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dc.contributor.authorMonette, Margaret Mariscal
dc.date.accessioned2014-03-04T18:29:04Z
dc.date.available2014-03-04T18:29:04Z
dc.date.issued2010-05
dc.identifier.othermonette_margaret_m_201005_ms
dc.identifier.urihttp://purl.galileo.usg.edu/uga_etd/monette_margaret_m_201005_ms
dc.identifier.urihttp://hdl.handle.net/10724/26429
dc.description.abstractThe nature and mechanism of action of host-derived molecules termed alarmins or damage-associated molecular patterns (DAMPs) in the inflammatory response remains elusive. The hypothesis in this work states that a soluble histone H1x-like protein, NCAMP-1 functions as an endogenous danger molecule in zebrafish. NCAMP-1 was present in the cytoplasm of different cell types and tissues and was released from immune cells. To identify pathways utilized by NCAMP-1 in cellular binding and activation, its effects were compared to those of ATP, known to act through the ligand-gated ion channel, P2X7 receptor. Binding of either agonist to zebrafish leukocytes initiated intracellular calcium mobilization, pore formation and increased cytotoxic killing. While some of the effects between the two agonists are similar, significant differences in their mechanisms of action were found. Therefore, NCAMP-1 may utilize a unique mechanism of cellular binding and activation in its role as a multi-functional effector molecule and inflammatory mediator.
dc.languageeng
dc.publisheruga
dc.rightspublic
dc.subjectalarmins
dc.subjectzebrafish
dc.subjectATP
dc.subjectP2X7 receptor
dc.subjectcalcium mobilization
dc.subjectcytotoxic killing
dc.subjectinflammatory mediator
dc.titleNCAMP-1
dc.title.alternativea novel class of danger molecules in teleosts
dc.typeThesis
dc.description.degreeMS
dc.description.departmentInfectious Diseases
dc.description.majorVeterinary and Biomedical Sciences
dc.description.advisorLiliana Jaso-Friedmann
dc.description.committeeLiliana Jaso-Friedmann
dc.description.committeeThomas Krunkosky
dc.description.committeeDonald Evans


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