An ecto-ATPase and an ecto-ATP diphosphohydrolase are expressed in rat brain

被引:204
|
作者
Kegel, B
Braun, N
Heine, P
Maliszewski, CR
Zimmermann, H
机构
[1] UNIV FRANKFURT,AK NEUOCHEM,BIOZENTRUM,D-60439 FRANKFURT,GERMANY
[2] IMMUNEX RES & DEV CORP,SEATTLE,WA 98101
关键词
ADP; ATP; ecto-apyrase; ecto-ATP diphosphohydrolase; ecto-nucleotidase; ecto-ATPase;
D O I
10.1016/S0028-3908(97)00115-9
中图分类号
Q189 [神经科学];
学科分类号
071006 ;
摘要
Extracellular nucleotides acting as signaling molecules are inactivated by hydrolysis catalyzed by ecto-nucleotidases. ATP is sequentially degraded via ADP and AMP to adenosine. Enzymes that can be involved in the extracellular hydrolysis chain are ecto-ATP diphosphohydrolase (ecto-apyrase), ecto-ATPase, ecto-ADPase and 5'-nucleotidase. Mammalian ecto-ATP diphosphohydrolase is a member of a family of apyrases sharing four ''apyrase conserved regions'' that presumably participate in the formation of the catalytic site. We report the presence of ecto-ATP diphosphohydrolase in rat brain and the primary structure of a new mammalian member of the apyrase family. Expression in CHO cells shows that it represents an ecto-ATPase. As revealed by Northern analysis of rat tissues, the ecto-ATPase is co-expressed with ecto-ATP diphosphohydrolase in heart, kidney, spleen, thymus, lung, skeletal muscle and brain. Signals for both ecto-nucleotidases are very weak in Liver. mRNAs for both proteins are present in PC12 cells, suggesting that the two nucleotidases may be co-expressed in the same neural cell. Using computer-aided sequence analysis, primary structure and membrane topography are compared with those of other members of the apyrase family. (C) 1997 Published by Elsevier Science Ltd.
引用
收藏
页码:1189 / 1200
页数:12
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