Literature DB >> 12729585

Heat shock proteins, cellular chaperones that modulate mitochondrial cell death pathways.

Arnaud Parcellier1, Sandeep Gurbuxani, Elise Schmitt, Eric Solary, Carmen Garrido.   

Abstract

Stress or heat shock proteins (HSPs) are ubiquitous and highly conserved proteins whose expression is induced in response to a wide variety of physiological and environmental insults. They allow the cells to survive to otherwise lethal conditions. Various mechanisms have been proposed to account for the cytoprotective functions of HSPs. These proteins play an essential role in intracellular "house-keeping" by assisting the correct folding of nascent and stress-accumulated misfolded proteins and preventing their aggregation. Several HSPs have also demonstrated to directly interact with various components of the tightly regulated programmed cell death machinery, upstream, and downstream of the mitochondrial events. Finally, HSPs could play a role in the proteasome-mediated degradation of selected proteins under stress conditions. Altogether, these properties could make HSPs appropriate targets for modulating cell death pathways.

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Year:  2003        PMID: 12729585     DOI: 10.1016/s0006-291x(03)00623-5

Source DB:  PubMed          Journal:  Biochem Biophys Res Commun        ISSN: 0006-291X            Impact factor:   3.575


  74 in total

1.  Hsp-27 induction requires POU4F2/Brn-3b TF in doxorubicin-treated breast cancer cells, whereas phosphorylation alters its cellular localisation following drug treatment.

Authors:  Rieko Fujita; Samir Ounzain; Alice Chun Yin Wang; Richard John Heads; Vishwanie Shanie Budhram-Mahadeo
Journal:  Cell Stress Chaperones       Date:  2011-01-29       Impact factor: 3.667

2.  In silico analyses of proteomic data suggest a role for heat shock proteins in umbilical cord blood hematopoietic stem cells.

Authors:  Angelo D'Alessandro; Giuliano Grazzini; Bruno Giardina; Lello Zolla
Journal:  Stem Cell Rev Rep       Date:  2010-12       Impact factor: 5.739

Review 3.  Role of Bcl-2 family proteins and caspases in the regulation of apoptosis.

Authors:  Mohammad Shamsul Ola; Mohd Nawaz; Haseeb Ahsan
Journal:  Mol Cell Biochem       Date:  2011-01-06       Impact factor: 3.396

4.  CD95-mediated alteration in Hsp70 levels is dependent on protein stabilization.

Authors:  Caoimhín G Concannon; Una FitzGerald; Carina I Holmberg; Eva Szegezdi; Lea Sistonen; Afshin Samali
Journal:  Cell Stress Chaperones       Date:  2005       Impact factor: 3.667

Review 5.  On the brotherhood of the mitochondrial chaperones mortalin and heat shock protein 60.

Authors:  Custer C Deocaris; Sunil C Kaul; Renu Wadhwa
Journal:  Cell Stress Chaperones       Date:  2006       Impact factor: 3.667

Review 6.  Apoptosis versus cell differentiation: role of heat shock proteins HSP90, HSP70 and HSP27.

Authors:  David Lanneau; Aurelie de Thonel; Sebastien Maurel; Celine Didelot; Carmen Garrido
Journal:  Prion       Date:  2007-01-24       Impact factor: 3.931

Review 7.  Heat shock protein 10 and signal transduction: a "capsula eburnea" of carcinogenesis?

Authors:  Anna M Czarnecka; Claudia Campanella; Giovanni Zummo; Francesco Cappello
Journal:  Cell Stress Chaperones       Date:  2006       Impact factor: 3.667

8.  Pioglitazone, a specific ligand of peroxisome proliferator-activated receptor-gamma, protects pancreas against acute cerulein-induced pancreatitis.

Authors:  Peter C Konturek; Artur Dembinski; Zygmunt Warzecha; Grzegorz Burnat; Piotr Ceranowicz; Eckhart G Hahn; Marcin Dembinski; Romana Tomaszewska; Stanislaw J Konturek
Journal:  World J Gastroenterol       Date:  2005-10-28       Impact factor: 5.742

Review 9.  Small heat-shock proteins: important players in regulating cellular proteostasis.

Authors:  Teresa M Treweek; Sarah Meehan; Heath Ecroyd; John A Carver
Journal:  Cell Mol Life Sci       Date:  2014-10-29       Impact factor: 9.261

10.  Cryptococcus neoformans gene expression during experimental cryptococcal meningitis.

Authors:  B R Steen; S Zuyderduyn; D L Toffaletti; M Marra; S J M Jones; J R Perfect; J Kronstad
Journal:  Eukaryot Cell       Date:  2003-12
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