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PMID: 3321066 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Expression of high and low molecular weight caldesmons during phenotypic modulation of smooth muscle cells.

Ueki N, Sobue K, Kanda K, Hada T, Higashino K

Abstract

We investigated the expression of two molecular weight forms of caldesmon in a wide range of tissues and cells. The distribution of high molecular weight caldesmon (h-caldesmon, Mr 120,000-150,000) was restricted to smooth muscles where it was found in large quantity. The low molecular weight protein (l-caldesmon, Mr 70,000-80,000) was widely distributed in nonmuscle tissues and cells. Therefore, the expression of h-caldesmon might be much more specific to smooth muscles. We then examined the expressional changes of two caldesmons during phenotypic modulation of smooth muscle cells (SMCs). In developing gizzards, the expression of caldesmons switched from the l- to the h-form. Contrarily, the expression turned from h- to l-caldesmon in association with dedifferentiation of aortic SMCs in primary culture. In agreement with these observations, the levels of those mRNAs that direct the synthesis of both caldesmons were apparently in proportion to the quantities of protein, as determined by use of an in vitro translation system. In addition, h-caldesmon in smooth muscle-like BC3H1 cells increased in its amount with a concomitant reduction of l-caldesmon following serum-depleted and contact-inhibited cytodifferentiation. These results suggest that the expressional changes of two caldesmons are closely correlated with the phenotypic modulation of SMCs.

