In Vivo Suppression of Heat Shock Protein (HSP)27 and HSP70 Accelerates DMBA-Induced Skin Carcinogenesis by Inducing Antigenic Unresponsiveness to the Initiating Carcinogenic Chemical-Reference-Cited by-同舟云学术

In Vivo Suppression of Heat Shock Protein (HSP)27 and HSP70 Accelerates DMBA-Induced Skin Carcinogenesis by Inducing Antigenic Unresponsiveness to the Initiating Carcinogenic Chemical

Published:2015-04-03 Issue:10 Volume:194 Page:4796-4803
ISSN:0022-1767
Container-title:The Journal of Immunology
language:en
Short-container-title:J.I.

Author:

Yusuf Nabiha,Nasti Tahseen H.,Ahmad Israr,Chowdhury Sanim,Mohiuddin Hasan,Xu Hui,Athar Mohammad,Timares Laura,Elmets Craig A.

Publisher

The American Association of Immunologists

Subject

Immunology,Immunology and Allergy

Reference51 articles.

1. Pathways of chaperone-mediated protein folding in the cytosol

2. Interaction of Heat Shock Proteins with Peptides and Antigen Presenting Cells: Chaperoning of the Innate and Adaptive Immune Responses

3. Necrotic but not apoptotic cell death releases heat shock proteins, which deliver a partial maturation signal to dendritic cells and activate the NF-κB pathway

4. Consequences of Cell Death

5. HSP70 stimulates cytokine production through a CD14-dependant pathway, demonstrating its dual role as a chaperone and cytokine

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