Heat shock proteins; an overview.
Heat shock proteins (Hsps) protect protein substrates against conformational damage to promote the function of the proteins, prevent aggregation and prevent formation of toxic inclusion bodies. Protein aggregates and fibrils have been associated with neurodegenerative diseases and with inclusion bodies. High-level expression of recombinant protein for biotechnological purposes often leads to insoluble inclusion bodies. Therefore, misfolded proteins must be properly folded or must be degraded through heat shock protein action. This function protects cells against cytotoxic outcomes. In addition to their cytoprotective roles, Hsps are involved in other functions since Hsps exist in all types of cells and tissues. Therefore, several diseases are associated with alterations of these biochemical functions. This first review of the theme issue will discuss general properties of Hsps concisely along with their potential use in pharmaceutical and biotechnological applications.
Tutar
Lütfi
L
Department of Biology, Science Faculty, Selçuk University, Konya, Turkey.
Tutar
Yusuf
Y
D000682:Amyloid / Q000378:metabolism; D000818:Animals; D001709:Biotechnology / Q000379:methods; D006360:Heat-Shock Proteins / Q000096:biosynthesis / Q000378:metabolism / Q000502:physiology*; D006801:Humans; D002479:Inclusion Bodies / Q000378:metabolism; D019636:Neurodegenerative Diseases / Q000188:drug therapy / Q000378:metabolism; D017510:Protein Folding; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000494:pharmacology / Q000627:therapeutic use; D013379:Substrate Specificity
D000682:Amyloid; D006360:Heat-Shock Proteins; D011994:Recombinant Proteins