Literature DB >> 17205671

The cellular "networking" of mammalian Hsp27 and its functions in the control of protein folding, redox state and apoptosis.

André-Patrick Arrigo1.   

Abstract

Cells possess effective mechanisms to cope with chronic or acute disturbance of homeostasis. Key roles in maintaining or restoring homeostasis are played by the various heat shock or stress proteins (Hsps). Among the Hsps, the group of proteins characterized by low molecular masses (between 20 to 30 kDa) and homology to alpha-crystallin are called small stress proteins (denoted sHsps). The present chapter summarizes the actual knowledge of the protective mechanisms generated by the expression of mammalian Hsp27 (also denoted HspB1 in human) against the cytotoxicity induced by heat shock and oxidative stress. It also describes the anti-apoptotic properties of Hsp27 and their putative consequences in different pathological conditions.

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Year:  2007        PMID: 17205671     DOI: 10.1007/978-0-387-39975-1_2

Source DB:  PubMed          Journal:  Adv Exp Med Biol        ISSN: 0065-2598            Impact factor:   2.622


  80 in total

Review 1.  Mammalian HspB1 (Hsp27) is a molecular sensor linked to the physiology and environment of the cell.

Authors:  André-Patrick Arrigo
Journal:  Cell Stress Chaperones       Date:  2017-01-31       Impact factor: 3.667

2.  Insights into small heat shock protein and substrate structure during chaperone action derived from hydrogen/deuterium exchange and mass spectrometry.

Authors:  Guilong Cheng; Eman Basha; Vicki H Wysocki; Elizabeth Vierling
Journal:  J Biol Chem       Date:  2008-07-11       Impact factor: 5.157

Review 3.  Unfolding the relationship between secreted molecular chaperones and macrophage activation states.

Authors:  Brian Henderson; Samantha Henderson
Journal:  Cell Stress Chaperones       Date:  2008-10-29       Impact factor: 3.667

4.  Hormesis and Cellular Quality Control: A Possible Explanation for the Molecular Mechanisms that Underlie the Benefits of Mild Stress.

Authors:  F A C Wiegant; S A H de Poot; V E Boers-Trilles; A M A Schreij
Journal:  Dose Response       Date:  2012-11-16       Impact factor: 2.658

5.  Structure and properties of chimeric small heat shock proteins containing yellow fluorescent protein attached to their C-terminal ends.

Authors:  Petr N Datskevich; Nikolai B Gusev
Journal:  Cell Stress Chaperones       Date:  2013-11-27       Impact factor: 3.667

6.  Modification and reorganization of the cytoprotective cellular chaperone Hsp27 during herpes simplex virus type 1 infection.

Authors:  Shomita S Mathew; Megan P Della Selva; April D Burch
Journal:  J Virol       Date:  2009-07-08       Impact factor: 5.103

Review 7.  Small heat shock proteins in smooth muscle.

Authors:  Sonemany Salinthone; Manoj Tyagi; William T Gerthoffer
Journal:  Pharmacol Ther       Date:  2008-05-16       Impact factor: 12.310

8.  Oligo-microarray analysis and identification of stress-immune response genes from manila clam (Ruditapes philippinarum) exposure to heat and cold stresses.

Authors:  Udeni Menike; Youngdeuk Lee; Chulhong Oh; W D N Wickramaarachchi; H K A Premachandra; Se Chang Park; Jehee Lee; Mahanama De Zoysa
Journal:  Mol Biol Rep       Date:  2014-07-15       Impact factor: 2.316

9.  Sequestration of toxic oligomers by HspB1 as a cytoprotective mechanism.

Authors:  Juhi Ojha; Gunasingh Masilamoni; David Dunlap; Ross A Udoff; Anil G Cashikar
Journal:  Mol Cell Biol       Date:  2011-06-13       Impact factor: 4.272

10.  Ristocetin induces phosphorylated-HSP27 (HSPB1) release from the platelets of type 2 DM patients: Anti-platelet agent-effect on the release.

Authors:  Haruhiko Tokuda; Gen Kuroyanagi; Takashi Onuma; Yukiko Enomoto; Tomoaki Doi; Hiroki Iida; Takanobu Otsuka; Shinji Ogura; Toru Iwama; Kumi Kojima; Osamu Kozawa
Journal:  Biomed Rep       Date:  2018-02-06
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