Abstract | BACKGROUND: METHODS: RESULTS: CONCLUSIONS: Unfolding of Type III domains within the fibronectin matrix may promote TRAIL resistance through the activation of a PI3K/Akt/αvβ5 signaling axis and point to a novel mechanism by which changes in secondary structure of fibronectin contribute to cancer cell resistance to apoptosis.
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Authors | Christina Cho, Carol Horzempa, David Jones, Paula J McKeown-Longo |
Journal | BMC cancer
(BMC Cancer)
Vol. 16
Pg. 574
(08 02 2016)
ISSN: 1471-2407 [Electronic] England |
PMID | 27484721
(Publication Type: Journal Article, Research Support, U.S. Gov't, Non-P.H.S., Research Support, N.I.H., Extramural)
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Chemical References |
- Fibronectins
- Receptors, Vitronectin
- TNF-Related Apoptosis-Inducing Ligand
- Vitronectin
- integrin alphaVbeta5
- Phosphatidylinositol 3-Kinases
- Proto-Oncogene Proteins c-akt
- CASP8 protein, human
- Caspase 8
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Topics |
- Carcinoma, Non-Small-Cell Lung
(metabolism)
- Caspase 8
(metabolism)
- Cell Line, Tumor
- Cell Survival
(drug effects)
- Drug Resistance, Neoplasm
- Fibronectin Type III Domain
- Fibronectins
(chemistry, pharmacology)
- Gene Expression Regulation, Neoplastic
(drug effects)
- Humans
- Lung Neoplasms
(metabolism)
- Phosphatidylinositol 3-Kinases
(metabolism)
- Protein Folding
- Proto-Oncogene Proteins c-akt
(metabolism)
- Receptors, Vitronectin
(metabolism)
- Signal Transduction
- TNF-Related Apoptosis-Inducing Ligand
(pharmacology)
- Vitronectin
(metabolism)
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