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Heat Shock Proteins and Cytoprotection

Author : Alexander E. Kabakov
Publisher : Springer Science & Business Media
Page : 244 pages
File Size : 35,7 MB
Release : 2012-12-06
Category : Science
ISBN : 1461560071

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Heat Shock Proteins in Cancer

Author : Stuart K. Calderwood
Publisher : Springer Science & Business Media
Page : 399 pages
File Size : 13,32 MB
Release : 2007-09-09
Category : Medical
ISBN : 1402064012

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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.

Heat Shock Proteins in Myocardial Protection

Author : Rakesh C. Kukreja
Publisher : CRC Press
Page : 145 pages
File Size : 17,46 MB
Release : 2000-08-01
Category : Science
ISBN : 1498712665

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Myocardial ischemic syndromes pose a major medical problem and a significant economic health care concern. Reperfusion, although used in the clinical arena as essential to the survival of acutely ischemic heart muscle carries with it the risk of reperfusion injury. Therefore the salvage of additional myocardium is highly desirable.

Heat Shock Proteins and Plants

Author : Alexzander A. A. Asea
Publisher : Springer
Page : 341 pages
File Size : 22,28 MB
Release : 2016-11-23
Category : Science
ISBN : 3319463403

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Heat Shock Proteins and Plants provides the most up-to-date and concise reviews and progress on the role of heat shock proteins in plant biology, structure and function and is subdivided into chapters focused on Small Plant HSPs (Part I), Larger Plant HSPs (Part II) and HSPs for Therapeutic Gain (Part III). This book is written by eminent leaders and experts from around the world and is an important reference book and a must-read for undergraduate, postgraduate students and researchers in the fields of Agriculture, Botany, Crop Research, Plant Genetics and Biochemistry, Biotechnology, Drug Development and Pharmaceutical Sciences.

The Role of Heat Shock Proteins in Reproductive System Development and Function

Author : Daniel J. MacPhee
Publisher : Springer
Page : 155 pages
File Size : 23,30 MB
Release : 2017-04-13
Category : Science
ISBN : 9783319514086

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Due to the paucity of reviews on this subject, this volume aims to be timely and promote additional basic and translational research on these proteins in reproductive system development and function within the fields of Anatomy, Embryology and Cell Biology. The breadth of the work being conducted within Reproduction is exemplified by the contributors to this series who will provide reviews on: Grp78 roles in female reproduction, small heat shock proteins/co-chaperones as players in uterine smooth muscle function, the role of heat shock proteins in sperm function and maternal contribution to oogenesis and early embryogenesis, heat shock factors and testes development, HSP90 in ovarian biology and pathology, and the role of HSP70 in regulation of autophagy in pregnancy and parturition.

Contribution of Heat Shock Protein 27 and Retinol Binding Protein to 11-Deoxy-16, 16-Dimethyl Prostaglandin E2 Mediated Cytoprotection

Author : Jean Lanette Lord-Garcia
Publisher :
Page : 440 pages
File Size : 30,23 MB
Release : 2008
Category :
ISBN :

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11-Deoxy-16,16-dimethyl prostaglandin E2 (DDM-PGE2) protects renal proximal tubular epithelial cells (LLC-PK1) against oncotic cell death induced by 2,3,5-tris(glutathione-S-yl)hydroquinone (TGHQ). Cytoprotection is associated with the up-regulation of several proteins including actin, heat shock protein 27 (Hsp27) and retinol binding protein (RBP). This dissertation reveals the induction and phosphorylation of Hsp27 by TGHQ treatment and DDM-PGE2 pretreatment. Treatment with TGHQ results in a dose-dependent disruption of the actin cytoskeleton that correlates with a decrease in cell viability, increased generation of reactive oxygen species, and the induction of Hsp27 nuclear translocation and co-localization with actin. Moreover, DDM-PGE2 pretreatment, but not co-treatment, prevents both TGHQ generation of ROS and actin cytoskeletal damage. DDM-PGE2 results in the enhanced induction and phosphorylation of nuclear Hsp27 that likely contributes to the inhibition of early effects of TGHQ induced ROS generation on the actin cytoskeleton. In correlation, we identify site specific phosphorylation of Hsp27 (p-Hsp27) at human Ser82 that negatively regulates cell survival, and p-Hsp27 at Ser15 associated with cell survival. We provide evidence that the TP receptor dependent increase in RBP expression is based on the ability of DDM-PGE2 to recruit the retinoid signalingpathway through activation of the RAR/RXR nuclear receptor heterodimers. All-trans retinoic acid (AtRA) pretreatment recapitulates the protective effects of DDM-PGE2 through a mechanism independent of TP receptor activation and the cytoprotective effects of AtRA were also investigated using an in vivo model. Finally, the ability of DDM-PGE2 to increase the cells antioxidant response, important in its cytoprotection against ROS is described. Taken together, these studies contribute to the mechanism of protection and will give insight into the affects of novel therapeutics in the modulation of chemical induced nephrotoxicity.

