Heat Shock Proteins; An Overview

Abstract

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.

Huperzine A derivative M3 protects PC12 cells against sodium nitroprusside-induced apoptosis

“…Indeed, treatment with M3 induced the expression of Hsp70 in a timedependent manner, unlike HupA. Hsp70, a member of the [13,14] .…”

Heat Shock Protein as Emerging Oncologic Drug Targets

“…Proteins are key macromolecules in biochemical cascades and they must be correctly folded and stabilized for proper function. Hsps chaperone cellular proteins to maintain native substrate protein structure and behave as cellular mechanics to fix substrate proteins [1].…”

“…Each compartment must be protected separately from stressors and this is probably the reason of Hsps existence in different cellular compartments. Heat, parasites, fungi, ischemia, infectious agents, malignancy, oxidative stress, and drugs are stressors and further cell protect itself from the effects of these factors by expressing Hsps for cell survival [1]. Under stress, cell induces more inductive Hsp form to help constitutively expressed Hsp.…”

Drug Dependent Stress and Heat Shock Protein Response

“…Hsps are chaperone cellular proteins by maintaining their native folded form so that they can perform their biochemical function promptly [1].…”

“…Hsps are induced by several factors including infectious agents, heat, parasites, fungi, ischemia, malignancy, and oxidative stress as well as drugs [1].…”