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Title
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NO-induced activation of cyclic GMP-dependent pathway down regulates ecto-nucleotide pyrophosphatase/phosphodiesterase 1 (NPP1) protein in rat C6 glioma
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Author
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Abstract
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| In rat C6 glioma cells, the ecto-nucleotide pyrophosphatase/phosphodiesterase-1 (NPP1), a modulator of purinergic receptor signaling, is down regulated after an increase in intracellular cAMP by addition of dibutyryl cAMP, a membrane-permeable cAMP-analog, or by activation of the β-adrenoceptor receptor with (−)-isoproterenol (Aerts et al., 2011, Eur. J. Pharmacol. 654, 19). In this communication we studied the effect of nitric oxide (NO)/cGMP, a pathway also affecting purinergic receptor signaling, on the level of NPP1 protein. Sodium nitroprusside (SNP), a NO donor, reduces NPP1 protein in a dose-dependent manner. A combination of SNP and 1H-[1,2,4]oxadiazolo[4,3-a]quinoxalin-1-one, an inhibitor of soluble guanylate cyclase, demonstrated that NO-dependent down regulation of NPP1 was caused by NO-sensitive guanylyl cyclase. Treatment with Rp-pCPT-cGMPS, an inhibitor of protein kinase G (PKG), showed that PKG is not involved in the down regulation of NPP1. In addition, we have shown that the cAMP- and cGMP-dependent decrease in NPP1 expression is unrelated. These results indicate that NO/cGMP regulates the level of NPP1 protein by a pathway that differs from the cAMP-induced decrease in NPP1. |
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Language
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English
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Source (journal)
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European journal of pharmacology. - Amsterdam, 1967, currens
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Publication
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Amsterdam
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North-Holland
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2011
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ISSN
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0014-2999
[print]
1879-0712
[online]
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DOI
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10.1016/J.EJPHAR.2011.03.004
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Volume/pages
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659
:1
(2011)
, p. 1-6
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ISI
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000291119300001
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Full text (Publisher's DOI)
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