HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Paron, I Articles by Damante, G Search for Related Content PubMed PubMed Citation Articles by Paron, I Articles by Damante, G

Dipartimento di Scienze e Tecnologie Biomediche, Università degli Studi di Udine, Udine, Italy
¹ Proteomics and Mass Spectrometry Laboratory, ISPAAM, National Research Council, Napoli, Naples, Italy
² Dipartimento di Biologia e Patologia Cellulare e Molecolare c/o Centro di Endocrinologia ed Oncologia Sperimentale del CNR, Università degli Studi di Napoli, Naples, Italy

(Requests for offprints should be addressed to Giuseppe Damante, Dipartimento di Scienze e Tecnologie Biomediche, Piazzale Kolbe 1 – 33100 Udine, Italy; Email: GDamante{at}mail.dstb.uniud.it)

Tumour suppressor p53 is a transcription factor essential for DNA damage checkpoints during cellular response to stress. Mutations in the p53 gene are the most common genetic alterations found in human tumours; most pathogenetic modifications are missense mutations that abolish the p53 DNA-binding function. In the same cell type, distinct p53 missense mutations may determine different phenotypes. The PC Cl3 cell line retains several markers of thyroid differentiation in vitro. Introduction of the V143A mutant p53 allele, which abolishes the p53 DNA-binding function, leads to loss of differentiation markers as well as TSH dependency for growth. Conversely, PC Cl3 cells transfected with the S392A mutant p53 allele, presenting the mutation located outside the DNA-binding domain, show only loss of TSH dependency for growth. To identify molecular differences existing between PC Cl3 cell lines transformed by the V143A and the S392A mutant alleles, a differential proteomic approach was used. Two-dimensional gel electrophoresis analyses indicated that expression of a significant portion of protein species was modified by both p53 mutants. In fact, compared with wild-type PC Cl3 cells, modification of expression in V143A mutant cells occurred in 23.6% of the entire protein species. Conversely, modification of S392A mutant cells affected 14.0% of total proteins. Among these components, 8.3% were common to both mutants. Several of these proteins were identified by mass spectrometry procedures; some proteins, such as HSP90 and T-complex proteins, are already known to be related to p53 function.

This article has been cited by other articles:

				R. T. Netea-Maier, S. W. Hunsucker, B. M. Hoevenaars, S. M. Helmke, P. J. Slootweg, A. R. Hermus, B. R. Haugen, and M. W. Duncan Discovery and Validation of Protein Abundance Differences between Follicular Thyroid Neoplasms Cancer Res., March 1, 2008; 68(5): 1572 - 1580. [Abstract] [Full Text] [PDF]