Qr. Ye et al., EXPRESSION OF CALMODULIN AND CALMODULIN-BINDING PROTEINS IN RAT FIBROBLASTS STABLY TRANSFECTED WITH PROTEIN-KINASE-C AND ONCOGENES, Biochimica et biophysica acta. Molecular cell research, 1359(1), 1997, pp. 89-96
Molecular mechanisms leading to elevated calmodulin (CaM) expression i
n cancer have not yet been discovered. We have quantitated the levels
of transcripts derived from all three CaM genes in a variety of the sa
me origin rat fibroblasts transformed with oncogenes in combination wi
th gene for protein kinase C using Northern blot analysis with three C
aM gene specific cDNA probes. Five species of CaM mRNA were detected i
n all these cells. Surprisingly many of the investigated cell lines ex
hibited a decreased content of all CaM mRNAs as compared to control ce
lls with CaMI and CaMII transcripts showing the most pronounced altera
tions. In contrast, CaM protein levels were increased in all these cel
l lines as determined by a radioimmunoassay. These results suggest tha
t oncogenic up-regulation of CaM synthesis takes place posttranscripti
onally. Several CaM binding proteins were found at different concentra
tions in the studied cell lines depending on the oncogenes used for tr
ansformation. However, CaM overexpression does not seem to affect the
overall levels of CaM binding proteins. (C) 1997 Elsevier Science B.V.