Periostin secreted by epithelial ovarian carcinoma is a ligand for αVβ3 and αVβ5 integrins and promotes cell motility

Lindsay Gillan, Daniela Matei, David A. Fishman, C. S. Gerbin, Beth Y. Karlan, David D. Chang

Research output: Contribution to journalArticlepeer-review

456 Scopus citations


Periostin (PN) is a secreted protein that shares a structural homology to the axon guidance protein fasciclin I in insects. Previously, we reported that PN expression is up-regulated in epithelial ovarian tumors. We further examined the role of PN in ovarian cancer. PN is expressed in several normal tissues but not in normal ovaries and has a tendency for higher expression in fetal tissues. Ovarian cancer cells secrete PN, which can accumulate in malignant ascites of ovarian cancer patients. Purified recombinant PN supports adhesion of ovarian epithelial cells that can be inhibited by monoclonal antibodies against αvβ3 or αvβ5 integrin, but not by anti-β1 integrin antibody. Furthermore, αvβ3 integrin, but not β1 integrins, colocalizes to the focal adhesion plaques formed on PN. Cells plated on PN form fewer stress fibers and are more motile compared with those plated on fibronectin. We propose PN functions as a ligand for αvβ3 and αvβ5 integrins to support adhesion and migration of ovarian epithelial cells.

Original languageEnglish (US)
Pages (from-to)5358-5364
Number of pages7
JournalCancer Research
Issue number18
StatePublished - Sep 15 2002

ASJC Scopus subject areas

  • Oncology
  • Cancer Research


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