| Popis: |
Heat shock proteins (HSPs) are molecular chaperons that are duly responsible for catalyzing the bonafide folding of incipient proteins as well as refolding of denatured proteins. Under certain pathological conditions, these stress proteins play a few cytoprotective ventures through the commencement of protein folding, repairing, misfolded peptide refolding, as well as feasible degradation of irremediable ones. Elevated reactive oxygen species (ROS) in cellular levels often result in imprudent apoptosis. This subsequently leads to the amplification of inflammatory reactions. This is familiar in the pathogenesis as well as in the succession of various human inflammatory diseases (HIDs), respiratory diseases, cancer, and other deadly diseases. For example, chronic obstructive pulmonary disease (COPD) is designated by an imbalance in oxidants and antioxidants, as well as vivid inflammatory response. Evidence proposes that HSPs have a crucial role in retaining a proper balance between oxidants/antioxidants in COPD patients. HSP 70 usually plays a key role in neuroprotection by delaying the prognosis of neurodegenerative diseases as well as preventing senescence. This chapter discusses how some of the important oxidative-stress-mediated human diseases can be barcoded by several heat shock proteins to redeem their disease-specific aggregation. |
