C76 HEAT SHOCK PROTEIN: Hsf1 Activation Regulates The Transcriptional Activity Of The Heat Shock And Unfolded Protein Responses Altering Myeloid Proteostasis And Driving Granulopoeisis

Proteostasis refers to the dynamic process by which cells control the concentration, conformation, binding interactions and stability of individual proteins of the proteome through a system of regulated networks of interacting and competing biological pathways which influence protein synthesis, fold...

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Bibliographic Details
Published in:American journal of respiratory and critical care medicine 2017-01, Vol.195
Main Authors: Gates, K L, Homan, P J, Lu, Z, Misharin, A V, Chandel, N S, Balch, W, Morimoto, R I, Sznajder, J I, Budinger, G S
Format: Article
Language:English
Subjects:
Bone marrow
Gene expression
Granulocytes
Heat shock proteins
Rodents
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Summary:Proteostasis refers to the dynamic process by which cells control the concentration, conformation, binding interactions and stability of individual proteins of the proteome through a system of regulated networks of interacting and competing biological pathways which influence protein synthesis, folding, trafficking, disaggregation, and degradation The heat shock (HSR) and the uncoupled protein response (UPR) are critical pathways whose signaling influences the cellular proteostatic network to maintain cellular homeostasis during stress. In celastrol-treated mice, there was a reduction in mature granulocytes in the bone marrow with no change in granulocyte myeloid progenitors (GMPs) despite an observed increase in granulocytes in the lung tissue.
ISSN:1073-449X
1535-4970