MCP Waters-The Science of What's Possible
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
QUICK SEARCH:   [advanced]


     

A more recent version of this article appeared on April 1, 2002.
This Article
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
M100028-MCP200v1
1/4/280    most recent
Right arrow Submit a response
Right arrow Alert me when this article is cited
Right arrow Alert me when eLetters are posted
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow Glossary
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Benvenuti, S.
Right arrow Articles by Jat, P. S.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Benvenuti, S.
Right arrow Articles by Jat, P. S.
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

Submitted on October 31, 2001
Revised on March 11, 2002
Accepted on March 11, 2002

Differential proteome analysis of replicative senescence in rat embryo fibroblasts

Silvia Benvenuti, Rainer Cramer, Christopher C. Quinn, Jim Bruce, Marketa Zvelebil, Steven Corless, Jacquelyn Bond, Alice Yang, Susan Hockfield, Alma L. Burlingame, Michael D. Waterfield, and Parmjit S. Jat

Ludwig Institute for Cancer Research, London W1W 7BS

Corresponding Author: parmjit{at}ludwig.ucl.ac.uk

Normal somatic cells undergo a finite number of divisions and then cease dividing whereas cancer cells are able to proliferate indefinitely. To identify the underlying mechanisms that limit the mitotic potential, a 2-D differential proteome analysis of replicative senescence in serially passaged rat embryo fibroblasts was undertaken. Triplicate independent 2-D gels containing over 1200 spots each were run, curated and analysed. This revealed 49 spots whose expression was altered more than two-fold. Of these, 42 spots yielded positive protein identification by mass spectrometry comprising a variety of cytoskeletal, heat shock and metabolic proteins as well as proteins involved in trafficking, differentiation and protein synthesis, turnover and modification. These included gelsolin, a candidate tumour suppressor for breast cancer and -glucosidase II, a member of the family of glucosidases that includes klotho; a defect in klotho expression in mice results in a syndrome that resembles human ageing. Changes in expression of TUC-1, 2, 4 and 4 , members of the TUC family critical for neuronal differentiation, were also identified. Some of the identified changes were also shown to occur in two other models of senescence, premature senescence of REF52 cells and replicative senescence of mouse embryo fibroblasts. The majority of these candidate proteins were previously unrecognised in replicative senescence. They are now implicated in a new role.


Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
 J. Biol. Chem.Home page
M. de Graauw, I. Tijdens, R. Cramer, S. Corless, J. F. Timms, and B. van de Water
Heat Shock Protein 27 Is the Major Differentially Phosphorylated Protein Involved in Renal Epithelial Cellular Stress Response and Controls Focal Adhesion Organization and Apoptosis
J. Biol. Chem., August 19, 2005; 280(33): 29885 - 29898.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Biol. CellHome page
K. Hardy, L. Mansfield, A. Mackay, S. Benvenuti, S. Ismail, P. Arora, M. J. O'Hare, and P. S. Jat
Transcriptional Networks and Cellular Senescence in Human Mammary Fibroblasts
Mol. Biol. Cell, February 1, 2005; 16(2): 943 - 953.
[Abstract] [Full Text] [PDF]

Home page
 Am. J. Physiol. Renal Physiol.Home page
P. R. Cutillas, R. J. Chalkley, K. C. Hansen, R. Cramer, A. G. W. Norden, M. D. Waterfield, A. L. Burlingame, and R. J. Unwin
The urinary proteome in Fanconi syndrome implies specificity in the reabsorption of proteins by renal proximal tubule cells
Am J Physiol Renal Physiol, September 1, 2004; 287(3): F353 - F364.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Cell. ProteomicsHome page
P. Gromov, G. L. Skovgaard, H. Palsdottir, I. Gromova, M. Ostergaard, and J. E. Celis
Protein Profiling of the Human Epidermis from the Elderly Reveals Up-regulation of a Signature of Interferon-{gamma}-induced Polypeptides That Includes Manganese-superoxide Dismutase and the p85{beta} Subunit of Phosphatidylinositol 3-Kinase
Mol. Cell. Proteomics, February 1, 2003; 2(2): 70 - 84.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
 All ASBMB Journals   Journal of Biological Chemistry 
 Journal of Lipid Research   ASBMB Today 
Copyright © 2002 by the American Society for Biochemistry and Molecular Biology.