{"title":"活化小鼠腹腔巨噬细胞中p72syk样蛋白的酪氨酸磷酸化。","authors":"K I Abu-Lawi, B M Sultzer","doi":"","DOIUrl":null,"url":null,"abstract":"<p><p>As a marker of macrophage activation, IL-1 alpha was measured after stimulation of murine resident peritoneal macrophages (RPM) with endotoxin-associated protein (EP). Significant IL-1 alpha was produced by EP-stimulated RPM from both C3H/OuJ and C3H/HeJ mouse strains. This EP-mediated IL-1 alpha production was blocked by tyrosine kinase inhibitors including genistein and tyrphostin, suggesting the involvement of a protein tyrosine kinase in the activation of RPM by EP. Immunoblot analysis using antiphosphotyrosine antibody showed that EP induces the tyrosine phosphorylation of a 71 kD protein (p71). The p71 and the spleen tyrosine kinase p72syk found in other cell types share common features including: similar molecular weight, PKC independent tyrosine phosphorylation, and inhibition of phosphorylation by piceatannol. Furthermore, immunoblot analysis using anti-p72syk antibody detected the p72syk kinase in EP-activated RPM. These results suggest that the activation of RPM involves an early tyrosine phosphorylation of p72syk or a p72syk-like protein.</p>","PeriodicalId":72545,"journal":{"name":"Cellular & molecular biology research","volume":"41 1","pages":"49-58"},"PeriodicalIF":0.0000,"publicationDate":"1995-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"The tyrosine phosphorylation of a p72syk-like protein in activated murine resident peritoneal macrophages.\",\"authors\":\"K I Abu-Lawi, B M Sultzer\",\"doi\":\"\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>As a marker of macrophage activation, IL-1 alpha was measured after stimulation of murine resident peritoneal macrophages (RPM) with endotoxin-associated protein (EP). Significant IL-1 alpha was produced by EP-stimulated RPM from both C3H/OuJ and C3H/HeJ mouse strains. This EP-mediated IL-1 alpha production was blocked by tyrosine kinase inhibitors including genistein and tyrphostin, suggesting the involvement of a protein tyrosine kinase in the activation of RPM by EP. Immunoblot analysis using antiphosphotyrosine antibody showed that EP induces the tyrosine phosphorylation of a 71 kD protein (p71). The p71 and the spleen tyrosine kinase p72syk found in other cell types share common features including: similar molecular weight, PKC independent tyrosine phosphorylation, and inhibition of phosphorylation by piceatannol. Furthermore, immunoblot analysis using anti-p72syk antibody detected the p72syk kinase in EP-activated RPM. These results suggest that the activation of RPM involves an early tyrosine phosphorylation of p72syk or a p72syk-like protein.</p>\",\"PeriodicalId\":72545,\"journal\":{\"name\":\"Cellular & molecular biology research\",\"volume\":\"41 1\",\"pages\":\"49-58\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1995-01-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Cellular & molecular biology research\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Cellular & molecular biology research","FirstCategoryId":"1085","ListUrlMain":"","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
The tyrosine phosphorylation of a p72syk-like protein in activated murine resident peritoneal macrophages.
As a marker of macrophage activation, IL-1 alpha was measured after stimulation of murine resident peritoneal macrophages (RPM) with endotoxin-associated protein (EP). Significant IL-1 alpha was produced by EP-stimulated RPM from both C3H/OuJ and C3H/HeJ mouse strains. This EP-mediated IL-1 alpha production was blocked by tyrosine kinase inhibitors including genistein and tyrphostin, suggesting the involvement of a protein tyrosine kinase in the activation of RPM by EP. Immunoblot analysis using antiphosphotyrosine antibody showed that EP induces the tyrosine phosphorylation of a 71 kD protein (p71). The p71 and the spleen tyrosine kinase p72syk found in other cell types share common features including: similar molecular weight, PKC independent tyrosine phosphorylation, and inhibition of phosphorylation by piceatannol. Furthermore, immunoblot analysis using anti-p72syk antibody detected the p72syk kinase in EP-activated RPM. These results suggest that the activation of RPM involves an early tyrosine phosphorylation of p72syk or a p72syk-like protein.