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PMID: 154671 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Calcium-sensitive regulation of actin-myosin interactions in baby hamster kidney (BHK-21) cells.

Yerna MJ, Dabrowska R, Hartshorne DJ, Goldman RD

Abstract

A fraction has been obtained from baby hamster kidney (BHK-21) cells that will stimulate the actin-moderated ATPase (ATP phosphohydrolase, EC 3.6.1.3) activity of both BHK-21 myosin and gizzard smooth muscle myosin. This activation is associated with the specific phosphorylation of the myosin 20,000-dalton light chain. The BHK-21 myosin light chain kinase preparation contains a major protein of approximately 105,000 molecular weight as determined by sodium dodecyl sulfate gel electrophoresis. Both the actin activation and phosphorylation events require the presence of Ca2+ and the so-called modulator or calcium-dependent regulator protein that has been isolated from smooth muscle, brain, and other tissues. On the basis of these results we propose that this kinase system constitutes a Ca2+-dependent regulatory mechanism for myosin-actin interactions in nonmuscle mammalian cells.

MeSH Terms
Actins/metabolism Adenosine Triphosphatases/metabolism Animals Calcium/physiology Cell Line Cell Movement Cricetinae Kidney Macromolecular Substances Molecular Weight Muscle, Smooth/metabolism Myosins/metabolism Phosphorylation Protein Kinases/metabolism
Chemicals
Actins Macromolecular Substances Protein Kinases Adenosine Triphosphatases Myosins Calcium
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Yerna M J
Dabrowska R
Hartshorne D J
Goldman R D
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29 references, click to expand
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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
1979-01-00
Pages
184-8
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC382901
Subset
IM
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