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dc.contributor.authorMacKenzie, Louise Susan
dc.contributor.authorLymn, Joanne
dc.contributor.authorHughes, Alun D.
dc.date.accessioned2013-12-04T10:30:01Z
dc.date.available2013-12-04T10:30:01Z
dc.date.issued2013-12
dc.identifier.citationMacKenzie , L S , Lymn , J & Hughes , A D 2013 , ' Linking Phospholipase C isoforms with differentiation function in human vascular smooth muscle cells ' , BBA - Molecular Cell Research , vol. 1833 , no. 12 , pp. 3006-3012 . https://doi.org/10.1016/j.bbamcr.2013.08.005
dc.identifier.urihttp://hdl.handle.net/2299/12263
dc.descriptionThis is an open-access article distributed under the terms of the Creative Commons Attribution-NonCommercial-No Derivative Works License, which permits non-commercial use, distribution, and reproduction in any medium, provided the original author and source are credited.
dc.description.abstractThe phosphoinositol phospholipase C (PLC) family of enzymes consists of a number of isoforms, each of which has different cellular functions. PLCγ1 is primarily linked to tyrosine kinase transduction pathways, whereas PLCδ1 has been associated with a number of regulatory proteins, including those controlling the cell cycle. Recent studies have shown a central role of PLC in cell organization and regulating a wide array of cellular responses. It is of importance to define the precise role of each isoform, and how this changes the functional outcome of the cell. Here we investigated differences in PLC isoform levels and activity in relation to differentiation of human and rat vascular smooth muscle cells. Using Western blotting and PLC activity assay, we show that that PLCδ1 and PLCγ1 are the predominant isoforms in randomly cycling human vascular smooth muscle cells (HVSMCs). Growth arrest of HVSMCs by seven days of serum deprivation was consistently associated with increases in PLCδ1 and SM α-actin, whereas there were no changes in PLCγ1 immuno-reactivity. Organ culture of rat mesenteric arteries in serum free media (SFM), a model of de-differentiation, led to a loss of contractility as well as a loss of contractile proteins (SM α-actin and calponin) and PLCδ1, and no change in PLCγ1 immuno-reactivity. Taken together, these data indicates that PLCδ1 is the predominant PLC isoform in vascular smooth muscle, and confirm that PLCδ1 expression is affected by conditions that affect the cell cycle, differentiation status and contractile function.en
dc.format.extent1101227
dc.language.isoeng
dc.relation.ispartofBBA - Molecular Cell Research
dc.titleLinking Phospholipase C isoforms with differentiation function in human vascular smooth muscle cellsen
dc.contributor.institutionSchool of Life and Medical Sciences
dc.contributor.institutionHealth & Human Sciences Research Institute
dc.contributor.institutionDepartment of Human and Environmental Sciences
dc.contributor.institutionPharmacology and Clinical Science Research
dc.contributor.institutionAgriculture, Food and Veterinary Sciences
dc.contributor.institutionCardiovascular Pathologies
dc.contributor.institutionDiabetic neuropathies
dc.description.statusPeer reviewed
rioxxterms.versionofrecord10.1016/j.bbamcr.2013.08.005
rioxxterms.typeJournal Article/Review
herts.preservation.rarelyaccessedtrue


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