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- W845464209 abstract "Small heat shock proteins (sHSP) are involved in many essential cellular mechanisms both in physiologic and pathologic conditions. HSP27 (HSPB1), αB-crystallin (HSPB5) and HSP20 (HSPB6), the most studied members, are stress-inducible chaperones with an anti-aggregation function. They have been shown to inhibit apoptosis by interacting with proteins involved in programmed cell death such as cytochrome c or caspases, to have anti-oxidant properties and/or to modulate protein homeostasis by participating in the proteasomal degradation of specific proteins under stress conditions. Heat shock proteins accumulate in cancer cells and this overexpression is needed for the cancer cells’ survival. Accordingly, the inhibition of heat shock proteins such as HSP27 is an emerging strategy in cancer therapy (already is in phase II clinical trials). Fibrogenesis and cancer share several properties as both pathologies are characterized by genetic alterations, uncontrolled cell proliferation, altered cell interaction and communication and tissue invasion. The current review will discuss the involvement of HSP27, αB-crystallin and HSP20 in the process of fibrogenesis and in established organ fibrosis. We will dissect the impact of their function inducing the recruitment of inflammatory cells, the secretion of profibrotic cytokines, mainly Transforming Growth Factor-β1 (TGF-β1), and modulating oxidative stress, apoptosis and/or the proteasome system in the fibrotic process." @default.
- W845464209 created "2016-06-24" @default.
- W845464209 creator A5019231730 @default.
- W845464209 creator A5019497529 @default.
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- W845464209 creator A5056826196 @default.
- W845464209 creator A5064514391 @default.
- W845464209 creator A5077285569 @default.
- W845464209 date "2015-01-01" @default.
- W845464209 modified "2023-10-01" @default.
- W845464209 title "Small Heat Shock Proteins and Fibrosis" @default.
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