Relationship between changes in the calcium dependent regulatory protein and adenylate cyclase during viral transformation

LaPorte, David C.; Gidwitz, Susan; Weber, Michael J.; Storm, Daniel R.

doi:10.1016/0006-291x(79)90240-7

Cited by 62 publications

(17 citation statements)

References 8 publications

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“…For these reasons, many investigators have suggested that the activity ofcalmodulin would be primarily regulated by alterations in the net flux or distribution of Ca2' and not by changes in the intracellular concentration of the protein. However, increases in the amount of calmodulin relative to total protein have been reported in chicken embryo fibroblasts transformed by Rous sarcoma virus, with calmodulin levels quantitated by either densitometric scanning of polyacrylamide gels (4) or bioassay (5). While both reports demonstrated at least 2-fold increases in the calmodulin specific activity in the transformed cells, neither.…”

mentioning

confidence: 99%

Regulation of intracellular levels of calmodulin and tubulin in normal and transformed cells.

Chafouleas¹,

Pardue²,

Brinkley³

et al. 1981

Proc. Natl. Acad. Sci. U.S.A.

133

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Transformation of mammalian tissue culture cells by oncogenic viruses results in a 2-fold increase in the intracellular concentration of calmodulin quantitated by radioimmunoassay. The two pairs of companion cell lines used in this study were the Swiss mouse 3T3/simian virus 40-transformed 3T3 cells and the normal rat kidney (NRK)/Rous sarcoma virus-transformed NRK cells. The increased intracellular levels of calmodulin in the transformed cells are due to a greater increase in the rate of synthesis (3-fold) relative to the change in the rate ofdegradation (1.4-fold). On the other hand, no increases were observed in tubulin levels as quantitated by a colchicine-binding assay. The lack of change in tubulin concentration was accounted for by a 2-fold increase in the rate of degradation that is compensated by a similar increase in the rate of synthesis. The consequence of such changes in both transformed cell types is a 2-fold increase in the calmodulin-to-tubulin protein ratio relative to that in their nontransformed counterparts. 996The publication costs ofthis article were defrayed in part by page charge payment. This article must therefore be hereby marked "advertisement" in accordance with 18 U. S. C. §1734 solely to indicate this fact.

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mentioning

confidence: 99%

Regulation of intracellular levels of calmodulin and tubulin in normal and transformed cells.

Chafouleas¹,

Pardue²,

Brinkley³

et al. 1981

Proc. Natl. Acad. Sci. U.S.A.

133

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“…We (29) and others (8) have previously demonstrated that transformed CEF have two-to fourfold higher levels of freely soluble calmodulin. More recently, Van Eldik and Burgess (23) have measured calmodulin in subcellular fractions of CEF and have shown that the total levels of calmodulin are higher in the transformed cells and that there is no major subcellular redistribution of calmodulin in transformed CEF.…”

mentioning

confidence: 70%

Biosynthesis of calmodulin in normal and virus-transformed chicken embryo fibroblasts.

Zendegui¹,

Zielinski²,

Watterson³

et al. 1984

Mol. Cell. Biol.

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We report here that the higher levels of calmodulin in transformed chicken embryo fibroblasts are due to an increase in the rate of synthesis of calmodulin that results from an increased amount of calmodulinspecific mRNA in transformed cells. Transformation of several types of eucaryotic cells by oncogenic viruses results in a two-to threefold increase in the intracellular levels of calmodulin. We used the normal chicken embryo fibroblast and its Rous sarcoma virus-transformed counterpart to examine the biosynthesis of calmodulin. We show that the higher levels of calmodulin found in transformed fibroblasts appear to be the consequence of a selective increase in the rate of synthesis of calmodulin above that of total soluble or total cellular protein. A significant difference in the rate of degradation of calmodulin or total protein between transformed and normal cells was not detected. We also examined the mechanism of the increased synthesis rate of calmodulin and show that the levels of calmodulin mRNA are increased in transformed fibroblasts as measured by both translational activity and hybridization to a calmodulin cDNA probe. It is suggested by these data that the higher levels of calmodulin in transformed cells may result from a specific increase in the rate of either calmodulin gene transcription or mRNA processing.

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“…In addition, the results presented here identify specific targets or activities for potential calcium and calmodulin regulation in CEF. That some of the activities may change as a function of the cell cycle and upon viral transformation of CEF, coupled with the demonstrated changes in calmodulin levels during the cell cycle and upon viral transformation (2,(44)(45)(46), indicate future directions for a more complete understanding of the role of calmodulin in the regulation of cell function .…”

Section: Discussionmentioning

confidence: 99%

Identification of calmodulin-binding proteins in chicken embryo fibroblasts.

Burgess¹,

Watterson²,

Eldik³

1984

The Journal of Cell Biology

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We recently reported the detection of multiple classes of calmodulin-binding proteins in subcellular fractions of chicken embryo fibroblasts by using a gel binding procedure (Van Eldik, L.J., and W.H. Burgess, 1983, J. Biol. Chem., 258:4539-4547). In this report we identify many of these calmodulin-binding proteins and provide further evidence for the existence of multiple classes of calmodulin-binding proteins based on the interaction of these proteins with calmodulin and other calcium-modulated proteins. The fact that, in some cases, the same calmodulin-binding protein can bind troponin C and S100 alpha suggests that similar functional domains may be present in these distinct calcium-modulated proteins. We also have used protocols based on purification steps for calmodulin-binding proteins and calmodulin-regulated activities from other systems, in conjunction with enzymatic assays and various immunological methods, to identify many of the calmodulin-binding proteins in chicken embryo fibroblasts. The identities of these proteins suggest in vivo roles for calmodulin in the regulation of cell shape and motility, cyclic nucleotide metabolism, and possibly nucleic acid and protein turnover in fibroblasts.

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Relationship between changes in the calcium dependent regulatory protein and adenylate cyclase during viral transformation

Cited by 62 publications

References 8 publications

Regulation of intracellular levels of calmodulin and tubulin in normal and transformed cells.

Regulation of intracellular levels of calmodulin and tubulin in normal and transformed cells.

Biosynthesis of calmodulin in normal and virus-transformed chicken embryo fibroblasts.

Identification of calmodulin-binding proteins in chicken embryo fibroblasts.

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