Accession Number:

ADA364684

Title:

Peroxisomal Oxidation in Normal and Tumoral Human Breast.

Descriptive Note:

Final rept. 13 Sep 96-13 Sep 98

Corporate Author:

MOUNT SINAI SCHOOL OF MEDICINE NEW YORK

Personal Author(s):

Report Date:

1998-10-01

Pagination or Media Count:

15.0

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 have examined the mRNA 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. In addition, we previously found that the human Peroxisome Proliferator-Activated Receptor hPPAR, a transcription factor involved in the regulation of peroxisomal beta-oxidation enzymes, is highly expressed in human mammary tissue. Therefore we also compared the levels of hPPAR with those of catalase and acyl-CoA oxidase. Using the polymerase chain reaction to quantitate the expression of the genes encoding each of these proteins, we found that the levels were similar in the human breast tumor samples and in normal controls, with the exception that we were unable to detect hPPAR in an estrogen receptor positive carcinoma cell line.

Subject Categories:

  • Biochemistry
  • Medicine and Medical Research

Distribution Statement:

APPROVED FOR PUBLIC RELEASE