Literature DB >> 15992180

Heat shock proteins: new keys to the development of cytoprotective therapies.

M Tytell1, P L Hooper.   

Abstract

All cells, from bacterial to human, have a common, intricate response to stress that protects them from injury. Heat shock proteins (Hsps), also known as stress proteins and molecular chaperones, play a central role in protecting cellular homeostatic processes from environmental and physiologic insult by preserving the structure of normal proteins and repairing or removing damaged ones. An understanding of the interplay between Hsps and cell stress tolerance will provide new tools for treatment and drug design that maximise preservation or restoration of health. For example, the increased vulnerability of tissues to injury in some conditions, such as ageing, diabetes mellitus and menopause, or with the use of certain drugs,, such as some antihypertensive medications, is associated with an impaired Hsp response. Additionally, diseases that are associated with tissue oxidation, free radical formation, disorders of protein folding, or inflammation, may be improved therapeutically by elevated expression of Hsps. The accumulation of Hsps, whether induced physiologically, pharmacologically, genetically, or by direct administration of the proteins, is known to protect the organism from a great variety of pathological conditions, including myocardial infarction, stroke, sepsis, viral infection, trauma, neurodegenerative diseases, retinal damage, congestive heart failure, arthritis, sunburn, colitis, gastric ulcer, diabetic complications and transplanted organ failure. Conversely, lowering Hsps in cancer tissues can amplify the effectiveness of chemo- or radiotherapy. Treatments and agents that induce Hsps include hyperthermia, heavy metals (zinc and tin), salicylates, dexamethasone, cocaine, nicotine, alcohol, alpha-adrenergic agonists, PPAR-gamma agonists, bimoclomol, geldanamycin, geranylgeranylacetone and cyclopentenone prostanoids. Compounds that suppress Hsps include quercetin (a bioflavinoid), 15-deoxyspergualin (an immunosuppressive agent) and retinoic acid. Researchers who are cognisant of the Hsp-related effects of these and other agents will be able to use them to develop new therapeutic paradigms.

Entities:  

Year:  2001        PMID: 15992180     DOI: 10.1517/14728222.5.2.267

Source DB:  PubMed          Journal:  Expert Opin Ther Targets        ISSN: 1472-8222            Impact factor:   6.902


  22 in total

1.  Administration of Hsp70 in vivo inhibits motor and sensory neuron degeneration.

Authors:  J Lille Tidwell; Lucien J Houenou; Michael Tytell
Journal:  Cell Stress Chaperones       Date:  2004-03       Impact factor: 3.667

Review 2.  Heat shock protein 70: roles in multiple sclerosis.

Authors:  María José Mansilla; Xavier Montalban; Carmen Espejo
Journal:  Mol Med       Date:  2012-09-07       Impact factor: 6.354

Review 3.  Xenohormesis: health benefits from an eon of plant stress response evolution.

Authors:  Philip L Hooper; Paul L Hooper; Michael Tytell; Lászlo Vígh
Journal:  Cell Stress Chaperones       Date:  2010-06-04       Impact factor: 3.667

4.  Short-term hyperthermia prevents activation of proinflammatory genes in fibroblast-like synoviocytes by blocking the activation of the transcription factor NF-kappaB.

Authors:  Marica Markovic; Karl M Stuhlmeier
Journal:  J Mol Med (Berl)       Date:  2006-09-06       Impact factor: 4.599

Review 5.  Heat shock proteins and kidney disease: perspectives of HSP therapy.

Authors:  Natalia Chebotareva; Irina Bobkova; Evgeniy Shilov
Journal:  Cell Stress Chaperones       Date:  2017-04-13       Impact factor: 3.667

Review 6.  Emerging Role of Nitric Oxide and Heat Shock Proteins in Insulin Resistance.

Authors:  Marisa Nile Molina; León Ferder; Walter Manucha
Journal:  Curr Hypertens Rep       Date:  2016-01       Impact factor: 5.369

7.  Recent advances in the management of radiation colitis.

Authors:  Jannis Kountouras; Christos Zavos
Journal:  World J Gastroenterol       Date:  2008-12-28       Impact factor: 5.742

8.  HSP72 attenuates renal tubular cell apoptosis and interstitial fibrosis in obstructive nephropathy.

Authors:  Haiping Mao; Zhilian Li; Yi Zhou; Zhijian Li; Shougang Zhuang; Xin An; Baiyu Zhang; Wei Chen; Jing Nie; Zhiyong Wang; Steven C Borkan; Yihan Wang; Xueqing Yu
Journal:  Am J Physiol Renal Physiol       Date:  2008-04-16

9.  Hsp70 localizes differently from chaperone Hsc70 in mouse mesoangioblasts under physiological growth conditions.

Authors:  Giuseppina Turturici; Fabiana Geraci; Maria Elena Candela; Giovanni Giudice; Fidelina Gonzalez; Gabriella Sconzo
Journal:  J Mol Histol       Date:  2008-10-08       Impact factor: 2.611

10.  Acute toxicity and gastroprotective role of M. pruriens in ethanol-induced gastric mucosal injuries in rats.

Authors:  Shahram Golbabapour; Maryam Hajrezaie; Pouya Hassandarvish; Nazia Abdul Majid; A Hamid A Hadi; Noraziah Nordin; Mahmood A Abdulla
Journal:  Biomed Res Int       Date:  2013-05-28       Impact factor: 3.411

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