{"title":"抗炎脂皮质素衍生肽。","authors":"M Perretti, R J Flower","doi":"10.1007/978-3-0348-7276-8_13","DOIUrl":null,"url":null,"abstract":"<p><p>Peptide Ac2-26, drawn from the sequence of human lipocortin 1, inhibited the release of elastase activity from cytoplasmic granules of human neutrophils, and neutrophil adhesion to monolayers of endothelial cells, in a concentration-dependent manner (approximate IC50 of 100 micrograms/ml, 33 microM). The effect of peptide Ac2-26 was not restricted to a specific neutrophil activator, being effective against formyl-Met-Leu-Phe (FMLP), leukotriene B4 (LTB4) and platelet-activating factor (PAF). Peptide Ac2-26 did not alter FMLP binding to its receptor. These in vitro observations complement in vivo data obtained with this peptide and may enable a better understanding of its pharmacology and, perhaps, that of of lipocortin 1 too.</p>","PeriodicalId":7491,"journal":{"name":"Agents and actions. Supplements","volume":"46 ","pages":"131-8"},"PeriodicalIF":0.0000,"publicationDate":"1995-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"7","resultStr":"{\"title\":\"Anti-inflammatory lipocortin-derived peptides.\",\"authors\":\"M Perretti, R J Flower\",\"doi\":\"10.1007/978-3-0348-7276-8_13\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>Peptide Ac2-26, drawn from the sequence of human lipocortin 1, inhibited the release of elastase activity from cytoplasmic granules of human neutrophils, and neutrophil adhesion to monolayers of endothelial cells, in a concentration-dependent manner (approximate IC50 of 100 micrograms/ml, 33 microM). The effect of peptide Ac2-26 was not restricted to a specific neutrophil activator, being effective against formyl-Met-Leu-Phe (FMLP), leukotriene B4 (LTB4) and platelet-activating factor (PAF). Peptide Ac2-26 did not alter FMLP binding to its receptor. These in vitro observations complement in vivo data obtained with this peptide and may enable a better understanding of its pharmacology and, perhaps, that of of lipocortin 1 too.</p>\",\"PeriodicalId\":7491,\"journal\":{\"name\":\"Agents and actions. Supplements\",\"volume\":\"46 \",\"pages\":\"131-8\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1995-01-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"7\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Agents and actions. Supplements\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.1007/978-3-0348-7276-8_13\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Agents and actions. Supplements","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1007/978-3-0348-7276-8_13","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 7
摘要
肽Ac2-26,从人脂皮质蛋白1序列中提取,以浓度依赖的方式抑制人中性粒细胞胞质颗粒中弹性酶活性的释放,以及中性粒细胞对内皮细胞单层的粘附(IC50约为100微克/毫升,33微米)。肽Ac2-26的作用不局限于特定的中性粒细胞激活剂,对甲酰基met - leu - phe (FMLP),白三烯B4 (LTB4)和血小板活化因子(PAF)有效。肽Ac2-26不改变FMLP与其受体的结合。这些体外观察补充了用这种肽获得的体内数据,并可能使我们更好地了解其药理学,也许也可以了解脂皮质素1的药理学。
Peptide Ac2-26, drawn from the sequence of human lipocortin 1, inhibited the release of elastase activity from cytoplasmic granules of human neutrophils, and neutrophil adhesion to monolayers of endothelial cells, in a concentration-dependent manner (approximate IC50 of 100 micrograms/ml, 33 microM). The effect of peptide Ac2-26 was not restricted to a specific neutrophil activator, being effective against formyl-Met-Leu-Phe (FMLP), leukotriene B4 (LTB4) and platelet-activating factor (PAF). Peptide Ac2-26 did not alter FMLP binding to its receptor. These in vitro observations complement in vivo data obtained with this peptide and may enable a better understanding of its pharmacology and, perhaps, that of of lipocortin 1 too.