Soluble ephrin a1 is necessary for the growth of HeLa and SK-BR3 cells |
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| Authors: | Spencer Alford Adam Watson-Hurthig Nadia Scott Amanda Carette Heather Lorimer Jessa Bazowski Perry L Howard |
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| Affiliation: | (1) Department of Chemistry, University of Alberta, 11227 Saskatchewan Drive, Edmonton, Alberta, T6G 2G2, Canada;(2) Department of Biochemistry and Microbiology, University of Victoria, P.O. Box 3055, Station CSC Victoria, British Columbia, V8W 3P6, Canada;(3) Department of Biology, University of Victoria, P.O. Box 3020, Station CSC Victoria, British Columbia, V8W 3N5, Canada;(4) Centre for Biomedical Research, University of Victoria, P.O. Box 3020, Station CSC Victoria, British Columbia, V8W 3N5, Canada |
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| Abstract: | Background Ephrin A1 (EFNA1) is a member of the A-type ephrin family of cell surface proteins that function as ligands for the A-type Eph receptor tyrosine kinase family. In malignancy, the precise role of EFNA1 and its preferred receptor, EPHA2, is controversial. Several studies have found that EFNA1 may suppress EPHA2-mediated oncogenesis, or enhance it, depending on cell type and context. However, little is known about the conditions that influence whether EFNA1 promotes or suppresses tumorigenicity. EFNA1 exists in a soluble form as well as a glycophosphatidylinositol (GPI) membrane attached form. We investigated whether the contradictory roles of EFNA1 in malignancy might in part be related to the existence of both soluble and membrane attached forms of EFNA1 and potential differences in the manner in which they interact with EPHA2. |
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