Calmodulin Plays a Pivotal Role in Cellular Regulation
SciencePublished 4 January 1980
Wai Yiu Cheung
Citations2,443
SJR quartileQ1
SJR score10.42
SNIP6.62
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TL;DR
The role of calcium ions (Ca2+) in cell function is beginning to be unraveled at the molecular level as a result of recent research on calcium-binding proteins and particularly on calmodulin.
Abstract
The role of calcium ions (Ca2+) in cell function is beginning to be unraveled at the molecular level as a result of recent research on calcium-binding proteins and particularly on calmodulin. These proteins interact reversibly with Ca2+ to form a protein . Ca2+ complex, whose activity is regulated by the cellular flux of Ca2+. Many of the effects of Ca2+ appear to be exerted through calmodulin-regulated enzymes.
Keywords
Biochemistry, Genetics and Molecular Biology
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123 Citations1976Margaret A. Brostrom, Charles O. Brostrom +2 more
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120 Citations1979Thomas J. Lynch, Wai Yiu Cheung
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116 Citations1974Y Teshima, Shiro Kakiuchi
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115 Citations1971Jack Erlichman, Allen H. Hirsch +1 more
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110 Citations1976Y P Liu, Wai Yiu Cheung
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109 Citations1980Jeffrey F. Harper, Wai Yiu Cheung +4 more
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95 Citations1976Thomas J. Lynch, E. Ann Tallant +1 more
The results suggest that the formation of the enzyme-activator complex is dependent on Ca++, and that adenylate cyclase activityin vivo could be modulated by the cellular flux of Ca++.
PubMedSpecific visualization of the distribution of the calcium dependent regulatory protein of cyclic nucleotide phosphodiesterase (modulator protein) in tissue culture cells by immunofluorescence microscopy: mitosis and intercellular bridge.
94 Citations1978Bogi Andersen, Mary Osborn +1 more
Monospecific antibodies against the homogeneous Ca++ dependent regulatory protein of cyclic nucleotide phosphodiesterase (CDR protein) from bovine brain were used in indirect immunofluorescence microscopy to visualize the cytoplasmic organization of this key regulatory protein in growing tissue culture cells.
PubMedCircular dichroism studies on Ca2+-dependent protein modulator oxidized with N-chlorosuccinimide.
91 Citations1978Michael P. Walsh, Frits C. Stevens +2 more
The far-UV spectra of native and oxidized modulator protein are virtually indistinguishable, indicating that oxidation of surface methionine residues does not alter the overall conformation of the molecule.
PubMedChemical modification studies on the Ca2+-dependent protein modulator: the role of methionine residues in the activation of cyclic nucleotide phosphodiesterase.
90 Citations1978Martin Walsh, Stevens Fc
The phosphodiesterase binding domain of the modulator protein appears to be located between the second and third Ca2+-binding loops, a region of the molecule known from previous partial proteolysis studies.
Biochemical and Biophysical Research CommunicationsHigh levels of a calcium-dependent modulator protein in spermatozoa and its similarity to brain modulator protein
88 Citations1978Harold Jones, Marion M. Bradford +2 more
Sperm from hamster, human, rooster, rabbit and sea urchin were found to contain relatively high levels of calcium-dependent modulator protein, which is similar to porcine and brain modulator proteins in its ability to activate brain cyclic nucleotide phosphodiesterase, its heat stability and electrophoretic migration.
Proceedings of the National Academy of SciencesCalcium-sensitive regulation of actin-myosin interactions in baby hamster kidney (BHK-21) cells.
84 Citations1979M J Yerna, Renata Dąbrowska +2 more
A fraction has been obtained from baby hamster kidney (BHK-21) cells that will stimulate the actin-moderated ATPase (ATP phosphohydrolase), which constitutes a Ca2+-dependent regulatory mechanism for myosin-actin interactions in nonmuscle mammalian cells.
Biochemical and Biophysical Research CommunicationsLung surfactant synthesis: A Ca++-dependent microsomal phospholipase A2 in the lung
82 Citations1975Agustina Garcı́a, John D. Newkirk +1 more
Marker enzyme measurements showed that the microsomal activity cannot be due to contamination with mitochondria, which also show phospholipase A 2 in both lung and liver.
Archives of Biochemistry and BiophysicsRat brain adenylate cyclase
81 Citations1977Thomas J. Lynch, E. Ann Tallant +1 more
It is shown that particulate rat brain adenylate cyclase also required the Ca2+-binding protein activator for maximum activity, and results suggest that the action of the activator is independent of the other two ligands.
Biochemical and Biophysical Research CommunicationsActivation of tryptophan 5-monooxygenase by calcium-dependent regulator protein
81 Citations1979Takashi Yamauchi, Hitoshi Fujisawa
Rat brainstem tryptophan 5-monooxygenase was activated about 2-fold by rat brain calcium-dependent regulator (CDR) protein in the presence of low concentrations of Ca 2+.
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