Cell protein degradation in cultured rat embryo fibroblasts suppression by vinblastine of the enhanced proteolysis by serum-deficient media

1976 ◽  
Vol 451 (2) ◽  
pp. 511-516 ◽  
Author(s):  
J.S. Amenta ◽  
F.M. Baccino ◽  
M.J. Sargus
Keyword(s):  
Protein Degradation ◽  
Cell Protein ◽  
Rat Embryo ◽  
Embryo Fibroblasts

scholarly journals Effect of microtubular or translational inhibitors on general cell protein degradation. Evidence for a dual catabolic pathway

1977 ◽  
Vol 168 (2) ◽  
pp. 223-227 ◽  
Author(s):  
J S Amenta ◽  
M J Sargus ◽  
F M Baccino
Keyword(s):  
Protein Degradation ◽  
Trichloroacetic Acid ◽  
Fold Increase ◽  
Cell Protein ◽  
Inhibitory Effects ◽  
Minimal Essential Medium ◽  
Catabolic Pathway ◽  
Rat Embryo ◽  
Step Down ◽  
Observation Period

Rat embryo fibroblasts were grown in Eagle's minimal essential medium with 10% serum and cell proteins prelabelled with L-[1-(14)C]leucine, followed by a 24h chase. When transferred to medium deprived of serum these cells showed a 2—3-fold increase in the production of trichloroacetic acid-soluble radioactivity during a 4h observation period. The microtubular poisons vinblastine, vincristine and colchicine partially inhibited this induced proteolysis, but had no effect on the proteolytic rate of cells maintained in medium with 10% serum. A similar discriminating effect on induced proteolysis was observed with cycloheximide, puromycin and insulin. The inhibitory effects of cycloheximide and vinblastine were not additive. These data support the hypothesis that, in addition to the basal turnover of cell proteins, a second mechanism of protein degradation involving cytoplasmic autophagy can be activated by nutritional step-down and is selectively inhibited by agents that interfere with microtubular function and protein synthesis.

scholarly journals Rapid catabolism of tyrosine-O-sulphated proteins and the formation of free tyrosine O-sulphate as an end product in rat embryo fibroblasts

1987 ◽  
Vol 243 (2) ◽  
pp. 555-559 ◽  
Author(s):  
M C Liu ◽  
M Suiko ◽  
F Lipmann
Keyword(s):  
Incubation Medium ◽  
Fresh Medium ◽  
Rat Embryo ◽  
Time Points ◽  
Rate Of Increase ◽  
Embryo Fibroblasts

Rat embryo fibroblasts, line 3Y1, were prelabelled for 24 h with [35S]sulphate and incubated in fresh medium without [35S]sulphate. A rapid efflux of the overall 35S-labelled compounds from the cells into the medium was observed. After 9 h of incubation, about 50% of the total 35S radioactivity appeared in the medium and up to 84.3% did so at the end of a 48 h incubation. Determination of [35S]sulphated macromolecules present in both the cell-associated and the incubation-medium fractions at different time points during incubation indicated that the majority of the 35S-labelled compounds released from the cells were low-Mr products derived from digestion of the [35S]sulphated macromolecules. Further analysis for tyrosine-O-[35S]sulphated proteins, which constituted only a small fraction of the overall [35S]sulphated macromolecules, showed that, after 9 h of incubation, there was a 65% decrease in the cell-associated fraction, and only 16.4% remained after 48 h. During that time, an amount equivalent to 20.7% of the cell-associated tyrosine-O-[35S]sulphated proteins originally present was released into the medium. Free tyrosine O-[35S]sulphate was generated in the cells and excreted into the incubation medium. Its rate of increase with time, however, was slow, and could account for only 12.4% of the tyrosine-O-[35S]sulphated proteins catabolized at the end of the 48 h incubation.

The role of the MEK/ERK pathway in regulation of HDACI-induced senescence of transformed rat embryo fibroblasts

2014 ◽  
Vol 8 (5) ◽  
pp. 374-383
Author(s):  
E. Yu. Kochetkova ◽  
T. V. Bykova ◽  
S. G. Zubova ◽  
T. V. Pospelova
Keyword(s):  
Erk Pathway ◽  
Rat Embryo ◽  
Embryo Fibroblasts

The mRNA 5' cap-binding protein, eIF-4E, cooperates with v-myc or E1A in the transformation of primary rodent fibroblasts

1992 ◽  
Vol 12 (3) ◽  
pp. 1234-1238
Author(s):  
A Lazaris-Karatzas ◽  
N Sonenberg
Keyword(s):  
Signal Transduction ◽  
Binding Protein ◽  
Signal Transduction Pathway ◽  
Transduction Pathway ◽  
Rat Embryo ◽  
Present Evidence ◽  
P21 Ras ◽  
Embryo Fibroblasts ◽  
Common Signal

We present evidence that eIF-4E, the mRNA 5' cap-binding protein, cooperates with two immortalizing oncogenes, v-myc and E1A, to cause transformation of rat embryo fibroblasts. eIF-4E alone can transform rat embryo fibroblasts when selection is applied. The pattern of transformation by eIF-4E is similar to that of p21 Ras, raising the possibility that eIF-4E shares a common signal transduction pathway with p21 Ras.

scholarly journals Transferrin Uptake by Cultured Rat Embryo Fibroblasts

2005 ◽  
Vol 115 (3) ◽  
pp. 611-618 ◽  
Author(s):  
Jean-Noël OCTAVE ◽  
Yves-Jacques SCHNEIDER ◽  
André TROUET ◽  
Robert R. CRICHTON
Keyword(s):  
Rat Embryo ◽  
Embryo Fibroblasts ◽  
Transferrin Uptake
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