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Syndecan-2 cytoplasmic domain regulates colon cancer cell migration via interaction with syntenin-1
- Title
- Syndecan-2 cytoplasmic domain regulates colon cancer cell migration via interaction with syntenin-1
- Authors
- Lee H.; Kim Y.; Choi Y.; Choi S.; Hong E.; Oh E.-S.
- Ewha Authors
- 오억수
- SCOPUS Author ID
- 오억수
- Issue Date
- 2011
- Journal Title
- Biochemical and Biophysical Research Communications
- ISSN
- 0006-291X
- Citation
- Biochemical and Biophysical Research Communications vol. 409, no. 1, pp. 148 - 153
- Indexed
- SCIE; SCOPUS
- Document Type
- Article
- Abstract
- The cell surface heparan sulfate proteoglycan, syndecan-2, is crucial for the tumorigenic activity of colon cancer cells. However, the role played by the cytoplasmic domain of the protein remains unclear. Using colon cancer cells transfected with various syndecan-2-encoding genes with deletions in the cytoplasmic domain, it was shown that syndecan-2-induced migration activity requires the EFYA sequence of the C-terminal region; deletion of these residues abolished the rise in cell migration seen when the wild-type gene was transfected and syndecan-2 interaction with syntenin-1, suggesting that syntenin-1 functioned as a cytosolic signal effector downstream from syndecan-2. Colon cancer cells transfected with the syntenin-1 gene showed increased migratory activity, whereas migration was decreased in cells in which syntenin-1 was knock-down using small inhibitory RNA. In addition, syntenin-1 expression potentiated colon cancer cell migration induced by syndecan-2, and syndecan-2-mediated cell migration was reduced when syntenin-1 expression diminished. However, syntenin-1-mediated migration enhancement was not noted in colon cancer cells transfected with a gene encoding a syndecan-2 mutant lacking the cytoplasmic domain. Furthermore, in line with the increase in cell migration, syntenin-1 mediated Rac activation stimulated by syndecan-2. Together, the data suggest that the cytoplasmic domain of syndecan-2 regulates colon cancer cell migration via interaction with syntenin-1. © 2011 Elsevier Inc.
- DOI
- 10.1016/j.bbrc.2011.04.135
- Appears in Collections:
- 자연과학대학 > 생명과학전공 > Journal papers
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