Intrastriatal hypoxanthine administration affects Na+,K+-ATPase, acetylcholinesterase and catalase activities in striatum, hippocampus and cerebral cortex of rats

被引:8
|
作者
Bavaresco, Caren Serra [1 ]
Chiarani, Fabria [1 ]
Wajner, Moacir [1 ]
Alexandre Netto, Carlos [1 ]
de Souza Wyse, Angela Terezinha [1 ]
机构
[1] Univ Fed Rio Grande do Sul, Dept Bioquim, Inst Ciencias Basicas Saude, BR-90035003 Porto Alegre, RS, Brazil
关键词
Lesch-Nyhan; metabolic disease; hypoxanthine; intrastriatal injection; Na+; K+-ATPase; acetylcholinesterase; catalase;
D O I
10.1016/j.ijdevneu.2006.08.007
中图分类号
Q [生物科学];
学科分类号
07 ; 0710 ; 09 ;
摘要
The aim of this study was to investigate the effects of a single intrastriatal injection of hypoxanthine, the major metabolite accumulating in Lesch-Nyhan disease, on Na+,K+-ATPase, acetylcholinesterase and catalase activities in striatum, cerebral cortex and hippocampus of rats at different post-infusion periods. Adult Wistar rats were divided in two groups: (1) vehicle-injected group (control) and (2) hypoxanthine-injected group. For Na+,K+-ATPase activity determination, the animals were sacrificed 3 h, 24 h and 7 days after drug infusion. For the evaluation of acetylcholinesterase and catalase activities, the animals were sacrificed 30 min, 3 h, 24 h and 7 days after hypoxanthine infusion. Results show regional and time dependent effects of hypoxanthine on Na+,K+-ATPase, acetylcholinesterase and catalase activities. The in vitro effect of hypoxanthine on the same enzymes in striatum was also investigated. Results showed that hypoxanthine inhibited Na+,K+-ATPase, but not the activities of acetylcholinesterase and catalase in rat striatum. We suggest that these modification on cerebral biochemical parameters (Na+,K+-ATPase, acetylcholinesterase and catalase activities) induced by intrastriatal administration of hypoxanthine in all cerebral structures studied, striatum, hippocampus and cerebral cortex, could be involved in the pathophysiology of Lesch-Nyhan disease. (c) 2006 ISDN. Published by Elsevier Ltd. All rights reserved.
引用
收藏
页码:411 / 417
页数:7
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