The role of heat shock proteins as chaperones on several human diseases.
Some heat shock proteins HSPs, act as molecular chaperones. These and other molecular chaperones that are not HSPs, function in a variety of protein biosynthetic event and protect proteins from the deleterious effects of stressors by stabilizing, and refolding proteins. They assist protein folding, assembly, transport and degradation. Several human diseases such as neurodegeneration, cancer, aging, retinal dystrophy, and inflammation arise from defects HSPs and protein folding. This review demonstrates the chaperones such as properties of HSPs in cellular processes and their implication in different kind of human diseases.
Mellati
Ali A
AA
Department of Biochemistry, Zanjan University of Medical Sciences, Shahrak Karmandan, Zanjan, Iran. mellati3000@yahoo.com
D002318:Cardiovascular Diseases / Q000378:metabolism; D006360:Heat-Shock Proteins / Q000235:genetics / Q000378:metabolism*; D006801:Humans; D018832:Molecular Chaperones / Q000235:genetics / Q000378:metabolism*; D019636:Neurodegenerative Diseases / Q000378:metabolism; D017510:Protein Folding; D012164:Retinal Diseases / Q000378:metabolism
D006360:Heat-Shock Proteins; D018832:Molecular Chaperones