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Modulation of heat shock proteins by statins
dc.contributor.author | Forouzanfar F. | |
dc.contributor.author | Butler A.E. | |
dc.contributor.author | Banach M. | |
dc.contributor.author | Barreto G.E. | |
dc.contributor.author | Sahbekar A. | |
dc.date.accessioned | 2020-09-02T22:17:57Z | |
dc.date.available | 2020-09-02T22:17:57Z | |
dc.date.issued | 2018 | |
dc.identifier | 10.1016/j.phrs.2018.06.020 | |
dc.identifier.citation | 134, , 134-144 | |
dc.identifier.issn | 10436618 | |
dc.identifier.uri | https://hdl.handle.net/20.500.12728/4516 | |
dc.description | Heat shock proteins (HSP or stress proteins) are intracellular molecules that participate in physiological cell metabolism and growth, although they are known to be involved in many stress conditions. Statins inhibit the action of the enzyme 3-hydroxy-3-methylglutaryl-coenzyme A reductase (HMG-CoA), which is important in the synthesis of cholesterol and essential isoprenoid intermediates, thereby lowering circulating low-density lipoprotein cholesterol (LDL), a major risk factor for cardiovascular disease (CVD). This review provides new insights into the mechanisms of action of statins in the regulation of HSPs. A better understanding of this involvement can help in development of new and more effective treatment strategies for CVD. © 2018 Elsevier Ltd | |
dc.language.iso | en | |
dc.publisher | Academic Press | |
dc.subject | Atherogenesis | |
dc.subject | Heat shock proteins | |
dc.subject | HMG-CoA | |
dc.subject | Statin | |
dc.subject | alpha crystallin | |
dc.subject | atorvastatin | |
dc.subject | beta crystallin | |
dc.subject | C reactive protein | |
dc.subject | calnexin | |
dc.subject | calreticulin | |
dc.subject | cerivastatin | |
dc.subject | chaperonin 60 | |
dc.subject | cholesterol | |
dc.subject | fluindostatin | |
dc.subject | glucose regulated protein 78 | |
dc.subject | glycoprotein gp 96 | |
dc.subject | heat shock cognate protein 70 | |
dc.subject | heat shock protein | |
dc.subject | heat shock protein 110 | |
dc.subject | heat shock protein 27 | |
dc.subject | heat shock protein 40 | |
dc.subject | heat shock protein 47 | |
dc.subject | heat shock protein 70 | |
dc.subject | heat shock protein 90 | |
dc.subject | high density lipoprotein cholesterol | |
dc.subject | hydroxymethylglutaryl coenzyme A reductase | |
dc.subject | hydroxymethylglutaryl coenzyme A reductase inhibitor | |
dc.subject | isoprenoid | |
dc.subject | low density lipoprotein cholesterol | |
dc.subject | mevinolin | |
dc.subject | rosuvastatin | |
dc.subject | simvastatin | |
dc.subject | triacylglycerol | |
dc.subject | unindexed drug | |
dc.subject | heat shock protein | |
dc.subject | hydroxymethylglutaryl coenzyme A reductase inhibitor | |
dc.subject | lipid | |
dc.subject | angiogenesis | |
dc.subject | atherosclerosis | |
dc.subject | cardiovascular disease | |
dc.subject | cholesterol blood level | |
dc.subject | cholesterol synthesis | |
dc.subject | drug mechanism | |
dc.subject | human | |
dc.subject | hypercholesterolemia | |
dc.subject | modulation | |
dc.subject | pleiotropy | |
dc.subject | priority journal | |
dc.subject | protein function | |
dc.subject | protein localization | |
dc.subject | Review | |
dc.subject | risk factor | |
dc.subject | triacylglycerol blood level | |
dc.subject | animal | |
dc.subject | blood | |
dc.subject | cardiovascular disease | |
dc.subject | complication | |
dc.subject | drug effect | |
dc.subject | dyslipidemia | |
dc.subject | metabolism | |
dc.subject | signal transduction | |
dc.subject | Animals | |
dc.subject | Cardiovascular Diseases | |
dc.subject | Dyslipidemias | |
dc.subject | Heat-Shock Proteins | |
dc.subject | Humans | |
dc.subject | Hydroxymethylglutaryl-CoA Reductase Inhibitors | |
dc.subject | Lipids | |
dc.subject | Signal Transduction | |
dc.title | Modulation of heat shock proteins by statins | |
dc.type | Review |