Ubiquitin pools, ubiquitin mRNA levels, and ubiquitin-mediated proteolysis in aging human fibroblasts

Jia Xiu Pan, Sharla R. Short, Stephen A Goff, J. Fred Dice

Research output: Contribution to journalArticle

26 Citations (Scopus)

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.

Original languageEnglish (US)
Pages (from-to)39-49
Number of pages11
JournalExperimental Gerontology
Volume28
Issue number1
DOIs
StatePublished - 1993
Externally publishedYes

Fingerprint

Proteolysis
Fibroblasts
Ubiquitin
Aging of materials
Messenger RNA
Proteins

ASJC Scopus subject areas

  • Aging
  • Medicine(all)

Cite this

Ubiquitin pools, ubiquitin mRNA levels, and ubiquitin-mediated proteolysis in aging human fibroblasts. / Pan, Jia Xiu; Short, Sharla R.; Goff, Stephen A; Dice, J. Fred.

In: Experimental Gerontology, Vol. 28, No. 1, 1993, p. 39-49.

Research output: Contribution to journalArticle

@article{1d57f31dc3584dca808e6babfacc2863,
title = "Ubiquitin pools, ubiquitin mRNA levels, and ubiquitin-mediated proteolysis in aging human fibroblasts",
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.",
author = "Pan, {Jia Xiu} and Short, {Sharla R.} and Goff, {Stephen A} and Dice, {J. Fred}",
year = "1993",
doi = "10.1016/0531-5565(93)90018-9",
language = "English (US)",
volume = "28",
pages = "39--49",
journal = "Experimental Gerontology",
issn = "0531-5565",
publisher = "Elsevier Inc.",
number = "1",

}

TY - JOUR

T1 - Ubiquitin pools, ubiquitin mRNA levels, and ubiquitin-mediated proteolysis in aging human fibroblasts

AU - Pan, Jia Xiu

AU - Short, Sharla R.

AU - Goff, Stephen A

AU - Dice, J. Fred

PY - 1993

Y1 - 1993

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=0027386791&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0027386791&partnerID=8YFLogxK

U2 - 10.1016/0531-5565(93)90018-9

DO - 10.1016/0531-5565(93)90018-9

M3 - Article

VL - 28

SP - 39

EP - 49

JO - Experimental Gerontology

JF - Experimental Gerontology

SN - 0531-5565

IS - 1

ER -