 743302
  21. The effect of phosphorylation of gizzard myosin on actin activation.
    Biochem Biophys Res Commun. 1976 Jul 12;71(1):325-31 PMID: 962924
  22. Isolation and properties of platelet myosin light chain kinase.
    Biochemistry. 1976 Jun 1;15(11):2370-7 PMID: 132187
  23. Ca-linked phosphorylation of a light chain of vertebrate smooth-muscle myosin.
    Eur J Biochem. 1977 Mar 1;73(2):477-83 PMID: 139309
  24. Myoblast myosin phosphorylation is a prerequisite for actin-activation.
    Nature. 1977 Aug 11;268(5620):558-60 PMID: 142215
  25. Purification of an activator of human erythrocyte membrane (Ca2++Mg2+)ATPase.
    Biochem Biophys Res Commun. 1977 Jul 25;77(2):678-87 PMID: 143282
  26. Composition of the myosin light chain kinase from chicken gizzard.
    Biochem Biophys Res Commun. 1977 Oct 24;78(4):1263-72 PMID: 144501
  27. Conformational transition accompanying the binding of Ca2+ to the protein activator of 3',5'-cyclic adenosine monophosphate phosphodiesterase.
    Biochemistry. 1977 Mar 8;16(5):1017-24 PMID: 14663
  28. Biochemistry of actomyosin-dependent cell motility (a review).
    Proc Natl Acad Sci U S A. 1978 Feb;75(2):588-99 PMID: 147464
  29. Protein measurement with the Folin phenol reagent.
    J Biol Chem. 1951 Nov;193(1):265-75 PMID: 14907713
  30. Calcium-sensitive regulation of actin-myosin interactions in baby hamster kidney (BHK-21) cells.
    Proc Natl Acad Sci U S A. 1979 Jan;76(1):184-8 PMID: 154671
  31. Cyclic 3',5'-nucleotide phosphodiesterase Ca++-dependent formation of bovine brain enzyme-activator complex.
    FEBS Lett. 1975 Jan 1;49(3):356-60 PMID: 162885
  32. Identification of a calcium-binding protein as a calcium-dependent regulator of brain adenylate cyclase.
    Proc Natl Acad Sci U S A. 1975 Jan;72(1):64-8 PMID: 164029
  33. Cyclic 3',5'-nucleotide phosphodiesterase: pronounced stimulation by snake venom.
    Biochem Biophys Res Commun. 1967 Nov 30;29(4):478-82 PMID: 16496522
  34. Thrombin-induced protein phosphorylation in human platelets.
    J Clin Invest. 1975 Oct;56(4):924-36 PMID: 169298
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.76.4.1653
Published
1979-04-00
Pages
1653-7
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC383448
Subset
IM
External Links
PubMed source DOI: 10.1073/pnas.76.4.1653 PMC Full Text View journal details
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