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

M J Yerna | Zendy; Renata Da̧browska | Zendy; David J. Hartshorne | Zendy; Robert D. Goldman | Zendy

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

Author(s) -

M J Yerna,

Renata Da̧browska,

David J. Hartshorne,

Robert D. Goldman

Publication year - 1979

Publication title -

proceedings of the national academy of sciences

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 5.011

H-Index - 771

eISSN - 1091-6490

pISSN - 0027-8424

DOI - 10.1073/pnas.76.1.184

Subject(s) - baby hamster kidney cell , myosin , myosin light chain kinase , actin , hamster , phosphorylation , calcium , microbiology and biotechnology , biochemistry , biology , chemistry , immunoglobulin light chain , cell , organic chemistry , antibody , immunology

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.

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