Epidermal growth factor increased the expression of alpha2beta1-integrin and modulated integrin-mediated signaling in human cervical adenocarcinoma cells
| Autor: | Satoko Yamashita, Ikuhito Yamanaka, Takahiro Suzuki, Motoiki Koizumi, Tsuyoshi Baba, Ryuichi Kudo |
|---|---|
| Rok vydání: | 2003 |
| Předmět: |
Collagen Type IV
Integrin Motility Uterine Cervical Neoplasms Adenocarcinoma Cell morphology Antibodies Epidermal growth factor Cell Movement Tumor Cells Cultured Humans Pseudopodia Enzyme Inhibitors Phosphorylation Cell Size biology Epidermal Growth Factor Cell migration Cell Biology Protein-Tyrosine Kinases Cell biology Fibronectins Fibronectin ErbB Receptors Focal Adhesion Kinase 1 Focal Adhesion Protein-Tyrosine Kinases Cancer research biology.protein Tyrosine Female Lamellipodium Integrin alpha2beta1 hormones hormone substitutes and hormone antagonists Signal Transduction |
| Zdroj: | Experimental cell research. 286(2) |
| ISSN: | 0014-4827 |
| Popis: | Epidermal growth factor (EGF) receptor (EGFR) is involved in various basic biochemical pathways and is thus thought to play an important role in cell migration. We examined the effect of EGF on motility, migration, and morphology of a human adenocarcinoma cell line CAC-1. EGF treatment increased the motility of cervical adenocarcinoma cells and promoted migration of the cells on fibronectin and type IV collagen. EGF induced morphological changes with lamellipodia during EGFR-mediated motility. The results of an immunoprecipitation study showed that EGF up-regulated the expression of alpha2beta1-integrin in a dose-dependent manner. EGF-induced cell migration was blocked by alpha2beta1-integrin antibody. Our results also showed that EGF treatment stimulated the level of tyrosine dephosphorylation of FAK, which is required for EGF-induced changes in motility, migration, and cell morphology. A tyrosine kinase inhibitor (ZD1839) blocked EGF-induced changes in cervical adenocarcinoma cells. The results suggest that EGF promotes cell motility and migration and increases the expression of alpha2beta1-integrin, possibly by decreasing FAK phosphorylation. |
| Databáze: | OpenAIRE |
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