{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,20]],"date-time":"2026-05-20T21:06:39Z","timestamp":1779311199179,"version":"3.51.4"},"reference-count":61,"publisher":"The Company of Biologists","issue":"23","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2002,12,1]]},"abstract":"<jats:p>Cytosolic phospholipase A2-\u03b1 (cPLA2-\u03b1) is a calcium-sensitive enzyme involved in receptor-mediated eicosanoid production. In resting cells, cPLA2-\u03b1 is present in the cytosol and nucleus and translocates to membranes via its calcium-dependent lipid-binding (CaLB) domain following stimulation. cPLA2-\u03b1 is also regulated by phosphorylation on several residues, which results in enhanced arachidonic acid release. Little is known about the factors controlling the nuclear localisation of cPLA2-\u03b1. Here the nuclear localisation of cPLA2-\u03b1 in the EA.hy.926 human endothelial cell line was investigated. Nuclear localisation was dependent on proliferation, with subconfluent cells containing higher levels of nuclear cPLA2-\u03b1 than contact-inhibited confluent or serum-starved cells. The broad-range protein kinase inhibitor staurosporine caused a decrease in the nuclear level of cPLA2-\u03b1, whereas the protein phosphatase inhibitor okadaic acid increased the level of nuclear cPLA2-\u03b1. Using inhibitors for specific mitogen-activated protein (MAP) kinases, both p42\/44MAPK and p38MAPK were shown to be important in modulating nuclear localisation. Finally, inhibition of nuclear import and export using Agaricus bisporus lectin and leptomycin B, respectively, demonstrated that cPLA2-\u03b1contains functional nuclear localisation and export signals. Thus we have identified a novel mode of regulation of cPLA2-\u03b1. This,together with the increasing body of evidence supporting the role of nuclear lipid second messengers in gene expression and proliferation, may have important implications for controlling the growth of endothelial cells in angiogenesis and tumour progression.<\/jats:p>","DOI":"10.1242\/jcs.00146","type":"journal-article","created":{"date-parts":[[2002,11,14]],"date-time":"2002-11-14T20:01:55Z","timestamp":1037304115000},"page":"4533-4543","source":"Crossref","is-referenced-by-count":28,"title":["Nuclear localisation of cytosolic phospholipase A2-\u03b1 in the EA.hy.926 human endothelial cell line is proliferation dependent and modulated by phosphorylation"],"prefix":"10.1242","volume":"115","author":[{"given":"Seema","family":"Grewal","sequence":"first","affiliation":[{"name":"School of Biochemistry and Molecular Biology, University of Leeds, Leeds, LS2 9JT, UK"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Ewan E.","family":"Morrison","sequence":"additional","affiliation":[{"name":"Cancer Research UK Clinical Centre, St. James' Hospital, University of Leeds,Leeds, LS9 7TF, UK"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Sreenivasan","family":"Ponnambalam","sequence":"additional","affiliation":[{"name":"School of Biochemistry and Molecular Biology, University of Leeds, Leeds, LS2 9JT, UK"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"John H.","family":"Walker","sequence":"additional","affiliation":[{"name":"School of Biochemistry and Molecular Biology, University of Leeds, Leeds, LS2 9JT, UK"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"237","reference":[{"key":"2021042517340196200_REF1","doi-asserted-by":"crossref","unstructured":"Abdullah, K., Cromlish, W. 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