Cell Stress Proteins

Portada
Stuart K. Calderwood
Springer Science & Business Media, 13 feb. 2009 - 460 páginas
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.
 

Comentarios de usuarios - Escribir una reseña

No hemos encontrado ninguna reseña en los sitios habituales.

Índice

Introduction Heat Shock ProteinsFrom Drosophila Stress Proteins to Mediators of Human Disease
2
Stress Response and Molecular Chaperones
6
Biology of the Heat Shock Response and Stress Conditioning
7
Bacterial Stress Sensors
36
Unfolded Protein Response Contributions to Development and Disease
57
Molecular Mechanisms of Stress Protein Expression
90
Genetic Models of HSF Function
91
HSF1 and HSP Gene Regulation
122
Mammalian HSP40DnaJ Chaperone Proteins in Cytosol
255
Role of Molecular Chaperones in Cell Regulation
280
FKBP CoChaperones in Steroid Receptor Complexes
281
Up and Down Regulation of the Stress Response by the CoChaperone Ubiquitin Ligase CHIP
313
Role of Cdc37 in Protein Kinase Folding
326
Intracellular and Extracellular Stress Proteins in Human Disease
340
Targeting Hsp90 in Cancer and Neurodegenerative Disease
341
gp96 and Tumor Immunity A Simple Matter of CrossPresentation Antigens?
364

Cellular Stress Proteins
142
Small Heat Shock Proteins in Physiological and StressRelated Processes
143
Large Mammalian hsp70 Family Proteins hsp110 and grp170 and Their Roles in Biology and Cancer Therapy
178
Molecular Chaperones and Protein Folding
208
Regulation of Hsp70 Function Hsp40 CoChaperones and Nucleotide Exchange Factors
209
Protein Disassembly by Hsp40Hsp70
228
Immunoregulatory Activities of Extracellular Stress Proteins
377
Heat Shock Proteins and Neurodegenerative Diseases
396
Heat Shock Proteins in the Progression of Cancer
422
Index
451
Página de créditos

Otras ediciones - Ver todo

Términos y frases comunes

Información bibliográfica