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| Author | : Mac Breven Robinson |
| Publisher | : |
| Total Pages | : 432 |
| Release | : 2007 |
| Genre | : |
| ISBN | : |
| Author | : Lynsi Henrickson |
| Publisher | : |
| Total Pages | : 89 |
| Release | : 2010 |
| Genre | : |
| ISBN | : |
The physiological responses to stressor exposure can be broadly grouped into the organismal and the cellular stress responses. The organismal stress response involves the release of hormones into general circulation, while the cellular stress response involves the synthesis of proteins, the most important being the heat shock proteins (HSPs), which play a role in maintaining protein homeostasis. Elevated HSP70 expression in response to stressors has been demonstrated in trout (Oncorhynchus mykiss) red blood cells (RBCs). The ease of repeated sampling of blood suggests the possibility of using this tissue as a non-lethal marker of cellular stress in fish. This study tested the hypothesis that stressor exposure will elevate HSP70 expression in trout RBCs and the role of stress hormones in mediating this response. Acute heat shock exposure (+12oC) significantly elevated plasma cortisol, glucose and lactate levels in heat shocked fish over 24 h. A tissue-specific response was seen in HSP70 expression in liver, brain, gill and RBCs. To enable measurement of RBC HSP70 concentrations, an enzyme-linked immunosorbent assay (ELISA) was developed using a commercially available rabbit anti-salmon HSP70 and a recombinant chinook salmon (Oncorhynchus tshawytscha) HSP70. To determine effects of chronic exposure, two studies were conducted exposing trout to either cadmium (0, 0.75 or 2.0 [mu]g/L over 28 d) or municipal wastewater effluent (0, 20 or 90% over 14 d). However, neither exposure elicited a significant HSP70 response. Effects of stress hormones on RBC HSP70 levels were tested by exposing cells in vitro to either cortisol (10 and 100 ng/mL) or epinephrine (10 nM) with or without heat shock. Heat shock elevated HSP70 content in trout RBCs but no modulation by stress hormones was seen. It was shown for the first time that RBCs release HSP70 content into the medium in response to an acute heat shock and this release is attenuated by stress hormones. Overall, HSP70 levels in RBCs have the potential to be a reliable non-lethal marker of acute cellular stress effects in fish. The release of HSP70 from RBCs leads to the hypothesis that HSP70 may also have an extracellular role in fish, and warrants further study.
| Author | : Chad Christopher Smith |
| Publisher | : |
| Total Pages | : 290 |
| Release | : 2015 |
| Genre | : Apoptosis |
| ISBN | : |
DNAJB6 is a member of the HSP40 family of heat shock proteins (HSPs), a family of proteins that canonically acts as co-chaperones for the refolding of misfolded and damaged proteins in cells undergoing stress from heat shock or exposure to toxic compounds. Although most studies on DNAJB6 have focused on its ability to suppress the aggregation of misfolded proteins and suppressing cellular death in models of neurodegenerative disease and proteotoxicity, the role of DNAJB6 in neurons under normal conditions or in models in which cell death is not due to misfolded proteins has not been explored. This is the focus of my dissertation. This dissertation is divided into the following three chapters: Chapter 1 of this dissertation reviews the regulated pathways in which neurons undergo programmed cell death. This chapter will discuss the role of proteinopathic stress in a number of neurodegenerative diseases and the progression of neurodegeneration in patients of these diseases. This will be followed by a discussion on the common proteolytic and protein chaperone mechanisms through which cells degrade and refold damaged and misfolded proteins. Lastly, I describe recent research into DNAJB6 and its identification as a potent suppressor of the aggregation of misfolded proteins and proteinopathic stress, as well as recent research into its role in cell signaling pathways. In Chapter 2, I will describe how DNAJB6 promotes neuronal apoptosis under non-proteotoxic stress conditions in neurons and that DNAJB6 is required for the progression of apoptosis in neurons. These conclusions are supported by experiments using shRNA knockdown and overexpression of DNAJB6. We show that DNAJB6-induced apoptosis is caused by activation of cyclin-dependent kinases and aberrant re-entry into the cell cycle. As the induction of HSP expression is viewed as a potential strategy for the treatment of neurodegenerative disease, our results suggest that this strategy may not be without dangers. In Chapter 3, I summarize and discuss the mechanisms through which DNAJB6 induces apoptosis. I describe how my research provides insight into the role of DNAJB6 in neurons in normal conditions as well as in proteotoxic stress.
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| Total Pages | : |
| Release | : 2005 |
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Heat shock proteins (HSP) improve cellular thermotolerance and protect against stress-induced cell death by reducing micro level damage and mediating apoptotic pathways. HSP72 levels increase in response to nonlethal heat stress in vitro, and occur due a variety of physiological stressful conditions, including heat exposure and exercise, in vivo. Multiple days of exercise in the heat lead to a heat acclimated state of improved whole-body thermotolerance, which is thought to be related to an accumulation of HSP72. Increased HSP72 expression has been shown to decrease apoptosis in vitro; however, the relationship between physiological adaptations to heat acclimation and the subsequent adaptations at the cellular level are less understood. The purpose of this study was to examine if heat acclimation (HA) increases HSP72 and if its protective mechanisms decrease apoptosis in lymphocytes. Twelve recreationally active males completed 8 consecutive days of cycling in 38°C for ~90 min at ~45% VO2max. Lymphocytes were isolated from whole blood pre- and post-exercise on days 1 and 8 of HA. The pre-exercise lymphocytes were heat shocked in vitro for 20, 40, or 60 min at 37, 41, 43, or 45°C to analyze apoptotic responses to heat, and post-exercise samples were analyzed to determine apoptotic responses to exercise. After HA, participants exhibited significantly improved thermotolerance. They experienced a resting plasma volume expansion of 6.29"6.18%, enhanced sweat loss (F=20.479, p=0.001), and decreased heart rate, core temperature, and skin temperature at all time points during the heat tolerance test following HA (F=2.968, p=0.046; F=3.634, p=0.023; and F=6.642, p=0.002, respectively). HSP72-mRNA increased during exercise on days 1 and 8 (4.08"1.09 and 3.80"0.50 fold, respectively), and resting HSP72-mRNA levels increased 2.11"0.35 fold from days 1 to 8. There was no change in in vitro apoptosis due to HA (F=0.820, p=0.385); however, there was an interaction of the time x te.
