About this Medicine article
Activation of rat hepatic stellate cells leads to loss of glutathionS-transferases and their enzymatic activity against products of oxidative stress by Richard Whalen; Don C. Rockey; Scott L. Friedman; Thomas D. Boyer is a Medicine article available to read on EtoBox.
Oxidative stress, mediated partly by lipid peroxidation products, may lead to increased collagen synthesis by hepatic stellate cells (HSC). Stellate cells are protected from oxidative stress by enzymes of detoxication such as the glutathione S-transferases (GSTs), which form glutathione conjugates with lipid peroxidation products (e.g., 4-hydroxy-2-nonenal [HNE]). To better understand the role of GSTs in stellate cell biology, we examined the expression and enzymatic activity of GSTs in normal and activated (both culture-and in vivo-activated) stellate cells. Normal stellate cells contained numerous isoforms of GST including those that detoxify HNE. High levels of enzymatic activity toward 1-chloro-2,4-dinitrobenzene (CDNB) and HNE were present in normal stellate cells and were similar to levels present in whole liver. Following activation by growth in culture, the expression of several GSTs (rGSTA1/A2, A3, and M1) was lost. Also, enzymatic activities toward CDNB and HNE fell ϳ90%. However, expression of rGSTP1 was maintained. A similar loss of rGSTA1/A2, A3, and M1 with persistent expression of rGSTP1 was present after activation in vivo. Furthermore, we identified 2 subpopulation
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- Author
- Richard Whalen; Don C. Rockey; Scott L. Friedman; Thomas D. Boyer
- Publisher
- Ovid Technologies (Wolters Kluwer Health)
- Published
- 1999
- Language
- EN
- Field
- Medicine (Health Sciences)