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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
9
|
| pubmed:dateCreated |
1998-2-5
|
| pubmed:databankReference | |
| pubmed:abstractText |
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.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Sep
|
| pubmed:issn |
0028-3908
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
36
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
1189-200
|
| pubmed:dateRevised |
2006-11-15
|
| pubmed:meshHeading |
pubmed-meshheading:9364474-Adenosine Triphosphatases,
pubmed-meshheading:9364474-Amino Acid Sequence,
pubmed-meshheading:9364474-Animals,
pubmed-meshheading:9364474-Apyrase,
pubmed-meshheading:9364474-Base Sequence,
pubmed-meshheading:9364474-Blotting, Northern,
pubmed-meshheading:9364474-Brain,
pubmed-meshheading:9364474-CHO Cells,
pubmed-meshheading:9364474-Chickens,
pubmed-meshheading:9364474-Cloning, Molecular,
pubmed-meshheading:9364474-Conserved Sequence,
pubmed-meshheading:9364474-Cricetinae,
pubmed-meshheading:9364474-DNA, Complementary,
pubmed-meshheading:9364474-Molecular Sequence Data,
pubmed-meshheading:9364474-Phylogeny,
pubmed-meshheading:9364474-Rats,
pubmed-meshheading:9364474-Sequence Alignment,
pubmed-meshheading:9364474-Sequence Analysis, DNA,
pubmed-meshheading:9364474-Transfection
|
| pubmed:year |
1997
|
| pubmed:articleTitle |
An ecto-ATPase and an ecto-ATP diphosphohydrolase are expressed in rat brain.
|
| pubmed:affiliation |
AK Neurochemie, Biozentrum der J. W. Goethe-Universität, Frankfurt am Main, Germany.
|
| pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
|