The chaperone system in autoimmunity, inflammation, and virus-induced diseases: Role of chaperonins

Macario, Alberto J.L.; Conway de Macario, Everly

doi:10.1016/b978-0-12-817558-3.00010-x

Cited by 2 publications

(1 citation statement)

References 65 publications

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“…However, whether neuronal damage is caused by antiviral immunity or whether the virus triggers an autoimmune response is not yet clear. In relation to this, it is interesting to highlight that, since many members of the CS are evolutionarily conserved and present in all living systems, it cannot be excluded that molecular similarity (cross-reactive immunogenic-antigenic epitopes) between human CS and viral proteins may elicit autoimmune reactions [73]. Cross-similarity as the possible cause of autoimmunity has also been reported for SARS-CoV-2 [74].…”

Section: Multiple Sclerosis (Ms)mentioning

confidence: 99%

Putative Roles and Therapeutic Potential of the Chaperone System in Amyotrophic Lateral Sclerosis and Multiple Sclerosis

Noori,

Saqagandomabadi,

Di Felice

et al. 2024

Cells

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The putative pathogenic roles and therapeutic potential of the chaperone system (CS) in amyotrophic lateral sclerosis (ALS) and multiple sclerosis (MS) are reviewed to provide a bibliographic and conceptual platform for launching research on the diagnostic and therapeutic applications of CS components. Various studies suggest that dysfunction of the CS contributes to the pathogenesis of ALS and MS, and here, we identify some of the implicated CS members. The physiology and pathophysiology of the CS members can be properly understood if they are studied or experimentally or clinically manipulated for diagnostic or therapeutic purposes, bearing in mind that they belong to a physiological system with multiple interacting and dynamic components, widespread throughout the body, intra- and extracellularly. Molecular chaperones, some called heat shock protein (Hsp), are the chief components of the CS, whose canonical functions are cytoprotective. However, abnormal chaperones can be etiopathogenic factors in a wide range of disorders, chaperonopathies, including ALS and MS, according to the data reviewed. Chaperones typically form teams, and these build functional networks to maintain protein homeostasis, the canonical role of the CS. However, members of the CS also display non-canonical functions unrelated to protein homeostasis. Therefore, chaperones and other members of the CS, if abnormal, may disturb not only protein synthesis, maturation, and migration but also other physiological processes. Thus, in elucidating the role of CS components in ALS and MS, one must look at protein homeostasis abnormalities and beyond, following the clues emerging from the works discussed here.

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Section: Multiple Sclerosis (Ms)mentioning

confidence: 99%