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- Publisher
- Springer Journals
- Copyright
- Copyright © 1999 by Kluwer Academic Publishers
- Subject
- Life Sciences; Cardiology; Medical Biochemistry; Oncology; Biochemistry, general
- ISSN
- 0300-8177
- eISSN
- 1573-4919
- DOI
- 10.1023/A:1006978622240
- Publisher site
- See Article on Publisher Site
Abstract
Murine embryonic 3T3-F442A fibroblasts contain elevated levels of a factor (dRF) inhibitory to the phosphorylation of PKR, when cultured under differentiation restrictive (10% cat serum) as compared to permissive conditions (10% fetal bovine serum). Experiments were conducted with the objective of understanding the effect of altered PKR activity on the growth characteristics of 3T3-F442A fibroblasts. Analysis of the phosphoprotein pattern confirmed that the phosphorylation of PKR was reduced in cells cultured in cat serum during specific stages of growth. In a similar manner, evaluation of eIF-2α phosphorylation by vertical slab gel iso-electric focusing indicated that inactivation of PKR correlated with reduction of eIF-2α phosphorylation. The expression of PKR was confirmed by western blotting ruling out the possibility of diminished protein as the cause of loss of activity. In addition, the expression of dRF coincided with the inactivation of PKR as shown by immunoblotting and phosphorylation studies. The reduction in PKR activity and subsequent deregulation of eIF-2α phosphorylation was related to appearance of tumor-like cellular morphology and increased cell density as shown by cell counts and [3H]-thymidine uptake. Taken together, these results support a hypothesis that PKR functions to regulate the growth of 3T3-F442A cells. Furthermore, our findings raise the possibility that deregulation of PKR by endogenous inhibitory molecules, such as dRF, may alter normal growth and differentiation. Such a deregulation of PKR may also contribute to the proliferation of tumor cells.
Journal
Molecular and Cellular Biochemistry – Springer Journals
Published: Sep 30, 2004