Heat Shock Proteins In Biology Research Articles

Stress biology: Complexity and multifariousness in health and disease.

Preserving and regulating cellular homeostasis in the light of changing environmental conditions or developmental processes is of pivotal importance for single cellular and multicellular organisms alike. To counteract an imbalance in cellular homeostasis transcriptional programs evolved, called the heat shock response, unfolded protein response, and integrated stress response, that act cell-autonomously in most cells but in multicellular organisms are subjected to cell-nonautonomous regulation. These transcriptional programs downregulatethe expression of most genes but increase theexpression of heat shock genes, including genes encoding molecular chaperones and proteases, proteins involved in therepair of stress-induced damage to macromolecules and cellular structures. Sixty-one years after the discovery of the heat shock response by Ferruccio Ritossa, many aspects of stress biology are still enigmatic. Recent progress in the understanding of stress responses and molecular chaperones was reported at the 12th International Symposium on Heat Shock Proteins in Biology, Medicineand the Environment in the Old Town Alexandria, VA, USA from 28th to 31st of October 2023.

The XIth International Online Symposium on Heat Shock Proteins in Biology and Medicine

Single cell and multicellular organisms encounter physical stress from their environment as well as behavioral stress experienced in more complex organisms. As these stresses can present an existential threat, organisms respond with a coordinated response at the tissue and cellular level, the heat shock response (HSR) and this was the major theme of the symposium. Much of the meeting was concentrated on the heat shock proteins (HSPs), the effector molecules of the response. The balance between the potency of the HSR and the experience of stress naturally plays a key role in the etiology of many disease. Roles in cancer, the immune response, cell metabolism and aging were discussed at length at the meeting. Finally, a major goal of this field is to enhance the HSR in pathological conditions where it becomes inadequate or over stimulated and important findings regarding pharmacological approaches to modulating the HSR were discussed.

Heat-shock proteins in diagnosis and treatment: an overview of different biochemical and immunological functions.

Heat-shock proteins (HSPs) have been involved in different functions including chaperone activity, protein folding, apoptosis, autophagy and immunity. The HSP families have powerful effects on the stimulation of innate immune responses through Toll-like receptors and scavenger receptors. Moreover, HSP-mediated phagocytosis directly enhances the processing and presentation of internalized antigens via the endocytic pathway in adaptive immune system. These properties of HSPs have been used for development of prophylactic and therapeutic vaccines against infectious and noninfectious diseases. Several studies also demonstrated the relationship between HSPs and drug resistance as well as their use as a novel biomarker for detecting tumors in patients. The present review describes different roles of HSPs in biology and medicine especially biochemical and immunological aspects.

The IXth CSSI international symposium on heat shock proteins in biology and medicine: stress responses in health and disease : Alexandria Old Town, Alexandria, Virginia, November 10-13, 2018.

The stress response has been studied now for over 50years and is known to have significance in the survival of organisms in a challenging environment and in the healthy development of all known descendants of the last common universal ancestor (LUCA). This meeting was concentrated mostly on the responses of cells and organisms to environmental and cell stress including the impact of thermal stress, which was a major theme throughout this meeting. One emphasis was on the deployment of the heat shock response that permits damage to proteins to be detected and responded to by the abundant synthesis of heat shock proteins (HSPs). Speakers and presenters of posters responded to the questions of how are the HSPs rapidly induced by stressors? By which mechanisms are they are regulated in the cell by protein-protein interactions or posttranslational modification? And, what are the consequences when these abundantly expressed proteins escape the confines of the cell and influence the extracellular microenvironment? Key among the questions was how does stress influence longevity and aging and what happens in terms of disease control (malignant, neurodegenerative) when stress responses become compromised? In this context, many presenters addressed the question of pharmacologically modifying the heat shock response and HSP functions and thus improving responses to a range of disease types.

Report on the VIIth International Symposium on Heat Shock Proteins in Biology & Medicine.

This seventh symposium in a series on heat shock proteins in biology and medicine was held November 1-5, 2014, at the Hilton Hotel in Old Town Alexandria, Virginia. Approximately 70 participants including principal investigators, postdoctoral fellows, and graduate students were in attendance. The major themes were: new properties of heat shock proteins (HSPs) and heat shock factor (HSF) and role in the etiology of cancer, molecular chaperones in aging, extracellular HSPs in inflammation and immunity, role of heat shock and the heat shock response in immunity and cancer, protein aggregation disorders and HSP expression, and Hsp70 in blood cell differentiation. The next meeting is planned for the fall of 2016 in the same venue.

Heat shock proteins in physiology and pathology: the Berlin meeting

The IIIrd International Symposium on Heat Shock Proteins in Biology and Medicine took place at Charite University in Berlin, Germany, on 23-25 May 2006. This Symposium, concentrating on the physiological and pathological correlations associated with heat shock proteins and the stress response was organized in collaboration with the European Society for Hyperthermic Oncology (ESHO) and the Cell Stress Society International (Fig 1). It was the third in a series that began at Woods Hole, MA, USA, in 2000. The meeting attracted over 100 participants and included 41 oral presentations and 20 posters. It was most appropriate that the auditorium (Fig 2) was near the entrance to the Rudolf Virchow Krankenhaus (Fig 3), named for the father of modern cellular pathology. The meeting began with a return to roots with the session Molecular Chaperones. Bernd Bukau (University of Heidelberg, Germany) gave a beautiful presentation showing a novel function for HspllO family members as nucleotide exchange factors for Hsp70 proteins. He showed that the yeast hspilO homolog Sselp is a powerful nuclear exchange factor for yeast Hsp70 family members Ssal and Ssbl and that cells deficient in Sselp are sensitive to stress. Lawrence Hightower (University of Connecticut, USA) then spoke regarding members of the human Hsp70 family focusing on the hsp70B' isoform, the most strictly stress-inducible of the Hsp70 members. His studies indicate that hsp70B' performs a unique role in the stress response and is reciprocally regulated with other members of the Hsp70 family. The focus next switched to the small HSP in a presentation by Robert Tanguay (Laval University, Canada). Dr. Tanguay has shown in a number of publications in recent years a connection between the HSP and longevity. Indeed,

Introducing Professor Nikki Holbrook, Stress Signaling and Aging Section Editor

Introducing Professor Nikki Holbrook, Stress Signaling and Aging Section Editor

Emerging Role of Heat Shock Proteins in Biology and Medicine

All cells, procaryotic and eucaryotic, respond to an elevation in temperature by increasing the synthesis of a family of proteins collectively known as heat shock proteins (HSPs). HSPs are among the most highly conserved and abundant proteins in nature. Studies on the regulation of the synthesis of HSPs have for several years shed light on the mechanisms regulating gene expression. The results from recent years, showing that HSPs play crucial roles in a wide variety of normal cellular processes, has made them an object of even broader interest, first to molecular and cellular biologists and later to specialists in various fields of medicine including oncology, immunology, infectious disease, autoimmunity, embryology, neurology and endocrinology. The aim of this review is to briefly summarize our present knowledge of the regulation of the heat shock response and the structure of the relevant gene products, HSPs. Moreover, some of the exciting associations between HSPs and various fields of medicine will be discussed.