Abstract | BACKGROUND:
Membrane proteins provide the interface between the cell and its environment and are responsible for cell adhesion, mobility, and intracellular signaling. Previous studies have focused on the LNCaP whole cell proteome and transcriptome but little is known about proteins at the prostate cell membrane and how they change in response to androgens. MATERIALS AND METHODS: RESULTS: We have demonstrated efficient and specific protein biotinylation and purification of LNCaP plasma membrane proteins using Western analysis. E-cadherin and LDLR were regulated at the cell surface in response to R1881 and bicalutamide. Mass spectrometry identified several androgen-regulated membrane associated proteins including Prx-3 and GRP78 which are known to localize to other cellular compartments as well as the plasma membrane. We confirmed the localization of the identified proteins in LNCaP cells by co-localization with E-cadherin and immunohistochemistry of prostate tissue. CONCLUSION:
|
Authors | Hayley C Whitaker, David P B Stanbury, Claire Brinham, Joanne Girling, Sarah Hanrahan, Nick Totty, David E Neal |
Journal | The Prostate
(Prostate)
Vol. 67
Issue 9
Pg. 943-54
(Jun 15 2007)
ISSN: 0270-4137 [Print] United States |
PMID | 17440980
(Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
|
Chemical References |
- Androgens
- Endoplasmic Reticulum Chaperone BiP
- HSPA5 protein, human
- Membrane Proteins
- Neoplasm Proteins
- Metribolone
|
Topics |
- Androgens
(pharmacology)
- Biotinylation
- Cell Line, Tumor
- Electrophoresis, Gel, Two-Dimensional
- Endoplasmic Reticulum Chaperone BiP
- Humans
- Male
- Membrane Proteins
(isolation & purification, metabolism)
- Metribolone
(pharmacology)
- Neoplasm Proteins
(isolation & purification, metabolism)
- Pilot Projects
- Prostatic Neoplasms
(pathology)
|