McNeely T B, Rosen G, Londner M V, Turco S J
Department of Biochemistry, University of Kentucky Medical Center, Lexington 40502.
Biochem J. 1989 Apr 15;259(2):601-4. doi: 10.1042/bj2590601.
Fragments of the lipophosphoglycan of Leishmania donovani were generated by phospholipase C digestion and mild acid hydrolysis. The fragments were purified and examined for inhibitory activity on protein kinase C isolated from rat brains. On a molar basis, the 1-O-alkylglycerol portion of LPG exhibited the most inhibitory activity, whereas the carbohydrate domain was not as effective. In addition, several glycolipid antigens from L. major, which contain short carbohydrate chains attached to phosphatidylinositol, were also efficient inhibitors of the enzyme. These results are consistent with the hypothesis that protein kinase C may be a key target for the parasites to overcome within host macrophages.
杜氏利什曼原虫的脂磷壁酸片段通过磷脂酶C消化和温和酸水解产生。对这些片段进行纯化,并检测其对从大鼠脑中分离出的蛋白激酶C的抑制活性。以摩尔计,脂磷壁酸的1-O-烷基甘油部分表现出最强的抑制活性,而碳水化合物结构域的效果则没那么好。此外,来自硕大利什曼原虫的几种糖脂抗原,它们含有连接在磷脂酰肌醇上的短碳水化合物链,也是该酶的有效抑制剂。这些结果与蛋白激酶C可能是寄生虫在宿主巨噬细胞内需要克服的关键靶点这一假说相符。