Molecular Cloning and Function of Fas/APO-1 Associated Protein in Breast Cancer.
Abstract
Fas/APO-1 is a cell surface receptor that controls a poorly understood signal transduction pathway leading to cell death via apoptosis. A protein tyrosine phosphatase, FAP-1 (Fas/APO-1 associated phosphatase), capable of interacting with the cytosolic domain of Fas, was isolated by yeast two hybrid system. The carboxy terminal 15 amino acids of Fas are necessary and sufficient for interaction with FAP-1. PAP-i expression is highest in tissues and cell lines (including MCF7 breast cancer cell line) that are relatively resistant to Fas-mediated cytotoxicity. Gene transfer- mediated;elevations in FAP-1 partially abolished Fas-induced apoptosis in a T-cell line. These findings are consistent with an inhibitory effect of FAP- 1 on Fas-signal transduction.
Document Details
- Document Type
- Technical Report
- Publication Date
- Jun 05, 1995
- Accession Number
- ADA297181
Entities
People
- John Reed
- Takaaki Sato
Organizations
- Sanford Burnham Prebys Medical Discovery Institute