Inhibition of nucleoside diphosphate kinase (NDPK/nm23) by cAMP analogues

Anciaux, Katelijne; Dommelen, Kristof Van; Willems, Roel; Roymans, Dirk; Slegers, Herman

doi:10.1016/s0014-5793(96)01358-0

Cited by 23 publications

(21 citation statements)

References 43 publications

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“…The affinity for PAP was one order of magnitude lower (K D ϭ 100 M). In the case of cAMP, the measured K D ϭ 500 M is in good agreement with the value previously reported (27,28). No saturation could be reached with AMP, indicating a K D Ͼ 10 mM.…”

Section: Resultssupporting

confidence: 91%

“…The inhibition constants (K I ) for PAP, PAPS, and cAMP derived from measurements of NDP kinase enzymatic activity were compared with equilibrium dissociation constants ( tion, they showed that replacing the Phe 64 phenyl group with the indole of a tryptophan has little effect on the nucleotide interaction with the enzyme, even though it is in direct contact with the nucleobase. The poorest inhibitor is cAMP, with a K D of 500 M. This agrees with a previous kinetic determination (27,28). The best is PAPS with a 50 times better affinity.…”

Section: Fig 2 Titration Curve Of Wild Type Ndp Kinase With Papssupporting

confidence: 90%

“…Although cAMP was shown to inhibit NDP kinase activity (27,28), its affinity for the enzyme was rather poor (0.5 mM). Flavonoid derivatives from plants were also reported as inhibitors of NDP kinase (29).…”

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confidence: 99%

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3′-Phosphorylated Nucleotides Are Tight Binding Inhibitors of Nucleoside Diphosphate Kinase Activity

Schneider

Janin

et al. 1998

Journal of Biological Chemistry

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Section: Resultssupporting

confidence: 91%

Section: Fig 2 Titration Curve Of Wild Type Ndp Kinase With Papssupporting

confidence: 90%

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3′-Phosphorylated Nucleotides Are Tight Binding Inhibitors of Nucleoside Diphosphate Kinase Activity

Schneider

Janin

et al. 1998

Journal of Biological Chemistry

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“…Previously, cyclic AMP analogues were shown to inhibit NDPK activity, with IC 50 values in the 100-500 μM range [54]. More recently, angiostatin (a proteolytic fragment of plasminogen), polyphenols, and adenosine 3′-phosphate 5′-phosphosulfate were shown to inhibit secreted NDPK-B, but only one of these compounds, ellagic acid, displayed inhibitory effect in the low micromolar concentration range (IC 50 ∼10 μM [55]).…”

Section: Discussionmentioning

confidence: 99%

Ebselen is a potent non-competitive inhibitor of extracellular nucleoside diphosphokinase

Lucia

Catharina

Mugesh

et al. 2010

Purinergic Signalling

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Nucleoside di-and triphosphates and adenosine regulate several components of the mucocilairy clearance process (MCC) that protects the lung against infections, via activation of epithelial purinergic receptors. However, assessing the contribution of individual nucleotides to MCC functions remains difficult due to the complexity of the mechanisms of nucleotide release and metabolism. Enzymatic activities involved in the metabolism of extracellular nucleotides include ecto-ATPases and secreted nucleoside diphosphokinase (NDPK) and adenyl kinase, but potent and selective inhibitors of these activities are sparse. In the present study, we discovered that ebselen markedly reduced NDPK activity while having negligible effect on ecto-ATPase and adenyl kinase activities.

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“…Western Blotting-Proteins in the lysates of 15 ϫ 10 6 platelets or 10 6 erythrocytes were separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, on a 20% (w/v) gel (27). The gel was electroblotted onto a Hybond-C cellulose membrane and nm23 immunodetected with either anti-nm23-H1 (Novocastra, Newcastle, UK) or anti-NDPK␣/ nm23-H2 antibody (Dr. Kimura, Tokyo Metropolitan Institute of Gerontology, Japan).…”

Section: Labeling Of Cells For Flow Cytometric Analysis-cellsmentioning

confidence: 99%

Decrease in Nucleoside Diphosphate Kinase (NDPK/nm23) Expression during Hematopoietic Maturation

Willems¹,

Bockstaele²,

Lardon³

et al. 1998

Journal of Biological Chemistry

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The nucleoside diphosphate kinase (NDPK/nm23) isoforms H1 and H2 were localized in hematopoietic tissues. Flow cytometric analysis and enzymatic assays were used to quantify the intracellular and extracellular concentrations of NDPK. Bone marrow CD34؉ progenitors contained the highest intracellular levels of both nm23-H1 and nm23-H2. Lower levels were measured in more mature bone marrow cells, whereas peripheral blood leukocytes had the lowest expression of nm23. These data suggest a function of NDPK in early hematopoiesis and a down-regulation of NDPK upon differentiation. In addition, an up-regulation of nm23 expression was observed in lymphocytes after induction of proliferation with phytohemagglutinin. Multiparameter flow cytometry demonstrated that this up-regulation occurred during the G 0 /G 1 -transition. Flow cytometric analysis also revealed a weak surface expression of nm23 on a number of hematopoietic cell lines, which was not detected on normal hematopoietic cells. Our data also demonstrated the presence of NDPK in human plasma, probably due to a limited in vivo lysis of red blood cells.

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Inhibition of nucleoside diphosphate kinase (NDPK/nm23) by cAMP analogues

Cited by 23 publications

References 43 publications

3′-Phosphorylated Nucleotides Are Tight Binding Inhibitors of Nucleoside Diphosphate Kinase Activity

3′-Phosphorylated Nucleotides Are Tight Binding Inhibitors of Nucleoside Diphosphate Kinase Activity

Ebselen is a potent non-competitive inhibitor of extracellular nucleoside diphosphokinase

Decrease in Nucleoside Diphosphate Kinase (NDPK/nm23) Expression during Hematopoietic Maturation

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