National Tsing Hua University Institutional Repository:ACTIVATION OF HUMAN PLATELET PHOSPHOLIPASE-C AND PHOSPHOLIPASE-A2 BY VARIOUS OXYGENATED TRITERPENES
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    National Tsing Hua University Institutional Repository > 生命科學院  > 生命科學系 > 期刊論文 >  ACTIVATION OF HUMAN PLATELET PHOSPHOLIPASE-C AND PHOSPHOLIPASE-A2 BY VARIOUS OXYGENATED TRITERPENES


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    题名: ACTIVATION OF HUMAN PLATELET PHOSPHOLIPASE-C AND PHOSPHOLIPASE-A2 BY VARIOUS OXYGENATED TRITERPENES
    作者: WANG, CN;CHEN, JS;SHIAO, MS;WANG, CT
    教師: 王成德
    日期: 1994
    出版者: Elsevier
    關聯: European Journal of Pharmacology: Molecular Pharmacology,Elsevier,Volume 267,Issue 1,15 March 1994,Pages 33-42
    关键词: OXYGENATED TRITERPENES
    PHOSPHOLIPASE-C
    PHOSPHOLIPASE-A2
    摘要: Eight structural analogues of oxygenated triterpenes exerted striking differences in activation of human platelets. They arc four pairs of stereoisomers and two pairs of positional isomers with varying: 1) acetoxyl/hydroxyl substituents; 2) the position of the substituents at C-3 and C-15; and 3) the stereochemistry of a substituent at C-3. It required a threshold concentration for each agent to cause the concentration-dependent activation. These triterpenes were hydrophobic with < 20% difference in the partition coefficients between 1-octanol and water. They caused differential effects on: inositol triphosphate production; the increase in [Ca2+]i; diacylglycerol formation; phosphatidic acid accumulation, protein phosphorylations and arachidonate release. These agents activated both phospholipases C and A2. The trend of activating phospholipase C was triterpenes with two acetoxyl substituents > one acetoxyl/one hydroxyl substituents > two hydroxyl substituents. In activating phospholipase A2, triterpenes with two acetoxyl substituents were most effective, whereas the paired isomers with a hydroxyl group at C-15a and an acetoxyl substituent at C-3 failed the activation. The results enable one to discuss the possible structure-activity relationship of various oxygenated triterpenes in the activation of both phospholipases C and A2.
    URI: http://www.elsevier.com/
    http://nthur.lib.nthu.edu.tw/dspace/handle/987654321/48346
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