Short Review on Types of Heat Shock Proteins and Their Fundamental Characters for Body Maintenance Together With Role in Cancer (original) (raw)
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Heat shock proteins: Molecules with assorted functions
2011
Heat shock proteins (Hsps) or molecular chaperones, are highly conserved protein families present in all studied organisms. Following cellular stress, the intracellular concentration of Hsps generally increases several folds. Hsps undergo ATP-driven conformational changes to stabilize unfolded proteins or unfold them for translocation across membranes or mark them for degradation. They are broadly classified in several families according to their molecular weights and functional properties. Extensive studies during the past few decades suggest that Hsps play a vital role in both normal cellular homeostasis and stress response. Hsps have been reported to interact with numerous substrates and are involved in many biological functions such as cellular communication, immune response, protein transport, apoptosis, cell cycle regulation, gametogenesis and aging. The present review attempts to provide a brief overview of various Hsps and summarizes their involvement in diverse biological activities.
Heat Shock Proteins - a Mini Review
2014
This article provides an insight towards the various applications of heat shock proteins and also gives a brief introduction, discovery & functions of heat shock proteins. An overview of role of heat shock proteins in cardiovascular disease, infectious diseases & in cancer is discussed. Heat shock proteins, a family of stress inducible proteins are involved in the pathogenesis of atherosclerotic vascular diseases, various infectious disease & also in tumor cells.
Heat shock proteins in human cancer
Electrophoresis, 2000
The heat shock proteins (hsp) are ubiquitous molecules induced in cells exposed to sublethal heat shock, present in all living cells, and highly conserved during evolution. Their function is to protect cells from environmental stress damage by binding to partially denatured proteins, dissociating protein aggregates, to regulate the correct folding, and to cooperate in transporting newly synthesized polypeptides to the target organelles. The molecular chaperones are involved in numerous diseases, including cancer, revealing changes of expression. In this review, we mainly describe the relationship of hsp expression with human cancer, and discuss what is known about their post-translational modifications according to malignancies.
Translationally controlled tumor protein is a novel heat shock protein with chaperone-like activity
Biochemical and Biophysical Research Communications, 2009
tumor protein (TCTP) is often designated as a stress-related protein because of 21 its highly regulated expression in stress conditions. Following a thermal shock, TCTP expression is highly 22 upregulated in a variety of cells. However, at present it is not known whether this upregulation has any 23 cell protective function similar to other heat shock proteins. In this study human TCTP (HuTCTP) and a 24 TCTP homolog (SmTCTP) from Schistosoma mansoni were evaluated for heat shock protein-like function and molecular chaperone activity. Our results show that similar to other molecular chaperones, both 26 human and parasite TCTPs can bind to a variety of denatured proteins and protect them from the harmful 27 effects of thermal shock. An important observation was the ability of both HuTCTP and SmTCTP to bind to 28 native protein and protect them from thermal denaturation. Over expression of TCTP in bacterial cells 29 protected them from heat shock-induced death. These findings suggest that TCTP may belong to a novel 30 small molecular weight heat shock protein.
Clinical and Therapeutic Significance of Heat Shock Proteins
International Journal of Approximate Reasoning, 2021
Multiple experimental investigations have been successful in suggesting the role of heat shock protein as a clinical biomarker and therapeutic target in several diseases. All living cells, from the simplest prokaryote to the most complex multicellular organism, contain heat shock proteins-molecular chaperones that are responsible for management of unfolded polypeptides within the cell. In view of the fundamental role of heat shock proteins in maintenance of protein homeostasis, it seems likely that malfunctions associated with members of heat shock protein families would have pathological effects. Such effects might be minimal under normal physiological conditions, but could be exacerbated at times. This review provides an overview of the cell biology and immunology of heat shock proteins focusing predominantly on immunological responses to heat shock proteins in a range of immune-mediated diseases and in infectious diseases.
65 | P a g e HEAT SHOCK PROTEINS -A MINI REVIEW
2020
This article provides an insight towards the various applications of heat shock proteins and also gives a brief introduction, discovery & functions of heat shock proteins. An overview of role of heat shock proteins in cardiovascular disease, infectious diseases & in cancer is discussed. Heat shock proteins, a family of stress inducible proteins are involved in the pathogenesis of atherosclerotic vascular diseases, various infectious disease & also in tumor cells.
Heat shock proteins: a therapeutic target worth to consider
Veterinary World, 2015
Heat shock proteins (HSPs) are the molecular chaperones, that are not only expressed during the normal growth process of cell cycle consecutively, but also get induced in cells during various stress conditions produced by cellular insult, environmental changes, temperature, infections, tumors etc. According to their molecular weight and functions, HSPs are divided into five major families. HSP90, HSP70, HSP60 and HSP100 are the most studied members of the family. Experimental studies have proved that overexpression and/or inhibition of HSPs play an important role in maintaining the tolerance and cell viability under above-described stress conditions. HSP90 is found to be a promising candidate for the diagnosis, prognosis and treatment of cancer. Similarly, HSP70, HSP60 and small HSPs experimentally and clinically have potential for the treatment of neurodegenerative disease, ischemia, cell death, autoimmunity, graft rejection, etc. In a way, exploring, the cytoprotective and immunoregulatory role of HSPs can open a new avenue for the drug discovery and treatment of critical diseases.
Heat Shock Proteins; An Overview
Current Pharmaceutical Biotechnology, 2010
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.
Clinical and Therapeutic Significance of Various Heat Shock Proteins
International Journal of Life Science and Pharma Research, 2021
The purpose of this study was to explore the different roles of heat shock proteins especially in immunity and infections. Heat shock proteins were discovered 56 years ago, and much of the work has focused on the role of these proteins that play in protecting cells from stress. Heat shock proteins are highly conserved class of proteins present in all species from bacteria to humans. Several experimental studies have been successful in pointing to the role of heat shock protein as a clinical biomarker and therapeutic target in a variety of diseases. It will also highlight features of HSP family, and will discuss future implications of HSPs in the diagnosis and prognosis of clinical and therapeutic significance. The development of membrane-interacting drugs that modify specific membrane domains, modulating heat shock response, may also be of significant therapeutic benefit. These proteins function as molecular chaperones, assisting in the refolding of misfolded proteins or their elimi...
The heat shock response is a rapid transient reprogramming of all cellular activities leading to a fast and complete recovery of the cell. Heat shock proteins (Hsps) form the most ancient cytoprotective system in all living organisms on earth and generally interact with a number of cellular systems. Both in vivo and in vitro studies proved that various environmental stressors over express Hsps to protect the cells. These proteins usually help to refold the misfolded proteins in an organism and also help to eliminate them if they become irreversibly damaged. Experiments are gradually revealing the promise of Hsps as pharmacological targets in health researches. Hsps are found to be over expressed in human diseases like cancer, arthritis, diabetes, cardiac and autoimmune diseases. Based on a direct correlation between the level of stress and the expression of heat shock proteins, an idea in research that has emerged is the use of stress genes or proteins expression as an indicator to evaluate the level of toxicity. Heat shock proteins can be used extensively as molecular biomarkers in the biomonitoring and toxicological researches. Study of the expressions of heat shock proteins in common soil organisms such as microbes, rotifers, earthworms and in the higher vertebrates as well can reveal the extent of contamination and possible health hazards. However, it is very difficult to identify a specific environmental problem which is solely responsible for heat shock response in a particular organism. Further investigations are required to get deeper insights in the multidimensional appilcations of Hsps in the medical diagnostics and environmental monitoring.