Source:http://linkedlifedata.com/resource/pubmed/id/11553676
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
5
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| pubmed:dateCreated |
2001-9-12
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| pubmed:abstractText |
The physiological action of extracellular ATP and other nucleotides in the nervous system is controlled by surface-located enzymes (ecto-nucleotidases) of which several families with partially overlapping substrate specificities exist. In order to identify ecto-nucleotidases potentially associated with neural cells, we chose PC12 cells for analysis. PC12 cells revealed surface-located ATPase and ADPase activity with apparent K(m)-values of 283 microM and 243 microM, respectively. Using PCR we identified the mRNA of all members of the ecto-nucleoside triphosphate diphosphohydrolase family investigated (NTPDase1 to NTPDase3, NTPDase5/6), of ecto-nucleotide pyrophosphatase/phosphodiesterase3 (NPP3), tissue-non-specific alkaline phosphatase and ecto-5'-nucleotidase. The surface-located catalytic activity differed greatly between the various enzyme species. Our data suggest that hydrolysis of ATP and ADP is mainly due to members of the ecto-nucleoside triphosphate diphosphohydrolase family. Activity of ecto-5'-nucleotidase and alkaline phosphatase was very low and activity of NPP3 was absent. For a detailed analysis of the cellular distribution of ecto-nucleotidases single and double transfections of PC12 cells were performed, followed by fluorescence analysis. Ecto-nucleotidases were distributed over the entire cell surface and accumulated intracellularly in varicosities and neurite tips. PC12 cell ecto-nucleotidases are likely to play an important role in terminating autocrine functions of released nucleotides and in producing extracellular nucleosides supporting the survival and neuritic differentiation of PC12 cells.
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| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Diphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphatases,
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Alkaline Phosphatase,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/ectoATPase
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| pubmed:status |
MEDLINE
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| pubmed:month |
Sep
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| pubmed:issn |
0022-3042
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:volume |
78
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
1019-28
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| pubmed:dateRevised |
2006-11-15
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| pubmed:meshHeading |
pubmed-meshheading:11553676-Adenosine Diphosphate,
pubmed-meshheading:11553676-Adenosine Triphosphatases,
pubmed-meshheading:11553676-Adenosine Triphosphate,
pubmed-meshheading:11553676-Alkaline Phosphatase,
pubmed-meshheading:11553676-Animals,
pubmed-meshheading:11553676-CHO Cells,
pubmed-meshheading:11553676-Cell Differentiation,
pubmed-meshheading:11553676-Cell Survival,
pubmed-meshheading:11553676-Cricetinae,
pubmed-meshheading:11553676-Enzyme Activation,
pubmed-meshheading:11553676-Gene Expression Regulation, Enzymologic,
pubmed-meshheading:11553676-Hydrolysis,
pubmed-meshheading:11553676-Membrane Proteins,
pubmed-meshheading:11553676-Neurons,
pubmed-meshheading:11553676-PC12 Cells,
pubmed-meshheading:11553676-RNA, Messenger,
pubmed-meshheading:11553676-Rats,
pubmed-meshheading:11553676-Transfection
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| pubmed:year |
2001
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| pubmed:articleTitle |
Multiple ecto-nucleotidases in PC12 cells: identification and cellular distribution after heterologous expression.
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| pubmed:affiliation |
Biozentrum der J.W. Goethe-Universität, AK Neurochemie, Zoologisches Institut, Frankfurt am Main, Germany.
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| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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