Elucidating the structure and function of S100 proteins in membranes

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dc.contributor.author Valenzuela, SM
dc.contributor.author Berkahn, M
dc.contributor.author Martin, DK
dc.contributor.author Huynh, T
dc.contributor.author Yang, Z
dc.contributor.author Geczy, CL
dc.date.accessioned 2010-07-13T08:50:41Z
dc.date.issued 2006
dc.identifier.citation Progress in Biomedical Optics and Imaging - Proceedings of SPIE, 2006, 6036
dc.identifier.issn 1605-7422
dc.identifier.other E1 en_US
dc.identifier.uri http://hdl.handle.net/10453/12683
dc.description.abstract S100 proteins are important Ca2+-binding proteins involved in vital cellular functions including the modulation of cell growth, migration and differentiation, regulation of intracellular signal transduction/ phosphorylation pathways, energy metabolism, cytoskeletal interactions and modulation of ion channels. Furthermore, they are implicated in oncogenesis and numerous other disease states. Three S100 proteins: S100A8, S100A9 and S100A12 are constitutively expressed in neutrophils and monocytes. At low levels of intracellular Ca2+, S100A8 and S100A9 are located predominantly in the cytosol but when Ca2+ concentrations are elevated as a consequence of activation, they translocate to membranes and complex with cytoskeletal components such as vimentin. The functions of S100A8 and S100A9 at the plasma membrane remain unclear. A possible role may be the regulation of ion channel proteins. The current study uses the techniques of Atomic Force Microscopy and production of artificial lipid membranes in the form of liposomes to investigate possible mechanisms for the insertion of these proteins into membranes in order to elucidate their structure and stoichiometry in the transmembrane state. We have successfully imaged the liposomes as a lipid bilayer, the S100A8/A9 protein complex in solution and the S100A8/A9 complex associating with lipid, using tapping-mode atomic force microscopy, in buffer.
dc.relation.isversionof en_US
dc.relation.isbasedon 10.1117/12.638873
dc.title Elucidating the structure and function of S100 proteins in membranes
dc.type Conference Proceeding
dc.parent Progress in Biomedical Optics and Imaging - Proceedings of SPIE
dc.journal.volume 6036
dc.journal.number en_US
dc.publocation Bellingham, USA en_US
dc.identifier.startpage 3619 en_US
dc.identifier.endpage 3619 en_US
dc.cauo.name SCI.Medical and Molecular Biosciences en_US
dc.conference Verified OK en_US
dc.conference Conference on BioMEMS and Nanotechnology II
dc.for 1007 Nanotechnology
dc.personcode 960727
dc.personcode 970908
dc.personcode 010690
dc.percentage 100 en_US
dc.classification.name Materials Engineering en_US
dc.classification.type FOR-08 en_US
dc.edition en_US
dc.custom Conference on BioMEMS and Nanotechnology II en_US
dc.date.activity 20051212 en_US
dc.date.activity 2005-12-12
dc.location.activity Brisbane, AUSTRALIA en_US
dc.description.keywords Atomic force microscopy
dc.description.keywords Liposomes
dc.description.keywords S100 proteins
pubs.embargo.period Not known
pubs.organisational-group /University of Technology Sydney
pubs.organisational-group /University of Technology Sydney/Faculty of Science
pubs.organisational-group /University of Technology Sydney/Faculty of Science/School of Medical and Molecular Sciences
pubs.organisational-group /University of Technology Sydney/Strength - Health Technologies
utslib.copyright.status Open Access
utslib.copyright.date 2015-04-15 12:23:47.074767+10
pubs.consider-herdc true
utslib.collection.history General (ID: 2)
utslib.collection.history School of Medical and Molecular Sciences (ID: 341)

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