A Novel Mechanism of Androgen Receptor Action
Abstract
This revised project has as its goal the characterization of a novel alternative product of the Her-2/neu/erbB2 protooncogene derived from intron retention. The product of this splicing mechanism termed herstatin is a secreted protein comprised of the N terminus of the Her-2 receptor tyrosine kinase and a unique intron-encoded C terminus that allows binding to the other members of the EGFR/erbB family. This binding down-regulates erbB expression and inhibits EGF family signaling and cell proliferation. We have found that herstatin also binds to and down-regulates the IGF-I receptor (IGF-IR) and modulates IGF signal transduction. Herstatin is therefore a novel bifunctional inhibitor of erbB and IGF-IR signaling. Herstatin is expressed in prostate tissue and may represent a promising therapeutic target and biomarker in CaP. The work proposed in this project will assess the effect of herstatin on CaP cell phenotype the expression of herstatin in CaP samples and potential mechanisms of regulation of herstatin expression.
Document Details
- Document Type
- Technical Report
- Publication Date
- Jan 01, 2008
- Accession Number
- ADA482241
Entities
People
- Charles T. Roberts Jr.
Organizations
- Oregon Health & Science University