| Author | : Alexzander A.A. Asea |
| Publisher | : Springer Science & Business Media |
| Total Pages | : 374 |
| Release | : 2008-04-06 |
| Genre | : Medical |
| ISBN | : 1402082312 |
With the prevalence of neurodegenerative diseases on the rise as average life expectancy increases, the hunt for effective treatments and preventive measures for these disorders is a pressing challenge. Neurodegenerative disorders such as Alzheimer’s disease, Huntington’s disease, Parkinson’s disease and amyotrophic lateral sclerosis have been termed ‘protein misfolding disorders’ that are char- terized by the neural accumulation of protein aggregates. Manipulation of the cellular stress response involving the induction of heat shock proteins offers a the- peutic strategy to counter conformational changes in neural proteins that trigger pathogenic cascades resulting in neurodegenerative diseases. Heat shock proteins are protein repair agents that provide a line of defense against misfolded, aggregati- prone proteins. Heat Shock Proteins and the Brain: Implications for Neurodegenerative Diseases and Neuroprotection reviews current progress on neural heat shock proteins (HSP) in relation to neurodegenerative diseases (Part I), neuroprotection (Part II), ext- cellular HSP (Part III) and aging and control of life span (Part IV). Key basic and clinical research laboratories from major universities and hospitals around the world contribute chapters that review present research activity and importantly project the field into the future. The book is a must read for researchers, postdoctoral fellows and graduate students in the fields of Neuroscience, Neurodegenerative Diseases, Molecular Medicine, Aging, Physiology, Pharmacology and Pathology.
| Author | : Matthias Gaestel |
| Publisher | : Springer Science & Business Media |
| Total Pages | : 464 |
| Release | : 2005-09-27 |
| Genre | : Science |
| ISBN | : 9783540258759 |
Molecular chaperones are involved in a wide variety of essential cellular processes in living cells. A subset of molecular chaperones have been initially described as heat shock proteins protecting cells from stress damage by keeping cellular proteins in a folding competent state and preventing them from irreversible aggregation. Later it became obvious that molecular chaperones are also expressed constitutively in the cell and are involved in complex processes such as protein synthesis, intracellular protein transport, post-translational modification and secretion of proteins as well as receptor signalling. Hence, it is not surprising that molecular chaperones are implicated in the pathogenesis of many relevant diseases and could be regarded as potential pharmacological targets. Starting with the analysis of the mode of action of chaperones at the molecular, cellular and organismic level, this book will then describe specific aspects where modulation of chaperone action could be of pharmacological and therapeutic interest.
| Author | : Stuart K. Calderwood |
| Publisher | : Springer Science & Business Media |
| Total Pages | : 399 |
| Release | : 2007-09-09 |
| Genre | : Medical |
| ISBN | : 1402064012 |
Heat shock proteins are emerging as important molecules in the development of cancer and as key targets in cancer therapy. These proteins enhance the growth of cancer cells and protect tumors from treatments such as drugs or surgery. However, new drugs have recently been developed particularly those targeting heat shock protein 90. As heat shock protein 90 functions to stabilize many of the oncogenes and growth promoting proteins in cancer cells, such drugs have broad specificity in many types of cancer cell and offer the possibility of evading the development of resistance through point mutation or use of compensatory pathways. Heat shock proteins have a further property that makes them tempting targets in cancer immunotherapy. These proteins have the ability to induce an inflammatory response when released in tumors and to carry tumor antigens to antigen presenting cells. They have thus become important components of anticancer vaccines. Overall, heat shock proteins are important new targets in molecular cancer therapy and can be approached in a number of contrasting approaches to therapy.
| Author | : Society for Neuroscience. Meeting |
| Publisher | : |
| Total Pages | : 1474 |
| Release | : 2000 |
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| Author | : |
| Publisher | : |
| Total Pages | : 1840 |
| Release | : 2000 |
| Genre | : Medicine |
| ISBN | : |
| Author | : Rosa Barrio |
| Publisher | : Springer Nature |
| Total Pages | : 350 |
| Release | : 2020-04-09 |
| Genre | : Science |
| ISBN | : 3030382664 |
This book, written by members of the European network PROTEOSTASIS, provides an up-to-date review of the research regarding protein homeostasis in health and disease. With new discoveries contributing to the increasing complexity of this topic, the book offers a detailed overview of the pathways regulating protein homeostasis, including autophagy and the ubiquitin protein family. Following a basic introduction, it explains how defects in protein homeostasis contribute to numerous pathologies, including cancer, neurodegeneration, inflammation and a number of rare diseases. In addition, it discusses, the role of protein homeostasis in cellular development and physiology. Highlighting the latest research in the field of protein homeostasis and its implications for various clinically relevant diseases, the book appeals to researchers and clinicians, while also offering a reference guide for scholars who are new to the field.
