Cell Stress Proteins

1. Auflage 2009
ISBN: 978-0-387-39717-7
Verlag: Springer-Verlag
Format: PDF
Kopierschutz: Adobe DRM (»Systemvoraussetzungen)

E-Book, Englisch, 460 Seiten

Stressproteinssuchastheheatshockproteins(Hsp)andglucose-regulatedproteins (Grp) are front-line molecules in responses to cellular insult and play key roles in the viability of single cell organisms exposed to environmental stresses. However, the discovery of the roles of Hsp and Grp as molecular chaperones indicates much wider functions in the physiology of cells and organisms. It is now clear that some stress proteins are expressed constitutively and are key mediators of housekeeping protein folding in the day-to-day existence of the cell. The maturation of enzymes, transcriptionfactors,andcellsurfacereceptorsreliesonthesefunctionsofthestress proteins. In addition, the ability of stress proteins to manipulate the structures of target proteins has lent them cell regulatory properties over and above their role in folding the proteome and they play key roles in controlling signal transduction, cell death pathways and transcription. Recently, novel extracellular roles for the Hsp have also emerged as it has become apparent that the Hsp can escape from the cytoplasm of cells and play a signi?cant extracellular role in signaling to neighbor cells and in immunosurveiIlance. As might be expected with such key molecules, dysregulation of Hsp expression over time can lead to disastrous results in terms of the health of the organism. Under-expression of the Hsp is associated with advanced aging and neurodegeneration. Elevated expression is associated with malignant progression. We have aimed in this volume to indicate advances in each oftheseaspectsofstressproteinresearch,withchaptersrangingfrombasicstudies of the role of Hsp in protein folding to reviews examining the breakdown of stress protein regulation in disease. Stuart K.

Autoren/Hrsg.

Inhaltsverzeichnis

1;Cell Stress Proteins;3
2;Contents;6
3;Foreword;9
4;Acknowledgement;10
5;List of Contributors;11
6;Introduction: Heat Shock Proteins— From Drosophila Stress Proteins to Mediators of Human Disease;14
7;Stress Response and Molecular Chaperones;18
7.1;Biology of the Heat Shock Response and Stress Conditioning;19
7.2;Bacterial Stress Sensors;48
7.3;Unfolded Protein Response: Contributions to Development and Disease;69
8;Molecular Mechanisms of Stress Protein Expression;101
8.1;Genetic Models of HSF Function;102
8.2;HSF1 and HSP Gene Regulation;133
9;Cellular Stress Proteins;151
9.1;Small Heat Shock Proteins in Physiological and Stress- Related Processes;152
9.2;Large Mammalian hsp70 Family Proteins, hsp110 and grp170, and Their Roles in Biology and Cancer Therapy;187
10;Molecular Chaperones and Protein Folding;215
10.1;Regulation of Hsp70 Function: Hsp40 Co- Chaperones and Nucleotide Exchange Factors;216
10.2;Protein Disassembly by Hsp40–Hsp70;235
10.3;Mammalian HSP40/DnaJ Chaperone Proteins in Cytosol;262
11;Role of Molecular Chaperones in Cell Regulation;285
11.1;FKBP Co-Chaperones in Steroid Receptor Complexes;286
11.2;Up and Down;318
11.3;Role of Cdc37 in Protein Kinase Folding;331
12;Intracellular and Extracellular Stress Proteins in Human Disease;343
12.1;Targeting Hsp90 in Cancer and Neurodegenerative Disease;344
12.2;gp96 and Tumor Immunity;367
12.3;Immunoregulatory Activities of Extracellular Stress Proteins;380
12.4;Heat Shock Proteins and Neurodegenerative Diseases;399
12.5;Heat Shock Proteins in the Progression of Cancer;425
13;Index;454
14;Color Plate I;463
15;Color Plate II;464