E-cadherin-mediated survival of androgen-receptor-expressing secretory prostate epithelial cells derived from a stratified in vitro differentiation model

2010 ◽  
Vol 123 (2) ◽  
pp. 266-276 ◽  
Author(s):  
L. E. Lamb ◽  
B. S. Knudsen ◽  
C. K. Miranti
2006 ◽  
Vol 175 (4S) ◽  
pp. 144-144
Author(s):  
Xu-Bao Shi ◽  
Lingru Xue ◽  
Clifford G. Tepper ◽  
Ralph W. deVere White

2007 ◽  
Vol 67 (9) ◽  
pp. 4364-4372 ◽  
Author(s):  
Mathew Casimiro ◽  
Olga Rodriguez ◽  
Llana Pootrakul ◽  
Maral Aventian ◽  
Nadia Lushina ◽  
...  

2008 ◽  
Vol 99 (4) ◽  
pp. 671-676 ◽  
Author(s):  
Hiroshi Fukamachi ◽  
Ayako Mimata ◽  
Issei Tanaka ◽  
Kosei Ito ◽  
Yoshiaki Ito ◽  
...  

2001 ◽  
Vol 29 (4) ◽  
pp. 287-292 ◽  
Author(s):  
Diane Krill ◽  
Angela Thomas ◽  
Su-Ping Wu ◽  
Rajiv Dhir ◽  
Michael J. Becich

2004 ◽  
Vol 15 (1) ◽  
pp. 397-406 ◽  
Author(s):  
Sanita Bharti ◽  
Heike Handrow-Metzmacher ◽  
Silvia Zickenheiner ◽  
Andreas Zeitvogel ◽  
Rudolf Baumann ◽  
...  

While searching for potential candidate molecules relevant for the pathogenesis of endometriosis, we discovered a 2910-base pair cDNA encoding a novel putative 411-amino acid integral membrane protein that we called shrew-1. The putative open-reading frame was confirmed with antibodies against shrew-1 peptides that labeled a protein of ∼48 kDa in extracts of shrew-1 mRNA-positive tissue and also detected ectopically expressed shrew-1. Expression of epitope-tagged shrew-1 in epithelial cells and analysis by surface biotinylation and immunoblots demonstrated that shrew-1 is indeed a transmembrane protein. Shrew-1 is able to target to E-cadherin-mediated adherens junctions and interact with the E-cadherin–catenin complex in polarized MCF7 and Madin-Darby canine kidney cells, but not with the N-cadherin–catenin complex in nonpolarized epithelial cells. Direct interaction of shrew-1 with β-catenin in in vitro pull-down assay suggests that β-catenin might be one of the proteins that targets and/or retains shrew-1 in the adherens junctions. Interestingly, shrew-1 was partially translocated in response to scatter factor (ligand of receptor tyrosine kinase c-met) from the plasma membrane to the cytoplasm where it still colocalized with endogenous E-cadherin. In summary, we introduce shrew-1 as a novel component of adherens junctions, interacting with E-cadherin–β-catenin complexes in polarized epithelial cells.


2013 ◽  
Vol 20 (2) ◽  
pp. R49-R64 ◽  
Author(s):  
Natalie Sampson ◽  
Hannes Neuwirt ◽  
Martin Puhr ◽  
Helmut Klocker ◽  
Iris E Eder

Prostate cancer (PCa) is one of the most common causes of male cancer-related death in Western nations. The cellular response to androgens is mediated via the androgen receptor (AR), a ligand-inducible transcription factor whose dysregulation plays a key role during PCa development and progression following androgen deprivation therapy, the current mainstay systemic treatment for advanced PCa. Thus, a better understanding of AR signaling and new strategies to abrogate AR activity are essential for improved therapeutic intervention. Consequently, a large number of experimental cell culture models have been established to facilitate in vitro investigations into the role of AR signaling in PCa development and progression. These different model systems mimic distinct stages of this heterogeneous disease and exhibit differences with respect to AR expression/status and androgen responsiveness. Technological advances have facilitated the development of in vitro systems that more closely reflect the physiological setting, for example via the use of three-dimensional coculture to study the interaction of prostate epithelial cells with the stroma, endothelium, immune system and tissue matrix environment. This review provides an overview of the most commonly used in vitro cell models currently available to study AR signaling with particular focus on their use in addressing key questions relating to the development and progression of PCa. It is hoped that the continued development of in vitro models will provide more biologically relevant platforms for mechanistic studies, drug discovery and design ensuring a more rapid transfer of knowledge from the laboratory to the clinic.


Oncogene ◽  
2002 ◽  
Vol 21 (31) ◽  
pp. 4747-4756 ◽  
Author(s):  
Marion Kubista ◽  
Margit Rosner ◽  
Ernst Kubista ◽  
Gerhard Bernaschek ◽  
Markus Hengstschläger

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