Regulation of Heat Shock Protein Responses

Author : Alexzander A A Asea
Publisher : Springer
Page : 471 pages
File Size : 11,91 MB
Release : 2018-05-01
Category : Medical
ISBN : 3319747150

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This books provides the most up-to-date reviews on current advances in our understanding of the regulation of heat shock protein responses. Key basic scientists and clinical research laboratories from major universities, academic medical centers and pharmaceutical companies around the world have contributed chapters that review present research activity and importantly project this field into the future. For easy readability, the book is sub divided into four sections, including, Section I - HSP and Stress Responses; Section II - Chaperone Functions of HSP; Section III - HSP in Human Diseases; Section IV - Prognosis & Diagnosis of HSP. The book is a must read for researchers involved in biomedical research, drug discovery and design to improve human health.

Signal Transduction in Cancer

Author : David A. Frank
Publisher : Springer Science & Business Media
Page : 358 pages
File Size : 18,21 MB
Release : 2002-12-31
Category : Medical
ISBN : 1402073402

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One of the most exciting areas of cancer research now is the development of agents which can target signal transduction pathways that are activated inappropriately in malignant cells. The understanding of the molecular abnormalities which distinguish malignant cells from their normal counterparts has grown tremendously. This volume summarizes the current research on the role that signal transduction pathways play in the pathogenesis of cancer and how this knowledge may be used to develop the next generation of more effective and less toxic anticancer agents. Series Editor comments: "The biologic behavior of both normal and cancer cells is determined by critical signal transduction pathways. This text provides a comprehensive review of the field. Leading investigators discuss key molecules that may prove to be important diagnostic and/or therapeutic targets."

Deciphering a Potential Cytoprotective Role of Novel Heat Shock Responsive Proteins Using a Proteomic Approach

Author : Charlene Patricia Kimar
Publisher :
Page : 192 pages
File Size : 15,98 MB
Release : 2012
Category : Heart cells
ISBN :

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period of 24 hours and cell viability was assessed by the MTT assay. Two dimensional proteomic analysis was carried out to compare the proteomes of H9c2 and H9c2 cells that over-express RhoE. This research demonstrates that both RhoE and TIP4I are induced in response to heat stress and that the over-expression of RhoE is able to protect H9c2 against camptothecin induced cell death. Furthermore a proteomic 2D analysis demonstrates differential protein expression between H9c2 cells and H9c2 that over-express RhoE. Proteomic analysis demonstrates that the over-expression of RhoE leads to the down-regulation of Rho-GDI a. It can be concluded from this study that the expression of RhoE in response to heat shock is a cytoprotcctive event. The mechanism of cytoprotection is likely to involve Rho-GDI a.

The Big Book on Small Heat Shock Proteins

Author : Robert M. Tanguay
Publisher : Springer
Page : 603 pages
File Size : 40,9 MB
Release : 2015-06-15
Category : Medical
ISBN : 331916077X

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Based upon a workshop entitled “The Small HSP World” held in Québec 2-5 October 2014. Twenty-five scientists provided chapters for the book. The chapters are from the best scientists currently working in this field. These colleagues include Arrigo, Benesch, Benjamin, Buchner-Haslbeck-Weinkauf, Benndorf, Boelens, Carra, Chang, Currie, Ecroyd, Emanuelsson, Fu, Garrido, Golenhofen, Gusev, Hightower, Kampinga, Lavoie, MacRae, Quinlan, Tanguay, Vierling, Vigh, Weeks and Wu. Briefly, the book starts with the structure of small heat shock proteins, moving to their functions and finishing with their involvement in diseases. Although this is quite broad, the structural aspect will be the unifying theme of the book.