Chaperonopathies of senescence and the scrambling of interactions between the chaperoning and the immune systems.
Aging entails progressive deterioration of molecules and supramolecular structures, including Hsp chaperones and their complexes, paralleled by functional decline. Recent research has changed our views on Hsp chaperones. They work inside and outside cells in many locations, alone or forming teams, interacting with cells, receptors, and molecules that are not chaperones, in roles that are not typically attributed to chaperones, such as protein folding. Hsp chaperones form a physiological system with a variety of functions and interactions with other systems, for example, the immune system. We propose that chaperone malfunctioning due to structural damage or gene dysregulation during aging has an impact on the immune system, creating the conditions for an overall malfunction of both systems. Pathological chaperones cannot interact with the immune system as normal ones do, and this leads to an overall readjustment of the interactions that is apparent during senescence and is likely to cause many of its manifestations.
University of Maryland Biotechnology Institute, Center of Marine Biotechnology, Columbus Center, Baltimore, Maryland, USA. macario@umbi.umd.edu
Alberto J L
AJ
Macario
Francesco
F
Cappello
Giovanni
G
Zummo
Everly
E
Conway de Macario
D000375:Aging / Q000235:genetics / Q000378:metabolism*; D002352:Carrier Proteins / Q000235:genetics / Q000378:metabolism*; D007107:Immune System / Q000378:metabolism*; D018832:Molecular Chaperones / Q000235:genetics / Q000378:metabolism* / Q000502:physiology*; D017510:Protein Folding
D002352:Carrier Proteins; D018832:Molecular Chaperones