A New Paradigm for Chaperone Proteins in Health and Disease
A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Molecular Biology".
Deadline for manuscript submissions: closed (15 November 2022) | Viewed by 9170
Special Issue Editor
Interests: Hsp60; Hsp10; mitochondrial chaperonins; mitochondrial matrix; immune-regulatory; aging; regeneration; mitochondrial unfold protein response; chaperonopathy; chaperonotherapy; protein folding and transport; heart failure; atherosclerosis; autoimmunity; neural degeneration; free radicals; autophagy; muscular degeneration and regeneration; apoptosis; atrophy and dystrophy; heat shock proteins; stress response; cancers; diabetes; chronic inflammation; fibrosis
Special Issue Information
Dear Colleagues,
Mammalian chaperones, including the families of heat shock proteins, are intriguing in their significance as “old molecules” made up of evolutionarily conserved sequences relating to bacterium, and yet the functions and signaling pathways leading to their activation as well as the consequences of induction in mammalian cells are not completely understood. By taking the mitochondrial chaperones as an example, mitochondrial chaperones, including mtHsp70, Hsp60, and Hsp10, and other assisting members are responsible for the folding of peptides imported into the mitochondrial matrix in addition to the refolding, degrading, and recycling of denatured proteins, thus protecting cells against noxious stress by maintaining mitochondrial homeostasis. The induction of chaperones, including mtHsp70 and Hsp60/10, has been found to be one of the beacons of the unfolded protein response in mitochondria. The association of changes in the expression of mitochondrial chaperones with human disease has been well-documented based on clinical samples from patients with cancer and associations with cancer prognoses, as well as those with cardiovascular and immune diseases; there are also data from animal models of neuronal, muscular, and inflammatory disorders showing the association of the expression of these chaperonins with disease. So far, the findings are far from conclusive. For example, while Hsp60 is elevated under many inflammatory states in various diseases, infringingly, it has long been known that Hsp60 expression in muscular tissues declines with ageing and in patients with metabolic disease, including obesity and diabetes featuring chronic inflammation.
The roles of mitochondrial chaperones are not limited to mitochondria. For example, inside the cell, Hsp60 and Hsp10 have been localized to the mitochondrial matrix, the cytosol, and the nucleus, and have also been found extracellularly, including inside exosomes. In different locations, Hsp60 binds to and modulates the trafficking and activities of important molecular clients, e.g., p53 and caspase 3, leading to its versatile roles in the cell cycle, apoptosis, senescence, and autophagy via those clients. New mechanisms of regulating the functions of clients by chaperones are continuing to be identified, e.g., the post-translational modification of Hsp60 and the subsequent effects on interactions with its molecular clients present many possibilities for the regulation of important cellular events.
For our Special Issue, entitled “A New Paradigm for Chaperone Proteins in Health and Disease”, we invite original research and review articles on topics related to new findings regarding the roles of chaperone proteins in all areas of biomedicine. We especially encourage the submission of reports on new cellular or animal models, as well as studies demonstrating the therapeutic potential of chaperones as molecular targets in the treatment of human diseases.
Dr. Kurt Ming-Chao Lin
Guest Editor
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Keywords
- Hsp60
- Hsp10
- mitochondrial chaperonins
- mitochondrial matrix
- immune-regulatory
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