Cellular Trafficking of Cell Stress Proteins in Health and Disease

1. Front Matter

   Pages 1-1

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2. Discovery of the Cellular Secretion of Cell Stress Proteins

   • Lawrence E. Hightower, Emily J. Noonan

   Pages 1-11

3. Discovery of the Extracellular Agonist Actions of Molecular Chaperones and Protein-Folding Catalysts

   • Brian Henderson

   Pages 13-27

4. Molecular Chaperones and Protein-Folding Catalysts in Biological Fluids

   • A. Graham Pockley

   Pages 29-42

5. Hsp27 Phosphorylation Patterns and Cellular Consequences

   • Ugo Moens, Sergiy Kostenko

   Pages 43-74

6. Evidence on Cholesterol-Controlled Lipid Raft Interaction of the Small Heat Shock Protein HSPB11

   • Zsolt Török, Ana-Maria Pilbat, Imre Gombos, Enikö Hocsák, Balázs Sümegi, Ibolya Horváth et al.

   Pages 75-85

7. Hsp70 Chaperone Systems in Vesicular Trafficking

   • J. Paul Chapple, David A. Parfitt, Daniel C. Campbell

   Pages 87-101

8. Pathways of Hsp70 Release: Lessons from Cytokine Secretion

   • Stuart K Calderwood, Ayesha Murshid

   Pages 103-113

9. Nucleolin: A Novel Intracellular Transporter of HSPA1A

   • Alexzander Asea, Appukuttan R. Pradeep, Punit Kaur

   Pages 115-124

10. The Hsp90-Based Protein Trafficking System and Linkage to Protein Quality Control

    • Yoichi Osawa, William B. Pratt, Yoshihiro Morishima, Andrew P. Lieberman

    Pages 125-150

11. Cell Surface Molecular Chaperones and the LPS Receptor

    • Martha Triantafilou, Kathy Triantafilou

    Pages 151-165

12. Chaperonin 60: An Unexpected Cell Surface Receptor in Prokaryotes and Eukaryotes

    • Brian Henderson

    Pages 167-183

13. Pathophysiological Barriers Impeding the Delivery of Heat Shock Protein (HSP)-Based Macromolecules and Nanotherapeutics to Solid Tumors

    • Peter Vaupel, Gabriele Multhoff

    Pages 185-199

14. The Chaperokine Activity of HSPA1A

    • Alexzander Asea, Punit Kaur

    Pages 201-213

15. Molecular Chaperones and Scavenger Receptors: Binding and Trafficking of Molecular Chaperones by Class F and Class H Scavenger Receptors

    • Ayesha Murshid, Jianlin Gong, Stuart K. Calderwood

    Pages 215-227

16. GRP78 (BiP): A Multifunctional Cell Surface Receptor

    • Mario Gonzalez-Gronow, Salvatore V. Pizzo, Uma K. Misra

    Pages 229-242

17. Mycobacterium tuberculosis Hsp60 as a Key Virulence Factor in Tuberculosis

    • Richard W. Stokes

    Pages 243-258

18. Heat Shock Protein 90 Versus Conventional Growth Factors in Acute and Diabetic Wound Healing

    • Wei Li, Kathryn O’Brien, David T. Woodley, Mei Chen

    Pages 259-277

19. Circulating Chaperones in Health and Disease

    • Zoltán Prohászka

    Pages 279-290

20. Back Matter

    Pages 281-281

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Since the beginning of the 21st Century there has been a rapid increase in our understanding of the cellular trafficking mechanisms of molecular chaperones in eukaryotes and in prokaryotes. In the former, molecular chaperone trafficking can occur between the various cellular compartments, with concomitant movement of other proteins. Such events can also result in the release of molecular chaperones from cells. In bacteria, molecular chaperones are involved in the trafficking of other proteins and are themselves released into the external milieu. The increasing appreciation of the role of molecular chaperones and Protein-Folding Catalysts in the interplay between bacteria and the cells of their hosts is now an important area of research for understanding the mechanisms of infectious diseases. This volume brings together experts in the biochemistry, cellular biology, immunology and molecular biology of molecular chaperones and Protein-Folding Catalysts with a focus on the mechanisms of cellular trafficking of these proteins and the role of these variegated trafficking mechanisms in both human and animal health and disease.

• Heat Shock Proteins
• Intracellular Trafficking
• Physiology
• Stress Responses

• Eastman Dental Institute, Div. Microbial Diseases, University College, London, London, United Kingdom

  Brian Henderson

• School of Medicine & Biomedical Science, University of Sheffield, Sheffield, United Kingdom

  A. Graham Pockley

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