TY - JOUR
T1 - Decreased retinoylation in NIH 3T3 cells transformed with activated Ha-ras
AU - Takahashi, Noriko
AU - De Luca, Luigi M.
AU - Breitman, Theodore R.
N1 - Funding Information:
*Department of Health Chemistry, Hoshi University, 4-41, Ebara 2-chome, Sinagawa-ku, Tokyo 142, Japan, ²Laboratory of Cellular Carcinogenesis and Tumor Promotion and ³Laboratory of Biological Chemistry, Division of Basic Sciences, National Cancer Institute, NIH, Bethesda, Maryland 20892-4255
PY - 1997/10/9
Y1 - 1997/10/9
N2 - Retinoylation (retinoic acid acylation) is a posttranslation modification of proteins occurring in a variety of mammalian cell lines and in vivo. To gain further knowledge of the role of retinoylation we studied it in NIH 3T3 cells and NIH 3T3 cells transformed by an activated Ha-ras oncogene (NIH Ha-ras-3T3 cells). In serum-free medium retinoic acid (RA) inhibited growth of NIH 3T3 cells but did not inhibit growth of NIH Ha-ras-3T3 cells. After incubation with [3H]RA, the level of retinoylated protein in NIH 3T3 cells was about 1.5-fold greater than in NIH Ha-ras-3T3 cells. On one-dimensional polyacrylamide gel electrophoresis, both the rate and the extent of retinoylation were greater in NIH 3T3 cells. We detected about 40 retinoylated proteins in NIH 3T3 cells by two-dimensional polyacrylamide gel electrophoresis. Only about 15 proteins were retinoylated, but at reduced levels, in NIH Ha-ras-3T3 cells. These results suggest that the activated ras oncogene inhibits retinoylation. This inhibition may in turn be related to the loss of other RA responses of NIH 3T3 cells, including growth inhibition, retinoic acid catabolism, down-regulation of fibronectin biosynthesis, and induction of tissue-type transglutaminase, which are not seen to the same extent in NIH Ha-ras-3T3 cells.
AB - Retinoylation (retinoic acid acylation) is a posttranslation modification of proteins occurring in a variety of mammalian cell lines and in vivo. To gain further knowledge of the role of retinoylation we studied it in NIH 3T3 cells and NIH 3T3 cells transformed by an activated Ha-ras oncogene (NIH Ha-ras-3T3 cells). In serum-free medium retinoic acid (RA) inhibited growth of NIH 3T3 cells but did not inhibit growth of NIH Ha-ras-3T3 cells. After incubation with [3H]RA, the level of retinoylated protein in NIH 3T3 cells was about 1.5-fold greater than in NIH Ha-ras-3T3 cells. On one-dimensional polyacrylamide gel electrophoresis, both the rate and the extent of retinoylation were greater in NIH 3T3 cells. We detected about 40 retinoylated proteins in NIH 3T3 cells by two-dimensional polyacrylamide gel electrophoresis. Only about 15 proteins were retinoylated, but at reduced levels, in NIH Ha-ras-3T3 cells. These results suggest that the activated ras oncogene inhibits retinoylation. This inhibition may in turn be related to the loss of other RA responses of NIH 3T3 cells, including growth inhibition, retinoic acid catabolism, down-regulation of fibronectin biosynthesis, and induction of tissue-type transglutaminase, which are not seen to the same extent in NIH Ha-ras-3T3 cells.
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U2 - 10.1006/bbrc.1997.7434
DO - 10.1006/bbrc.1997.7434
M3 - Article
C2 - 9345273
AN - SCOPUS:0031561378
SN - 0006-291X
VL - 239
SP - 80
EP - 84
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 1
ER -