Hsp70, a messenger from hyperthermia for the immune system
| Autor: | Rolf D. Issels, Elfriede Noessner, Katharina Elmer, Henriette Bendz, Anna Jolesch |
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| Rok vydání: | 2010 |
| Předmět: |
CD4-Positive T-Lymphocytes
Protein Folding Histology Hot Temperature Fever Cell Gene Expression Biology Protein aggregation CD8-Positive T-Lymphocytes Lymphocyte Activation Pathology and Forensic Medicine Interferon-gamma Mice Necrosis Immune system Cross-Priming Heat shock protein Neoplasms medicine Tumor Microenvironment Animals Humans HSP70 Heat-Shock Proteins Cell Biology General Medicine Dendritic Cells Immunity Innate Cell biology Hsp70 Interleukin-10 Killer Cells Natural Interleukin 10 medicine.anatomical_structure Immune System Protein folding Interleukin-5 Intracellular Signal Transduction |
| Zdroj: | European journal of cell biology. 91(1) |
| ISSN: | 1618-1298 |
| Popis: | Heat shock proteins (Hsps) hold a dual role depending on their location. Inside cells, they fulfill essential survival functions as molecular chaperones forming complexes with intracellular polypeptides (self or foreign) to help in protein folding, the resolution of protein aggregates and intracellular protein transport. Released from the cell, they act as messengers communicating the cells’ interior protein composition to the immune system for initiation of immune responses against intracellular proteins. Here we describe the mechanisms by which Hsp70, the heat-inducible Hsp70 family member, crosstalks with the immune system. Further, we discuss that clinical hyperthermia could be a way to initiate the immunologic activity of Hsp70 by upregulating its expression and facilitating release through local necrosis. |
| Databáze: | OpenAIRE |
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