The cancer chemopreventive agent resveratrol induces tensin, a cell-matrix adhesion protein with signaling and antitumor activities
| Autor: | Paul-Henri Romeo, Marc Bracke, Christelle M Rodrigue, Erik Bruyneel, Françoise Porteu, Nicole Navarro, Christian Gespach, Marie-Claude Garel |
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| Rok vydání: | 2005 |
| Předmět: |
Cancer Research
Cytoplasm Time Factors endocrine system diseases Phosphatidylinositol 3-Kinases Cell-matrix adhesion Cell Movement Neoplasms Tensins Stilbenes Tensin Cycloheximide Enzyme Inhibitors Cytoskeleton Protein Synthesis Inhibitors biology Reverse Transcriptase Polymerase Chain Reaction Microfilament Proteins Vinculin Flow Cytometry Cell biology Gene Expression Regulation Neoplastic Biochemistry biological phenomena cell phenomena and immunity hormones hormone substitutes and hormone antagonists Signal Transduction DNA Complementary Integrin Immunoblotting macromolecular substances Focal adhesion Cell Line Tumor Genetics Cell Adhesion Anticarcinogenic Agents Humans Neoplasm Invasiveness RNA Messenger Cell adhesion neoplasms Molecular Biology Dose-Response Relationship Drug Antineoplastic Agents Phytogenic Actins Fibronectin Resveratrol Cancer cell biology.protein K562 Cells Cell Adhesion Molecules |
| Zdroj: | Oncogene. 24(20) |
| ISSN: | 0950-9232 |
| Popis: | During a search to identify resveratrol (3,5,4'-trihydroxy-trans-stilbene, RV) target genes in the human erythroleukemic K562 cell line, we show here that the tensin gene and protein levels are remarkably induced by this dietary polyphenol. Tensin, a cell-matrix adhesion protein binding the integrins and cytoskeletal actin filaments also interacts with PI3-kinase and JNK signaling pathways. Tensin induction by RV is associated with increased K562 cell adhesion to fibronectin, cell spreading and actin polymerization. The same responses were observed in the tensin-deficient MCF7 human breast cancer cell line. In K562 and MCF7 cells treated by RV, tensin was found in punctate and intracytoplasmic areas. In MCF7 epithelial cells, induction of tensin is not exclusively associated with plasma membrane-bound vinculin, suggesting a dual localization of tensin in both focal and fibrillar adhesions. Pharmacological blockade of PI3-kinase and Rho GTPases/Rho-kinase resulted in selective depletion of focal adhesions, disorganization of tensin localization and disruption of stress fibers. RV increased cell motility and attachment to fibronectin in MCF7 cells submitted to mechanical laminar flow stress, and abrogated estrogen-induced MCF7 cancer cell invasion. Our data support the conclusion that induction of tensin by RV contributes to the chemopreventive and anti-invasive activity of this natural dietary compound in tensin-negative and -deficient leukemic cells or epithelioid cancers. |
| Databáze: | OpenAIRE |
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