Distribution of ectonucleotidases in the rodent brain revisited
- 9 October 2008
- journal article
- research article
- Published by Springer Science and Business Media LLC in Cell and tissue research
- Vol. 334 (2), 199-217
- https://doi.org/10.1007/s00441-008-0681-x
Abstract
Nucleotides comprise a major class of signaling molecules in the nervous system. They can be released from nerve cells, glial cells, and vascular cells where they exert their function via ionotropic (P2X) or metabotropic (P2Y) receptors. Signaling via extracellular nucleotides and also adenosine is controlled and modulated by cell-surface-located enzymes (ectonucleotidases) that hydrolyze the nucleotide to the respective nucleoside. Extracellular hydrolysis of nucleotide ligands involves a considerable number of enzymes with differing catalytic properties differentially affecting the nucleotide signaling pathway. It is therefore important to investigate which type of ectonucleotidase(s) contributes to the control of nucleotide signaling in distinct cellular and physiological settings. By using a classical enzyme histochemical approach and employing various substrates, inhibitors, and knockout animals, we provide, for the first time, a comparative analysis of the overall distribution of catalytic activities reflecting four ectonucleotidase families: ecto-5′-nucleotidase, alkaline phosphatases, ectonucleoside triphosphate diphosphohydrolases (E-NTPDases), and ectonucleotide pyrophyphatases/phosphodiesterases (E-NPPs). We place into perspective the earlier literature and provide novel evidence for a parenchymal localization of tissue non-specific alkaline phosphatase, E-NPPs, and E-NTPDases in the mouse brain. In addition, we specify the location of ectonucleotidases within the brain vasculature. Most notably, brain vessels do not express ecto-5′-nucleotidase. The preponderance of individual enzymes differs considerably between brain locations. The contribution of all types of ectonucleotidases thus needs to be considered in physiological and pharmacological studies of purinergic signaling in the brain.Keywords
This publication has 84 references indexed in Scilit:
- Biochemical analysis of ecto-nucleotide pyrophosphatase phosphodiesterase activity in brain membranes indicates involvement of NPP1 isoenzyme in extracellular hydrolysis of diadenosine polyphosphates in central nervous systemNeurochemistry International, 2007
- Alkaline PhosphatasesPurinergic Signalling, 2006
- The E-NTPDase family of ectonucleotidases: Structure function relationships and pathophysiological significancePurinergic Signalling, 2006
- Comparative hydrolysis of P2 receptor agonists by NTPDases 1, 2, 3 and 8Purinergic Signalling, 2005
- Ecto‐alkaline phosphatase in NG108‐15 cells : a key enzyme mediating P1 antagonist‐sensitive ATP responseBritish Journal of Pharmacology, 2000
- Ecto‐enzymes and metabolism of extracellular ATPDrug Development Research, 1994
- Morphology and distribution of ecto-5′-nucleotidase-positive cells in the rat choroid plexusJournal of Neurocytology, 1994
- 5′-Nucleotidase in postnatal ontogeny of rat cerebellum: a marker for migrating nerve cells?Developmental Brain Research, 1988
- Localization of Alkaline Phosphatase Activity in Endothelia of Developing and Mature Mouse Blood-Brain BarrierDevelopmental Neuroscience, 1986
- THE EFFECT OF GLUTARALDEHYDE AND FORMALDEHYDE ON THE CALCIUM PUMP OF THE SARCOPLASMIC RETICULUMThe Journal of cell biology, 1967