Christoph C. Geilen , Rüdiger Haase , Klaus Buchner , Thomas Wieder , Ferdinand Hucho , Werner Reutter
{"title":"磷脂类似物,十六烷基磷脂胆碱,在体外抑制蛋白激酶C和拮抗酚酯刺激的细胞增殖","authors":"Christoph C. Geilen , Rüdiger Haase , Klaus Buchner , Thomas Wieder , Ferdinand Hucho , Werner Reutter","doi":"10.1016/0277-5379(91)90438-J","DOIUrl":null,"url":null,"abstract":"<div><p>The antineoplastic agent, hexadecylphosphocholine, a phospholipid analogue, inhibited phosphatidylserine-activated protein kinase C <em>in vitro</em> at concentrations higher than 40 μmol/l. The half-inhibitory concentration (IC<sub>50</sub>) was 62 μmol/l. Another alkylphosphocholine, dodecylphosphocholine, did not have an inhibitory effect on protein kinase C. At the same concentrations, hexadecylphosphocholine antagonised the phorbol ester-stimulated proliferation of Madin-Darby canine kidney cells whereas dodecylphosphocholine had no effect. In addition, phorbol ester-induced morphological changes of these epithelial cells were antagonised by hexadecylphosphocholine. Both effects of hexadecylphosphocholine, the inhibition of protein kinase C and the antagonisation of the altered cell morphology induced by phorbol ester, were comparable to those observed after treatment with sphingosine, a known protein kinase C inhibitor. We conclude that one possible mechanism of the antineoplatic action of hexadecylphosphocholine is mediated by inhibition of protein kinase C.</p></div>","PeriodicalId":11925,"journal":{"name":"European Journal of Cancer and Clinical Oncology","volume":"27 12","pages":"Pages 1650-1653"},"PeriodicalIF":0.0000,"publicationDate":"1991-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0277-5379(91)90438-J","citationCount":"60","resultStr":"{\"title\":\"The phospholipid analogue, hexadecylphosphocholine, inhibits protein kinase C in vitro and antagonises phorbol ester-stimulated cell proliferation\",\"authors\":\"Christoph C. Geilen , Rüdiger Haase , Klaus Buchner , Thomas Wieder , Ferdinand Hucho , Werner Reutter\",\"doi\":\"10.1016/0277-5379(91)90438-J\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p>The antineoplastic agent, hexadecylphosphocholine, a phospholipid analogue, inhibited phosphatidylserine-activated protein kinase C <em>in vitro</em> at concentrations higher than 40 μmol/l. The half-inhibitory concentration (IC<sub>50</sub>) was 62 μmol/l. Another alkylphosphocholine, dodecylphosphocholine, did not have an inhibitory effect on protein kinase C. At the same concentrations, hexadecylphosphocholine antagonised the phorbol ester-stimulated proliferation of Madin-Darby canine kidney cells whereas dodecylphosphocholine had no effect. In addition, phorbol ester-induced morphological changes of these epithelial cells were antagonised by hexadecylphosphocholine. Both effects of hexadecylphosphocholine, the inhibition of protein kinase C and the antagonisation of the altered cell morphology induced by phorbol ester, were comparable to those observed after treatment with sphingosine, a known protein kinase C inhibitor. We conclude that one possible mechanism of the antineoplatic action of hexadecylphosphocholine is mediated by inhibition of protein kinase C.</p></div>\",\"PeriodicalId\":11925,\"journal\":{\"name\":\"European Journal of Cancer and Clinical Oncology\",\"volume\":\"27 12\",\"pages\":\"Pages 1650-1653\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1991-12-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1016/0277-5379(91)90438-J\",\"citationCount\":\"60\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"European Journal of Cancer and Clinical Oncology\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/027753799190438J\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"European Journal of Cancer and Clinical Oncology","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/027753799190438J","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
The phospholipid analogue, hexadecylphosphocholine, inhibits protein kinase C in vitro and antagonises phorbol ester-stimulated cell proliferation
The antineoplastic agent, hexadecylphosphocholine, a phospholipid analogue, inhibited phosphatidylserine-activated protein kinase C in vitro at concentrations higher than 40 μmol/l. The half-inhibitory concentration (IC50) was 62 μmol/l. Another alkylphosphocholine, dodecylphosphocholine, did not have an inhibitory effect on protein kinase C. At the same concentrations, hexadecylphosphocholine antagonised the phorbol ester-stimulated proliferation of Madin-Darby canine kidney cells whereas dodecylphosphocholine had no effect. In addition, phorbol ester-induced morphological changes of these epithelial cells were antagonised by hexadecylphosphocholine. Both effects of hexadecylphosphocholine, the inhibition of protein kinase C and the antagonisation of the altered cell morphology induced by phorbol ester, were comparable to those observed after treatment with sphingosine, a known protein kinase C inhibitor. We conclude that one possible mechanism of the antineoplatic action of hexadecylphosphocholine is mediated by inhibition of protein kinase C.