Characterization of A-type ephrin signaling

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dc.contributor.authorBazowski, Jessa
dc.contributor.supervisorHoward, Perry
dc.date.accessioned2007-08-31T23:17:31Z
dc.date.available2007-08-31T23:17:31Z
dc.date.copyright2007en_US
dc.date.issued2007-08-31T23:17:31Z
dc.degree.departmentDept. of Biologyen_US
dc.degree.levelMaster of Science M.Sc.en_US
dc.description.abstractMembrane attachment of ephrin ligands plays an important role in Eph receptor activation. Membrane anchorage is thought to provide a clustering effect to ephrins that is necessary for stimulation of Eph receptor kinase activity. The presence of soluble A-type ephrin in conditioned media of numerous cultured cancer cell lines and normal endothelial cells prompted me to question the purpose of ephrin release. In this thesis I show that ephrin A1, a potent angiogenic factor, is released from several cancer cell lines and is a substrate for tissue transglutaminase, a multifunctional enzyme with the ability to form covalent crosslinks between substrate proteins. I show that tissue transglutaminase crosslinking primes soluble ephrin A1 to promote Eph A2 activity. These results suggest a role for soluble A-type ephrins in promoting Eph receptor activity at distant sites and also indicate that ephrin A1 may be acting as a soluble angiogenic factor during tumor neovascularization.en_US
dc.identifier.bibliographicCitationAlford, S.C., Bazowski, J., Lorimer, H., Elowe, S., and Howard, P. Tissue Transglutaminase clusters soluble A-type ephrins into active high molecular weight oligomers. Exp. Cell Res. In Press.en_US
dc.identifier.urihttp://hdl.handle.net/1828/223
dc.languageEnglisheng
dc.language.isoenen_US
dc.rightsAvailable to the World Wide Weben_US
dc.subjectephrinen_US
dc.subjecttransglutaminaseen_US
dc.subjectEphen_US
dc.subjectoligomerizationen_US
dc.subjectclusteringen_US
dc.subject.lcshUVic Subject Index::Sciences and Engineering::Biologyen_US
dc.titleCharacterization of A-type ephrin signalingen_US
dc.typeThesisen_US

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