Molecular chaperones regulate p53 and suppress senescence programs

Sherman, Michael Y.; Gabai, Vladimir L.; O'Callaghan, Cornelia; Yaglom, Julia A.

doi:10.1016/j.febslet.2007.05.036

Cited by 38 publications

(30 citation statements)

References 59 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The mechanism by which p53 promotes senescence is only partially understood. P53 target genes have been implicated in the induction of senescence, these include the CDK inhibitor p21, the plasminogen activator inhibitor-1 (PAI-1) (Mu and Higgins, 1995;Serrano et al, 1997) and MIC-1, a cytokine inducing senescence (Sherman et al, 2007).…”

Section: Introductionmentioning

confidence: 99%

E6AP is required for replicative and oncogene-induced senescence in mouse embryo fibroblasts

Levav-Cohen¹,

Wolyniec

Alsheich-Bartok³

et al. 2011

Oncogene

View full text Add to dashboard Cite

Section: Introductionmentioning

confidence: 99%

E6AP is required for replicative and oncogene-induced senescence in mouse embryo fibroblasts

Levav-Cohen¹,

Wolyniec

Alsheich-Bartok³

et al. 2011

Oncogene

View full text Add to dashboard Cite

“…Several reports also indicate that HSP60 plays immunoregulatory functions, moving this protein triggers a senescent status in neoblasts. Vertebrate and invertebrate mortalins have the ability to prevent senescence and apoptosis and promote cell immortalization by sequestering p53 protein in the cytoplasm (Wadhwa et al, 2002;Walker et al, 2006;Sherman et al, 2007). Cross-reaction with a heterologous antibody, designed against the mortalin p53-binding region also suggests that Djmot possesses an active p53-binding domain.…”

Section: Hsp70 Genesmentioning

confidence: 99%

Stem cell protection mechanisms in planarians: the role of some heat shock genes

Isolani¹,

Conte²,

Deri³

et al. 2012

Int. J. Dev. Biol.

View full text Add to dashboard Cite

Planarians contain a large population of stem cells, named neoblasts, and use these for continuous turnover of all cell types. In addition, thanks to the amazing flexibility of these cells, planarians respond well to the effects of stressful situations, for example activating regeneration after trauma. How neoblasts respond to stress and support continuous proliferation, maintaining long-term stability, is still an open question. Heat shock proteins (HSPs) are a complex protein family with key roles in maintaining protein homeostasis, as well as in apoptosis and growthrelated processes. We recently characterized some planarian homologs of hsp genes that are highly expressed in mammalian stem cells, and observed that some of them are critical for neoblast survival/maintenance. The results of these studies support the notion that some HSPs play crucial roles in the modulation of pathways regulating stem cell activity, regeneration and tissue repair. In this review we compare the evidence available for planarian hsp genes and focus on questions emerging from these results.

show abstract

“…HSP27 is a member of the small HSP family and acts as a powerful antagonist of programmed cell death in the regulation of epithelial cell growth and differentiation (Sherman & Goldberg 2001, Sherman et al 2007. Studies have shown that phosphorylated HSP27 enhances cell migration in several cell lines and tumor tissues (Morino et al 1997, Piotrowicz et al 1998, Rust et al 1999, Shin et al 2005.…”

Section: Endocrine-related Cancermentioning

confidence: 99%

Proteomic analysis of differentially expressed proteins in normal human thyroid cells transfected with PPFP

Li¹,

Wang²,

Liu³

et al. 2012

Endocrine-Related Cancer

View full text Add to dashboard Cite

The fusion gene encoding the thyroid-specific transcription factor PAX8 and peroxisome proliferator-activated receptor g (PPARg (PPARG)) (designated as the PPFP gene) is oncogenic and implicated in the development of follicular thyroid carcinoma (FTC). The effects of PPFP transfection on the biological characteristics of Nthy-ori 3-1 cells were studied by MTT assay, colony formation, soft-agar colony formation, and scratch wound-healing assays as well as by flow cytometry. Furthermore, the differentially expressed proteins were analyzed on 2-DE maps and identified by MALDI-TOF-MS. Validation of five identified proteins (prohibitin, galectin-1, cytokeratin 8 (CK8), CK19, and HSP27) was determined by western blot analysis. PPFP not only significantly increased the viability, proliferation, and mobility of the Nthy-ori 3-1 cells but also markedly inhibited cellular apoptosis. Twenty-eight differentially expressed proteins were identified, among which 19 proteins were upregulated and nine proteins were downregulated in Nthy-ori 3-1 PPFP (Nthy-ori 3-1 cells transfected with PPFP). The western blot results, which were consistent with the proteome analysis results, showed that prohibitin was downregulated, whereas galectin-1, CK8, CK19, and HSP27 were upregulated in Nthy-ori 3-1 PPFP . Our results suggest that PPFP plays an important role in malignant thyroid transformation. Proteomic analysis of the differentially expressed proteins in PPFP-transfected cells provides important information for further study of the carcinogenic mechanism of PPFP in FTCs.

show abstract

Molecular chaperones regulate p53 and suppress senescence programs

Cited by 38 publications

References 59 publications

E6AP is required for replicative and oncogene-induced senescence in mouse embryo fibroblasts

E6AP is required for replicative and oncogene-induced senescence in mouse embryo fibroblasts

Stem cell protection mechanisms in planarians: the role of some heat shock genes

Proteomic analysis of differentially expressed proteins in normal human thyroid cells transfected with PPFP

Contact Info

Product

Resources

About