Title |
Heat shock protein 70 down-regulates the production of toll-like receptor-induced pro-inflammatory cytokines by a heat shock factor-1/constitutive heat shock element-binding factor-dependent mechanism
|
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Published in |
Journal of Inflammation, July 2014
|
DOI | 10.1186/1476-9255-11-19 |
Pubmed ID | |
Authors |
Eduardo Ferat-Osorio, Aldair Sánchez-Anaya, Mireille Gutiérrez-Mendoza, Ilka Boscó-Gárate, Isabel Wong-Baeza, Rodolfo Pastelin-Palacios, Gustavo Pedraza-Alva, Laura C Bonifaz, Pedro Cortés-Reynosa, Eduardo Pérez-Salazar, Lourdes Arriaga-Pizano, Constantino López-Macías, Yvonne Rosenstein, Armando Isibasi |
Abstract |
Heat shock protein 70 (Hsp70) is an intracellular chaperone protein with regulatory and cytoprotective functions. Hsp70 can also be found in the extracellular milieu, as a result of active secretion or passive release from damaged cells. The role of extracellular Hsp70 is not fully understood. Some studies report that it activates monocytes, macrophages and dendritic cells through innate immune receptors (such as Toll-like receptors, TLRs), while others report that Hsp70 is a negative regulator of the inflammatory response. In order to address this apparent inconsistency, in this study we evaluated the response of human monocytes to a highly purified recombinant Hsp70. |
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