title: EMMPRIN regulates cytoskeleton reorganization and cell adhesion in prostate cancer.
abstract: BACKGROUND
  Proteins on cell surface play important roles during cancer progression and metastasis via their ability to mediate cell-to-cell interactions and navigate the communication between cells and the microenvironment.
  
  
  METHODS
  In this study a targeted proteomic analysis was conducted to identify the differential expression of cell surface proteins in human benign (BPH-1) versus malignant (LNCaP and PC-3) prostate epithelial cells. We identified EMMPRIN (extracellular matrix metalloproteinase inducer) as a key candidate and shRNA functional approaches were subsequently applied to determine the role of EMMPRIN in prostate cancer cell adhesion, migration, invasion as well as cytoskeleton organization.
  
  
  RESULTS
  EMMPRIN was found to be highly expressed on the surface of prostate cancer cells compared to BPH-1 cells, consistent with a correlation between elevated EMMPRIN and metastasis found in other tumors. No significant changes in cell proliferation, cell cycle progression, or apoptosis were detected in EMMPRIN knockdown cells compared to the scramble controls. Furthermore, EMMPRIN silencing markedly decreased the ability of PC-3 cells to form filopodia, a critical feature of invasive behavior, while it increased expression of cell-cell adhesion and gap junction proteins.
  
  
  CONCLUSIONS
  Our results suggest that EMMPRIN regulates cell adhesion, invasion, and cytoskeleton reorganization in prostate cancer cells. This study identifies a new function for EMMPRIN as a contributor to prostate cancer cell-cell communication and cytoskeleton changes towards metastatic spread, and suggests its potential value as a marker of prostate cancer progression to metastasis.
authors.affiliation: Department of Molecular and Cellular Biochemistry, College of Medicine, University of Kentucky, Lexington, Kentucky, USA.
authors.forename: Haining
authors.initials: H
authors.lastname: Zhu
authors.forename: Jun
authors.initials: J
authors.lastname: Zhao
authors.forename: Beibei
authors.initials: B
authors.lastname: Zhu
authors.forename: Joanne
authors.initials: J
authors.lastname: Collazo
authors.forename: Jozsef
authors.initials: J
authors.lastname: Gal
authors.forename: Ping
authors.initials: P
authors.lastname: Shi
authors.forename: Li
authors.initials: L
authors.lastname: Liu
authors.forename: Anna-Lena
authors.initials: AL
authors.lastname: Ström
authors.forename: Xiaoning
authors.initials: X
authors.lastname: Lu
authors.forename: Richard O
authors.initials: RO
authors.lastname: McCann
authors.forename: Michal
authors.initials: M
authors.lastname: Toborek
authors.forename: Natasha
authors.initials: N
authors.lastname: Kyprianou
mesh_terms: D000230:Adenocarcinoma / Q000235:genetics / Q000378:metabolism* / Q000473:pathology; D051926:Basigin / Q000235:genetics / Q000378:metabolism*; D002448:Cell Adhesion / Q000235:genetics / Q000502:physiology*; D045744:Cell Line, Tumor; D002462:Cell Membrane / Q000235:genetics / Q000378:metabolism / Q000473:pathology; D003599:Cytoskeleton / Q000235:genetics / Q000378:metabolism* / Q000473:pathology; D018450:Disease Progression; D006801:Humans; D008297:Male; D009361:Neoplasm Invasiveness / Q000235:genetics / Q000473:pathology; D011467:Prostate / Q000378:metabolism* / Q000473:pathology; D011471:Prostatic Neoplasms / Q000235:genetics / Q000378:metabolism* / Q000473:pathology; D014407:Tumor Cells, Cultured
chemical_list: D051926:Basigin