MeSH Terms
Animals Calmodulin-Binding Proteins/metabolism Cattle Cell Differentiation Cell Line Cytoskeletal Proteins/metabolism Gene Expression Regulation Gizzard, Non-avian/physiology Immunologic Techniques Mice Muscle, Smooth/cytology,physiology Muscle, Smooth, Vascular/physiology RNA, Messenger/metabolism Rats
Chemicals
Calmodulin-Binding Proteins Cytoskeletal Proteins RNA, Messenger
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Ueki N
Department of Neurochemistry and Neuropharmacology, Osaka University Medical School, Japan.
Sobue K
Kanda K
Hada T
Higashino K
References (37)
37 references, click to expand
  1. Studies on the avian gizzard: the development of the gizzard and its innervation.
    Z Zellforsch Mikrosk Anat. 1969;98(4):599-621 PMID: 5807130
  2. Caldesmon regulates the three-dimensional contraction (myosin-dependent contraction of the actin binding protein-induced actin gel).
    Biochem Biophys Res Commun. 1987 Apr 29;144(2):936-43 PMID: 3579949
  3. Characterization of a unique muscle cell line.
    J Cell Biol. 1974 May;61(2):398-413 PMID: 4363958
  4. Regulation of adenylate kinase and creatine kinase activities in myogenic cells.
    Proc Natl Acad Sci U S A. 1974 Jun;71(6):2377-81 PMID: 4366764
  5. An efficient mRNA-dependent translation system from reticulocyte lysates.
    Eur J Biochem. 1976 AUG 1;67(1):247-56 PMID: 823012
  6. Comparison of vascular smooth muscle cells from adult human, monkey and rabbit in primary culture and in subculture.
    Cell Tissue Res. 1977 Feb 14;177(4):503-22 PMID: 402216
  7. The appearance of acetylcholine receptors triggered by fusion of myoblasts in vitro.
    FEBS Lett. 1978 Apr 15;88(2):327-31 PMID: 565722
  8. The smooth muscle cell in culture.
    Physiol Rev. 1979 Jan;59(1):1-61 PMID: 108688
  9. Differential expression of gizzard actin genes during chick embryogenesis.
    J Biol Chem. 1979 Nov 10;254(21):11119-25 PMID: 500629
  10. 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
  11. Isolation of biologically active ribonucleic acid from sources enriched in ribonuclease.
    Biochemistry. 1979 Nov 27;18(24):5294-9 PMID: 518835
  12. Phenotype-dependent response of cultured aortic smooth muscle to serum mitogens.
    J Cell Biol. 1981 May;89(2):379-83 PMID: 7251658
  13. 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
  14. Multiple controls for the synthesis of muscle-specific proteins in BC3H1 cells.
    J Cell Biol. 1982 Feb;92(2):350-6 PMID: 7061588
  15. Reconstitution of Ca2+-sensitive gelation of actin filaments with filamin, caldesmon and calmodulin.
    FEBS Lett. 1982 Feb 22;138(2):289-92 PMID: 7067839
  16. Developmental change of protein constituents in chicken gizzards.
    Dev Biol. 1983 Jun;97(2):483-93 PMID: 6343162
  17. Regulation of surface expression of acetylcholine receptors in response to serum and cell growth in the BC3H1 muscle cell line.
    J Biol Chem. 1983 Nov 25;258(22):13946-53 PMID: 6643459
  18. Induction of vascular smooth muscle alpha-isoactin expression in BC3H1 cells.
    J Biol Chem. 1984 Mar 10;259(5):3152-9 PMID: 6699010
  19. Isolation of the native form of chicken gizzard myosin light-chain kinase.
    Biochem J. 1984 Mar 15;218(3):863-70 PMID: 6326748
  20. 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
  21. Smooth muscle caldesmon. Rapid purification and F-actin cross-linking properties.
    J Biol Chem. 1984 Oct 25;259(20):12873-80 PMID: 6092349
  22. Inhibition of smooth muscle actin-activated myosin Mg2+-ATPase activity by caldesmon.
    J Biol Chem. 1984 Nov 25;259(22):13656-9 PMID: 6150036
  23. Identification and localization of immunoreactive forms of caldesmon in smooth and nonmuscle cells: a comparison with the distributions of tropomyosin and alpha-actinin.
    J Cell Biol. 1985 May;100(5):1656-63 PMID: 2985624
  24. Purification and characterization of caldesmon77: a calmodulin-binding protein that interacts with actin filaments from bovine adrenal medulla.
    Proc Natl Acad Sci U S A. 1985 Aug;82(15):5025-9 PMID: 2991905
  25. Caldesmon150 regulates the tropomyosin-enhanced actin-myosin interaction in gizzard smooth muscle.
    Biochem Biophys Res Commun. 1985 Oct 30;132(2):645-51 PMID: 4062943
  26. Caldesmon is a Ca2+-regulatory component of native smooth-muscle thin filaments.
    Biochem J. 1985 Nov 1;231(3):517-22 PMID: 2934055
  27. Identification of a secretory granule-binding protein as caldesmon.
    Nature. 1986 Jan 2-8;319(6048):68-70 PMID: 3941739
  28. Identification by monoclonal antibodies and characterization of human platelet caldesmon.
    J Cell Biol. 1986 May;102(5):1748-57 PMID: 3517005
  29. Caldesmon is an elongated, flexible molecule localized in the actomyosin domains of smooth muscle.
    EMBO J. 1986 Feb;5(2):251-7 PMID: 3709514
  30. Vascular smooth muscle caldesmon.
    J Biol Chem. 1986 Jun 15;261(17):8028-35 PMID: 2940249
  31. Functional domain of caldesmon.
    FEBS Lett. 1986 Jul 7;202(2):182-6 PMID: 2941315
  32. The effects of caldesmon on smooth muscle heavy actomeromyosin ATPase activity and binding of heavy meromyosin to actin.
    J Biol Chem. 1986 Dec 5;261(34):16155-60 PMID: 2946681
  33. The mechanism of Ca2+ regulation of vascular smooth muscle thin filaments by caldesmon and calmodulin.
    J Biol Chem. 1987 Jan 5;262(1):116-22 PMID: 2947901
  34. Ca2+ can control vascular smooth-muscle thin filaments without caldesmon phosphorylation.
    Biochem J. 1986 Jul 15;237(2):605-7 PMID: 2948493
  35. The role of tropomyosin in the interactions of F-actin with caldesmon and actin-binding protein (or filamin).
    Eur J Biochem. 1987 Mar 16;163(3):467-71 PMID: 3830166
  36. Purification of caldesmon and myosin light chain (MLC) kinase from arterial smooth muscle: comparisons with gizzard caldesmon and MLC kinase.
    J Biochem. 1987 Jan;101(1):1-9 PMID: 3553171
  37. 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
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
Published
1987-12-00
Pages
9049-53
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC299689
Subset
IM
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