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Isolating Potentiated Hsp104 Variants Using Yeast Proteinopathy Models
Published on: November 11, 2014
Hsp27 (HspB1) and alphaB-crystallin (HspB5) as therapeutic targets
André-Patrick Arrigo1, Stéphanie Simon, Benjamin Gibert
1Laboratoire Stress, Chaperons et Mort Cellulaire, CNRS, UMR5534, Centre de Génétique Moléculaire et Cellulaire, Université Lyon 1, Bat. Gregor Mendel, 16 Rue Dubois, F-69622, Villeurbanne Cedex, France. arrigo@univ-lyon1.fr
Abstract:
Hsp27 and alphaB-crystallin are molecular chaperones that are constitutively expressed in several mammalian cells, particularly in pathological conditions. These proteins share functions as diverse as protection against toxicity mediated by aberrantly folded proteins or oxidative-inflammation conditions. In addition, these proteins share anti-apoptotic properties and are tumorigenic when expressed in cancer cells. This review summarizes the current knowledge about Hsp27 and alphaB-crystallin and the implications, either positive or deleterious, of these proteins in pathologies such as neurodegenerative diseases, myopathies, asthma, cataracts and cancers. Approaches towards therapeutic strategies aimed at modulating the expression and/or the activities of Hsp27 and alphaB-crystallin are presented.
Insights
Heat shock protein 27 (Hsp27) and alphaB-crystallin are chaperones with dual roles in disease. They protect cells but can also promote cancer, highlighting their complex implications in various pathologies.
Area of Science:
- Molecular Biology
- Cellular Stress Response
- Pathology
Background:
- Heat shock protein 27 (Hsp27) and alphaB-crystallin are constitutively expressed molecular chaperones.
- These proteins protect cells against proteotoxicity, oxidative stress, and inflammation.
- Both Hsp27 and alphaB-crystallin exhibit anti-apoptotic properties and can be tumorigenic in cancer cells.
Purpose of the Study:
- To review current knowledge on Hsp27 and alphaB-crystallin.
- To explore the implications of these chaperones in various diseases.
- To present therapeutic strategies targeting Hsp27 and alphaB-crystallin.
Main Methods:
- Literature review of existing research on Hsp27 and alphaB-crystallin.
- Synthesis of information regarding their functions and roles in disease.
- Analysis of therapeutic approaches for modulating chaperone activity.
Main Results:
- Hsp27 and alphaB-crystallin have diverse protective functions.
- These chaperones are implicated in neurodegenerative diseases, myopathies, asthma, cataracts, and cancers.
- Their roles can be both beneficial and detrimental depending on the pathological context.
Conclusions:
- Hsp27 and alphaB-crystallin are key players in cellular homeostasis and disease pathogenesis.
- Modulating their expression or activity offers potential therapeutic avenues.
- Further research is needed to fully elucidate their complex roles and optimize therapeutic strategies.
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