Focal Adhesion Kinase Activated by β4 Integrin Ligation to mCLCA1 Mediates Early Metastatic Growth*
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Summary
It is shown that lung colonization by B16-F10 cells is licensed by β4 integrin adhesion to the mouse lung endothelial Ca2+-activated chloride channel protein mCLCA1, which is associated with FAK complexing, activation, and signaling to promote early, intravascular, metastatic growth.
- Type
- article
- Published
- 2002-09-13
- Cited by
- 121
- References
- 44
- Access
- Open access
- OpenAlex
- https://openalex.org/W2094395747
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:19294016
Keywords
Focal adhesion, Integrin, Ligation, Cancer research, Adhesion
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Cited by
- The Putative Chloride Channel hCLCA2 Has a Single C-terminal Transmembrane Segment*
- FAK expression regulation and therapeutic potential.
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- The Molecular Function Of Mclca1, Mclca2 And Mclca4 In Murine Life
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- Roles of Ion Transport in Control of Cell Motility
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- The molecular and cellular impact of wave interactions on the aggressiveness of PC-3 cells
- Tumour exosome integrins determine organotropic metastasis
- A FAK scaffold inhibitor disrupts FAK and VEGFR-3 signaling and blocks melanoma growth by targeting both tumor and endothelial cells
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