Endoplasmic Reticulum (ER) Based Chaperones and Protein Disulfide Isomerases in Lung Diseases
The endoplasmic reticulum (ER) is an active tubular network involved in protein folding, gluconeogenesis, lipid synthesis, mitochondrial fission and calcium storage. Cellular events that demand an increase in protein folding will create an imbalance in protein folding enzymes and will increase unfolded proteins in the ER, eliciting a response called the Unfolded Protein Response (UPR). The UPR initially shuts down selective protein synthesis and activates transcription factors such as ATF6, ATF4 and Xbp-1 that promote synthesis of chaperones (e.g. GRP94 and GRP78), protein disulfide isomerases (PDIs, e.g. ERp57, ERp5, ERp72) to correctly fold the unfolded proteins.
We have found that the UPR is activated by various agents (allergens, viruses and biological ligands) in the structural and immune cells of the lung. Currently we are characterizing the functional or pathological role of UPR in 1) allergen-induced lung inflammation and airway fibrotic remodeling, 2) influenza virus protein folding and propagation and 3) during the differentiation of T helper cells into various subsets (e.g. Th1, Th2 and Th17).
Our laboratory utilizes various systems (cell culture, human samples and transgenic mouse) and techniques (microscopy, molecular, biochemical and forced oscillation) to investigate how UPR contributes to the development of inflammation, fibrosis or propagation of influenza virus and ultimately to the pathophysiology of the lung.
Department of Pathology
Office: HSRF 216
Lab: HSRF 223
- 1/13/2015 11:30 AM – 12:30 PM
- 1/20/2015 11:30 AM – 12:30 PM
- 1/27/2015 11:30 AM – 12:30 PM
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