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Biochem. Biophys. Res. Commun. · Aug 2004
Ligation of EphA2 by Ephrin A1-Fc inhibits pancreatic adenocarcinoma cellular invasiveness.
- Mark S Duxbury, Hiromichi Ito, Michael J Zinner, Stanley W Ashley, and Edward E Whang.
- Department of Surgery, Brigham and Women's Hospital, Harvard Medical School, Boston, MA 02115, USA. duxbury@doctors.org.uk
- Biochem. Biophys. Res. Commun. 2004 Aug 6; 320 (4): 1096-102.
AbstractThe Eph tyrosine kinases interact with ligands of the Ephrin family and have diverse cellular functions. EphA2 has been recognized to be an oncoprotein of importance in a range of cancers. Here, we examine the effect of EphA2 overexpression and ligation by chimeric Ephrin A1-Fc on the invasive phenotype of pancreatic adenocarcinoma cells. We show that EphA2 overexpression induces a FAK-dependent increase in MMP-2 expression and invasiveness. EphA2 ligation induces proteosomal degradation of EphA2, attenuates the invasive phenotype, and decreases both FAK phosphorylation and MMP-2 expression. EphA2 appears to represent a rational therapeutic target and ligation by Ephrin A1-Fc is one strategy to modulate levels of this oncoprotein.
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