Ubiquitin pools, ubiquitin mRNA levels, and ubiquitin-mediated proteolysis in aging human fibroblasts - PubMed (original) (raw)
Ubiquitin pools, ubiquitin mRNA levels, and ubiquitin-mediated proteolysis in aging human fibroblasts
J X Pan et al. Exp Gerontol. 1993 Jan-Feb.
Abstract
Senescent cells have less free ubiquitin and more ubiquitin-protein conjugates than do young cells. The ubiquitin-protein conjugates are heterogeneous in size but contain prominent bands at 106, 55, and 22 kDa. The age-related increase in ubiquitin-protein conjugates applies primarily to the 55-kDa band, while the 106-kDa and 22-kDa conjugates change little with age. Ubiquitin mRNA levels do not change with age, and the ability of cells to degrade two proteins that are good substrates for ubiquitin-mediated proteolysis is unaltered by aging. These results indicate that an increase in ubiquitin-protein conjugates does not necessarily reflect alterations in ubiquitin-mediated proteolysis. Furthermore, an overactive pathway of ubiquitin-mediated proteolysis does not appear to contribute to the proliferative arrest in senescent cells.
Comment in
- Effect of aging on ubiquitin-mediated proteolysis.
del Monte U, Costa RC, Bianchi C. del Monte U, et al. Exp Gerontol. 1994 Jan-Feb;29(1):101-2. doi: 10.1016/0531-5565(94)90066-3. Exp Gerontol. 1994. PMID: 8187836 No abstract available.
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