Perturbation of the Calmodulin System in Transformed Cells

  • Linda J. Van Eldik
  • Warren E. Zimmer
  • Steven W. Barger
  • D. Martin Watterson
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 269)


In eukaryotic cells, calcium acts as an intracellular signal transducer primarily through its interaction with a class of calcium binding proteins, of which calmodulin (CaM) is the most highly conserved, phylogenetically ubiquitous member (for reviews, see Van Eldik et al., 1982; Van Eldik and Roberts, 1988; Cohen and Klee, 1988). CaM transduces a calcium signal into a biological response by its ability to regulate the activity of other proteins in a calcium dependent manner. Because CaM is probably the most widely distributed mediator of intracellular calcium signals, fundamental insights can be derived from an enhanced knowlege about the genetic encoding, biosynthetic assembly and regulation of CaM-modulated calcium response pathways. Regardless, in order to understand fully the roles of CaM in the eukaryotic cell and obtain insight into how CaM-modulated pathways can respond differentially to calcium signals, it is necessary to be able to describe in some detail all of the CaM pathways for at least one biological system. This has not been done yet for any biological system. Chicken embryo fibroblasts (CEF) represent one biological system for which a relatively extensive body of information has been described. Also, CEF transformed by Rous sarcoma virus exhibit a number of phenotypic alterations that are potentially mediated by CaM and CaM binding proteins, and perturbations in CaM regulation have been described for normal and transformed CEF. In a more general sense, because perturbations of CaM pathways occur in many kinds of virus-transformed cells, knowledge of how alterations in CaM expression are coupled to oncogene expression may yield insight into how CaM-regulated calcium response pathways are involved in mechanisms of oncogenic transformation.


Myosin Light Chain Kinase Normal Rabbit Serum Chicken Embryo Fibroblast Rous Sarcoma Virus Deoxyglucose Uptake 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


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Copyright information

© Plenum Press, New York 1990

Authors and Affiliations

  • Linda J. Van Eldik
    • 1
    • 2
  • Warren E. Zimmer
    • 1
    • 3
  • Steven W. Barger
    • 2
  • D. Martin Watterson
    • 1
    • 3
  1. 1.Department of PharmacologyVanderbilt UniversityNashvilleUSA
  2. 2.Department of Cell BiologyVanderbilt UniversityNashvilleUSA
  3. 3.Howard Hughes Medical InstituteVanderbilt Univ.NashvilleUSA

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