Peroxisomal Oxidation in Normal and Tumoral Human Breast.
Abstract
The peroxisomal enzyme catalase protects aerobic organisms from free radical damage by converting hydrogen peroxide (H2O2) to molecular oxygen and water before it can decompose to form the highly reactive hydroxyl radical. In this manner catalase plays a central role in protecting against cellular oxidative damage. In humans, changes in catalase activity have been implicated in aging and in a number of disease states including cancer. We hypothesized that reduced catalase could potentially lead to an excess of H2O2 produced by peroxisomal oxidative reactions, which may then leak into the cell and cause DNA damage. To test this hypothesis we are examining the levels of catalase and peroxisomal fatty acyl-CoA oxidase in a variety of human breast samples and in breast cancer cell lines and in normal tissue and non immortalized cells in culture. Catalase and acyl-CoA oxidase activities were extremely low in the human breast tumor samples therefore we have established conditions for using the polymerase chain reaction to quantitate the expression of the genes encoding peroxisomal catalase and acyl-CoA oxidase in a variety of breast cancer cell lines and in normal breast epithelial cells.
Document Details
- Document Type
- Technical Report
- Publication Date
- Oct 01, 1997
- Accession Number
- ADA337865
Entities
People
- Gillian Small
Organizations
- Icahn School of Medicine at Mount Sinai