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PMID: 2934055 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Caldesmon is a Ca2+-regulatory component of native smooth-muscle thin filaments.

The Biochemical journal ·Vol. 231 ·No. 3 ·1985-11-01 ·Pages 517-22

Marston SB, Lehman W

Abstract

Thin-filament preparations from four smooth muscle types (gizzard, stomach, trachea, aorta) all activate myosin MgATPase activity, are regulated by Ca2+, and contain actin, tropomyosin and a 120000-140000-Mr protein in the molar proportions 1:1/7:1/26. The 120000-140000-Mr protein from all sources is a potent inhibitor of actomyosin ATPase activity. Peptide-mapping and immunological evidence is presented showing that it is identical with caldesmon. Quantitative immunological data suggest that caldesmon is a component of all the thin filaments and that the thin-filament-bound caldesmon accounts for all the caldesmon in intact tissue. The myosin light-chain kinase content of thin-filament preparations was found to be negligible. We propose that caldesmon-based thin-filament Ca2+ regulation is a physiological mechanism in all smooth muscles.

MeSH Terms

Adenosine Triphosphatases/metabolism Animals Calcium/metabolism Calmodulin-Binding Proteins/immunology,metabolism Chemical Precipitation Chickens Electrophoresis, Polyacrylamide Gel Enzyme Activation/drug effects Enzyme-Linked Immunosorbent Assay In Vitro Techniques Muscle Proteins/metabolism Muscle, Smooth/metabolism Peptide Fragments/analysis

Chemicals

Calmodulin-Binding Proteins Muscle Proteins Peptide Fragments Adenosine Triphosphatases Calcium

Authors & Affiliations

2 authors, click to expand affiliations / ORCID

Marston S B

Lehman W

References (27)

27 references, click to expand

The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis.
J Biol Chem. 1969 Aug 25;244(16):4406-12 PMID: 5806584
Effects of Ca2+ and Mg2+ on the actomyosin adenosine-5'-triphosphatase of stably phosphorylated gizzard myosin.
Biochemistry. 1985 May 21;24(11):2731-6 PMID: 3161538
The contractile proteins of smooth muscle. Properties and components of a Ca2+-sensitive actomyosin from chicken gizzard.
Arch Biochem Biophys. 1975 Mar;167(1):203-12 PMID: 236728
Filamin, a new high-molecular-weight protein found in smooth muscle and non-muscle cells.
Proc Natl Acad Sci U S A. 1975 Nov;72(11):4483-6 PMID: 53835
Myosin-linked calcium regulation in vertebrate smooth muscle.
J Mol Biol. 1976 Mar 25;102(1):75-92 PMID: 131863
Peptide mapping by limited proteolysis in sodium dodecyl sulfate and analysis by gel electrophoresis.
J Biol Chem. 1977 Feb 10;252(3):1102-6 PMID: 320200
Regulation of the actin-myosin interaction in vertebrate smooth muscle: activation via a myosin light-chain kinase and the effect of tropomyosin.
J Mol Biol. 1977 Jun 5;112(4):559-76 PMID: 195061
Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications.
Proc Natl Acad Sci U S A. 1979 Sep;76(9):4350-4 PMID: 388439
The Croonian lecture, 1979: Regulation of muscle contraction.
Proc R Soc Lond B Biol Sci. 1980 Mar 21;207(1168):259-86 PMID: 6102396
Calcium ion-regulated thin filaments from vascular smooth muscle.
Biochem J. 1980 Feb 1;185(2):355-65 PMID: 6446898
The stoichiometry and location of troponin I- and troponin C-like proteins in the myofibril of the bay scallop, Aequipecten irradians.
Biochem J. 1980 May 1;187(2):447-56 PMID: 6249269
Enzyme immunoassay ELISA and EMIT.
Methods Enzymol. 1980;70(A):419-39 PMID: 6999296
Regulation of smooth muscle actomyosin.
Annu Rev Physiol. 1981;43:519-30 PMID: 6260022
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
Regulation of actin-activated ATP hydrolysis by arterial myosin.
Proc Natl Acad Sci U S A. 1982 Jan;79(2):292-6 PMID: 6210906
The regulation of smooth muscle contractile proteins.
Prog Biophys Mol Biol. 1983;41(1):1-41 PMID: 6130572
Caldesmon, a calmodulin-binding, F actin-interacting protein, is present in aorta, uterus and platelets.
FEBS Lett. 1983 Apr 18;154(2):351-6 PMID: 6403386
Quantitative, single-tube, kinetic-dependent enzyme-linked immunosorbent assay (k-ELISA).
Methods Enzymol. 1983;92:391-403 PMID: 6343771
Identification of a troponin-I like protein in platelet preparations as histone H2B.
FEBS Lett. 1983 Jun 27;157(1):129-32 PMID: 6862010
Isolation of the native form of chicken gizzard myosin light-chain kinase.
Biochem J. 1984 Mar 15;218(3):863-70 PMID: 6326748
Occurrence of caldesmon (a calmodulin-binding protein) in cultured cells: comparison of normal and transformed cells.
Proc Natl Acad Sci U S A. 1984 May;81(10):3133-7 PMID: 6328499
The binding of smooth muscle myosin light chain kinase and phosphatases to actin and myosin.
J Biol Chem. 1984 Jun 25;259(12):7740-6 PMID: 6330077
Smooth muscle caldesmon. Rapid purification and F-actin cross-linking properties.
J Biol Chem. 1984 Oct 25;259(20):12873-80 PMID: 6092349
Detection of caldesmon in muscle and non-muscle tissues of the chicken using polyclonal antibodies.
Biochem Biophys Res Commun. 1985 Mar 15;127(2):533-9 PMID: 2983725
Mechanisms of the regulation of myofibrillar function in vascular smooth muscle.
Biochem Soc Trans. 1984 Dec;12(6):945-8 PMID: 6530043
Disassembly and reconstitution of the Ca2+-sensitive thin filaments of vascular smooth muscle.
FEBS Lett. 1985 May 6;184(1):115-9 PMID: 3987897
Cleavage of structural proteins during the assembly of the head of bacteriophage T4.
Nature. 1970 Aug 15;227(5259):680-5 PMID: 5432063

Article Info

Journal

The Biochemical journal

Abbr.

Biochem J

ISSN

0264-6021

DOI

10.1042/bj2310517

Published

1985-11-01

Pages

517-22

Language

English

Region

England

NLM ID

2984726R

PMCID

PMC1152781

Subset

External Links

PubMed source DOI: 10.1042/bj2310517 PMC Full Text View journal details

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Caldesmon is a Ca2+-regulatory component of native smooth-muscle thin filaments.

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