{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,15]],"date-time":"2026-04-15T14:27:55Z","timestamp":1776263275216,"version":"3.50.1"},"reference-count":0,"publisher":"Portland Press Ltd.","issue":"1","content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[1992,10,1]]},"abstract":"<jats:p>A comparative study of real-time kinetics of respiratory burst, monitored by H2O2-dependent chemiluminescence, and phospholipase D (PLD)-mediated phosphatidylcholine breakdown has been undertaken on human neutrophils stimulated by N-formylmethionyl-leucylphenylalanine in the absence of cytochalasin B. The fungal metabolite 17-hydroxywortmannin (HWT), an inhibitor of NADPH oxidase activation, decreases phosphatidic acid (PA) production by 30% at a concentration of 1 nM. Higher concentrations (10 nM-1 microM) inhibit PA formation maximally by 50% as compared with control. In all cases, the inhibition is delayed by 20-30 s after addition of the agonist. Thus the full PA generation is actually the result of an early (HWT-insensitive) and a late (HWT-sensitive) phosphatidylcholine breakdown. However, under all conditions, alkylacylglycerol remains at the basal level. PLD activity is dependent on Ca2+ influx, but is fully inhibited in cells depleted of Ca2+ with EGTA and Quin 2. The effect of HWT on the respiratory burst was investigated by measuring the kinetics of H2O2-induced chemiluminescence. This method allows to distinguish various phases of superoxide ion production: a lag, an increase in H2O2 formation (early phase), the duration of H2O2 production (late phase) and the termination of the oxidative burst. The lag remains constant for all HWT concentrations. A concentration of 10 nM-HWT, which fully inhibits the HWT-sensitive part of PA production, decreases superoxide ion production with a delay of about 20 s after addition of the agonist. Higher HWT concentrations, which have no additional effect on PLD inhibition, equally affect an early and a late phase of the burst. Thus high doses of HWT have a site of action which decreases the whole burst but does not affect the PLD any more. Therefore HWT and Ca2+ provide evidence for a two-step process for PLD activation. Only the delayed PA generation is functionally linked to a late phase of the oxidative burst.<\/jats:p>","DOI":"10.1042\/bj2870067","type":"journal-article","created":{"date-parts":[[2015,8,10]],"date-time":"2015-08-10T21:28:56Z","timestamp":1439242136000},"page":"67-72","update-policy":"https:\/\/doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":27,"title":["Human neutrophil phospholipase D activation by <i>N<\/i>-formylmethionyl-leucylphenylalanine reveals a two-step process for the control of phosphatidylcholine breakdown and oxidative burst"],"prefix":"10.1042","volume":"287","author":[{"given":"P","family":"G\u00e9las","sequence":"first","affiliation":[{"name":"INSERM U 326, H\u00f4pital Purpan, Place Dr. Baylac, 31059 Toulouse Cedex, France."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"V","family":"Von Tscharner","sequence":"additional","affiliation":[{"name":"Theodor Kocher Institute, University of Bern, CH-3000 Bern-9, Switzerland"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"M","family":"Record","sequence":"additional","affiliation":[{"name":"INSERM U 326, H\u00f4pital Purpan, Place Dr. Baylac, 31059 Toulouse Cedex, France."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"M","family":"Baggiolini","sequence":"additional","affiliation":[{"name":"Theodor Kocher Institute, University of Bern, CH-3000 Bern-9, Switzerland"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"H","family":"Chap","sequence":"additional","affiliation":[{"name":"INSERM U 326, H\u00f4pital Purpan, Place Dr. Baylac, 31059 Toulouse Cedex, France."}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"288","container-title":["Biochemical Journal"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/287\/1\/67\/607265\/bj2870067.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/287\/1\/67\/607265\/bj2870067.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,11,23]],"date-time":"2021-11-23T21:59:34Z","timestamp":1637704774000},"score":1,"resource":{"primary":{"URL":"https:\/\/portlandpress.com\/biochemj\/article\/287\/1\/67\/28319\/Human-neutrophil-phospholipase-D-activation-by-N"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1992,10,1]]},"references-count":0,"journal-issue":{"issue":"1","published-print":{"date-parts":[[1992,10,1]]}},"URL":"https:\/\/doi.org\/10.1042\/bj2870067","relation":{},"ISSN":["0264-6021","1470-8728"],"issn-type":[{"value":"0264-6021","type":"print"},{"value":"1470-8728","type":"electronic"}],"subject":[],"published":{"date-parts":[[1992,10,1]]}}}