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dc.contributor.authorDave, R.
dc.contributor.authorHume, D.
dc.contributor.authorElsegood, Caryn
dc.contributor.authorKellie, S.
dc.date.accessioned2017-01-30T12:33:51Z
dc.date.available2017-01-30T12:33:51Z
dc.date.created2016-09-12T08:36:25Z
dc.date.issued2009
dc.identifier.citationDave, R. and Hume, D. and Elsegood, C. and Kellie, S. 2009. CD148/DEP-1 association with areas of cytoskeletal organisation in macrophages. Experimental Cell Research. 315 (10): pp. 1734-1744.
dc.identifier.urihttp://hdl.handle.net/20.500.11937/22836
dc.identifier.doi10.1016/j.yexcr.2009.02.023
dc.description.abstract

In macrophages, tyrosine phosphorylation regulates many signalling pathways leading to growth, differentiation, activation, phagocytosis and adhesion. Protein tyrosine phosphatases (PTPs) represent a biochemical counterbalance to the activity of protein tyrosine kinases, thus regulating the dynamic phosphorylation state of a cell. CD148 is a receptor PTP that is highly expressed in macrophages and is further regulated by pro-inflammatory stimuli. CD148 is normally localised to the plasma membrane of macrophages. Following stimulation with CSF-1 or LPS, there was a re-distribution and concentration of CD148 in areas of membrane ruffling. Treatment of macrophages with anti-CD148 monoclonal antibody inhibited CSF-1-induced macrophage spreading, cytoskeletal re-arrangements and chemotaxis, without affecting cell survival. There were no detectable effects on the CSF-1 receptor-akt signalling pathway. These results are consistent with the hypothesis that CD148 is a regulator of macrophage activity. © 2009 Elsevier Inc. All rights reserved.

dc.publisherAcademic Press
dc.titleCD148/DEP-1 association with areas of cytoskeletal organisation in macrophages
dc.typeJournal Article
dcterms.source.volume315
dcterms.source.number10
dcterms.source.startPage1734
dcterms.source.endPage1744
dcterms.source.issn0014-4827
dcterms.source.titleExperimental Cell Research
curtin.departmentSchool of Biomedical Sciences
curtin.accessStatusFulltext not available


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