{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,29]],"date-time":"2026-04-29T08:18:00Z","timestamp":1777450680082,"version":"3.51.4"},"reference-count":50,"publisher":"Oxford University Press (OUP)","issue":"5","license":[{"start":{"date-parts":[[2007,5,1]],"date-time":"2007-05-01T00:00:00Z","timestamp":1177977600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/academic.oup.com\/pages\/standard-publication-reuse-rights"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2007,5,1]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>We examined the mechanism by which lysophosphatidylcholine (LPC) regulates \u03b22-integrin\u2013mediated adhesion of eosiniophils. Eosinophils were isolated from blood of mildly atopic volunteers by negative immunomagnetic selection. \u03b22-integrin\u2013dependent adhesion of eosinophils to plated bovine serum albumin (BSA) was measured by residual eosinophil peroxidase activity. LPC caused maximal adhesion of eosinophils to plated BSA at 4 \u03bcM. Lysophosphatidylinositol, which has a similar molecular shape, mimicked the effect of LPC on eosinophil adhesion, while neither lysophosphatidylserine nor lysophosphatidylethanolamine had any effect. Phosphatidylethanolamine, a lipid that has a molecular orientation that is the inverse of LPC, blocked eosinophil adhesion caused by LPC. Unlike platelet-activating factor, a G-protein\u2013coupled receptor agonist, LPC did not cause Ca2+-store depletion, but caused increased Ca2+ influx upon addition of Ca2+ to extracellular medium. This influx was not inhibited by U73122, a phospholipase C inhibitor, demonstrating independence from the G protein\u2013activated phospholipase C pathway. Ca2+ influx was inhibited by either preincubation of phosphotidylethanolamine or La3+, a broad spectrum blocker of cation channels. LPC induced up-regulation of the active conformation of CD11b, which was blocked by preincubation with phosphatidylethanolamine. These data suggest that LPC causes a non\u2013store-operated Ca2+ influx into eosinophils, which subsequently activates CD11b\/CD18 to promote eosinophil adhesion.<\/jats:p>","DOI":"10.1165\/rcmb.2006-0391oc","type":"journal-article","created":{"date-parts":[[2007,1,11]],"date-time":"2007-01-11T21:05:10Z","timestamp":1168549510000},"page":"585-593","source":"Crossref","is-referenced-by-count":32,"title":["Regulation of Eosinophil Adhesion by Lysophosphatidylcholine via a Non\u2013Store-Operated Ca2+ Channel"],"prefix":"10.1093","volume":"36","author":[{"given":"Xiangdong","family":"Zhu","sequence":"first","affiliation":[{"name":"Section of Pulmonary and Critical Care Medicine, Department of Medicine; and Department of Neurobiology, Pharmacology and Physiology, Pediatrics, Anesthesia and Critical Care, and Committees on Clinical Pharmacology, Cell Physiology and Molecular Medicine, Division of the Biological Sciences, The University of Chicago, Chicago, 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Illinois"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Lilly","family":"Zhu","sequence":"additional","affiliation":[{"name":"Section of Pulmonary and Critical Care Medicine, Department of Medicine; and Department of Neurobiology, Pharmacology and Physiology, Pediatrics, Anesthesia and Critical Care, and Committees on Clinical Pharmacology, Cell Physiology and Molecular Medicine, Division of the Biological Sciences, The University of Chicago, Chicago, Illinois"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Peter V.","family":"Usatyuk","sequence":"additional","affiliation":[{"name":"Section of Pulmonary and Critical Care Medicine, Department of Medicine; and Department of Neurobiology, Pharmacology and Physiology, Pediatrics, Anesthesia and Critical Care, and Committees on Clinical Pharmacology, Cell Physiology and Molecular Medicine, Division of the Biological Sciences, The University of Chicago, Chicago, 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