Heat Shock Proteins and Phytochemicals: Role in Human Health and Disease

2016 ◽  
pp. 211-232
Author(s):  
Xinyu Wang ◽  
Srujana Rayalam ◽  
Vishakha Bhave
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Human Health ◽  
Health And Disease ◽  
Shock Proteins

Heat Shock Proteins (Hsp): Classifications and Its Involvement in Health and Disease

2017 ◽  
Vol 3 (3) ◽  
pp. 334-337
Author(s):  
Karuna Datta ◽  
Kshitij Rahalkar ◽  
Dinesh Kumar Dubey
Keyword(s):  
Wound Healing ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Heat Shock Protein ◽  
High Pressures ◽  
Cellular Proteins ◽  
Morphological Alterations ◽  
Health And Disease ◽  
Folded Proteins ◽  
Shock Proteins

For the reason that no model will ever totally replicate clinical human wound healing, it is necessary that the model operated be selected with care. Heat shock proteins (HSP) are articulated in response to numerous biological stresses, comprising heat, high pressures, and toxic composites. It is also one of the mainly bountiful cellular proteins found under non-stress situation.Hsp70 and Hsp90 refer to families of heat shock proteins on the order of 70,90 kilodaltons in size, respectively. The small 8-kilodalton protein ubiquitin, which marks proteins for degradation, also has features of a heat shock protein. Cells are attentive about getting these folds right for the reason that mis folded proteins can change the normal life of the cell. In some cases change is good, in others deadly. When Heat Shock Proteins90 is conceded the number of morphological alterations upsurges, which lead to creation of inactive or abnormally active polypeptides.

scholarly journals Heat shock proteins as modulators and therapeutic targets of chronic disease: an integrated perspective

2017 ◽  
Vol 373 (1738) ◽  
pp. 20160521 ◽  
Author(s):  
Adrienne L. Edkins ◽  
John T. Price ◽  
A. Graham Pockley ◽  
Gregory L. Blatch
Keyword(s):  
Chronic Disease ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Critical Role ◽  
Therapeutic Targets ◽  
Theme Issue ◽  
Human Disorders ◽  
Health And Disease ◽  
Shock Proteins ◽  
And Function

Many heat shock proteins (HSPs) are essential to survival as a consequence of their role as molecular chaperones, and play a critical role in maintaining cellular proteostasis by integrating the fundamental processes of protein folding and degradation. HSPs are arguably among the most prominent classes of proteins that have been broadly linked to many human disorders, with changes in their expression profile and/or intracellular/extracellular location now being described as contributing to the pathogenesis of a number of different diseases. Although the concept was initially controversial, it is now widely accepted that HSPs have additional biological functions over and above their role in proteostasis (so-called ‘protein moonlighting’). Most importantly, these new insights are enlightening our understanding of biological processes in health and disease, and revealing novel and exciting therapeutic opportunities. This theme issue draws on therapeutic insights from established research on HSPs in cancer and other non-communicable disorders, with an emphasis on how the intracellular function of HSPs contrasts with their extracellular properties and function, and interrogates their potential diagnostic and therapeutic value to the prevention, management and treatment of chronic diseases. This article is part of the theme issue ‘Heat shock proteins as modulators and therapeutic targets of chronic disease: an integrated perspective’.

scholarly journals Heat Shock Proteins in Glioblastoma Biology: Where Do We Stand?

2019 ◽  
Vol 20 (22) ◽  
pp. 5794 ◽  
Author(s):  
Rebeca Piatniczka Iglesia ◽  
Camila Felix de Lima Fernandes ◽  
Bárbara Paranhos Coelho ◽  
Mariana Brandão Prado ◽  
Maria Isabel Melo Escobar ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Cell Types ◽  
Current Evidence ◽  
Health And Disease ◽  
Shock Proteins ◽  
Mitochondrial Chaperones ◽  
Different Cell Types ◽  
Small Subpopulation

Heat shock proteins (HSPs) are evolutionary conserved proteins that work as molecular chaperones and perform broad and crucial roles in proteostasis, an important process to preserve the integrity of proteins in different cell types, in health and disease. Their function in cancer is an important aspect to be considered for a better understanding of disease development and progression. Glioblastoma (GBM) is the most frequent and lethal brain cancer, with no effective therapies. In recent years, HSPs have been considered as possible targets for GBM therapy due their importance in different mechanisms that govern GBM malignance. In this review, we address current evidence on the role of several HSPs in the biology of GBMs, and how these molecules have been considered in different treatments in the context of this disease, including their activities in glioblastoma stem-like cells (GSCs), a small subpopulation able to drive GBM growth. Additionally, we highlight recent works that approach other classes of chaperones, such as histone and mitochondrial chaperones, as important molecules for GBM aggressiveness. Herein, we provide new insights into how HSPs and their partners play pivotal roles in GBM biology and may open new therapeutic avenues for GBM based on proteostasis machinery.

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