Source:http://linkedlifedata.com/resource/pubmed/id/17786543
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1-2
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pubmed:dateCreated |
2007-10-22
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pubmed:abstractText |
In the present study we investigate the biochemical properties of the members of NPP family in synaptosomes prepared from rat heart left ventricles. Using p-nitrophenyl-5'-thymidine monophosphate (p-Nph-5'-TMP) as substrate for E-NPPs in rat cardiac synaptosomes, we observed an alkaline pH dependence, divalent cation dependence and the K ( M ) value corresponded to 91.42 +/- 13.97 microM and the maximal velocity (V ( max )) value calculated was 63.79 +/- 3.59 nmol p-nitrophenol released/min/mg of protein (mean +/- SD, n = 4). Levamisole (1 mM), was ineffective as inhibitor of p-Nph-5'-TMP hydrolysis in pH 8.9 (optimum pH for the enzyme characterized). Suramin (0.25 mM) strongly reduced the hydrolysis of p-Nph-5'-TMP by about 46%. Sodium azide (10 and 20 mM) and gadolinium chloride (0.3 and 0.5 mM), E-NTPases inhibitors, had no effects on p-Nph-5'-TMP hydrolysis. RT-PCR analysis of left ventricle demonstrated the expression of NPP2 and NPP3 enzymes, but excluded the presence of NPP1 member. By quantitative real-time PCR we identified the NPP3 as the enzyme with the highest expression in rat left ventricle. The demonstration of the presence of the E-NPP family in cardiac system, suggest that these enzymes could contribute with the fine-tuning control of the nucleotide levels at the nerve terminal endings of left ventricles that are involved in several cardiac pathologies.
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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/4-nitrophenol,
http://linkedlifedata.com/resource/pubmed/chemical/Antineoplastic Agents,
http://linkedlifedata.com/resource/pubmed/chemical/Enpp3 protein, rat,
http://linkedlifedata.com/resource/pubmed/chemical/Enzyme Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Nitrophenols,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoric Diester Hydrolases,
http://linkedlifedata.com/resource/pubmed/chemical/Pyrophosphatases,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/Sodium Azide,
http://linkedlifedata.com/resource/pubmed/chemical/Suramin,
http://linkedlifedata.com/resource/pubmed/chemical/Thymidine Monophosphate,
http://linkedlifedata.com/resource/pubmed/chemical/ectonucleotide pyrophosphatase...
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0300-8177
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
306
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
247-54
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pubmed:dateRevised |
2011-7-15
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pubmed:meshHeading |
pubmed-meshheading:17786543-Animals,
pubmed-meshheading:17786543-Antineoplastic Agents,
pubmed-meshheading:17786543-Enzyme Inhibitors,
pubmed-meshheading:17786543-Heart Ventricles,
pubmed-meshheading:17786543-Hydrolysis,
pubmed-meshheading:17786543-Male,
pubmed-meshheading:17786543-Nitrophenols,
pubmed-meshheading:17786543-Phosphoric Diester Hydrolases,
pubmed-meshheading:17786543-Pyrophosphatases,
pubmed-meshheading:17786543-RNA, Messenger,
pubmed-meshheading:17786543-Rats,
pubmed-meshheading:17786543-Rats, Wistar,
pubmed-meshheading:17786543-Reverse Transcriptase Polymerase Chain Reaction,
pubmed-meshheading:17786543-Sodium Azide,
pubmed-meshheading:17786543-Suramin,
pubmed-meshheading:17786543-Synaptosomes,
pubmed-meshheading:17786543-Thymidine Monophosphate
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pubmed:year |
2007
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pubmed:articleTitle |
Biochemical characterization of ecto-nucleotide pyrophosphatase/phosphodiesterase (E-NPP, E.C. 3.1.4.1) from rat heart left ventricle.
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pubmed:affiliation |
Departamento de Bioquímica, Instituto de Ciências Básicas da Saúde, Universidade Federal do Rio Grande do Sul - UFRGS, Rua Ramiro Barcelos, 2600 - Prédio ANEXO, Porto Alegre, RS CEP 90035-003, Brazil.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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