Chapter 30 Ecto-nucleotidases—molecular structures, catalytic properties, and functional roles in the nervous system

https://doi.org/10.1016/S0079-6123(08)63570-0Get rights and content

Publisher Summary

This chapter discusses the molecular structures, catalytic properties, and functional roles of ecto-nucleotidases in the nervous system. Only one ecto-5’-nucleotidase gene is known in vertebrates. Ecto-5’-nucleotidase plays a critical role in the extracellular hydrolysis cascade of nucleotides and in neural development. Several families of ectonucleotidases function in the nervous system. They differ in their catalytic and other functional properties and consist of several members each. The chapter presents that nucleotidergic signaling pathways are widely distributed in the nervous system and that the ecto-nucleotidases play a significant part in it. The functional properties of the presently known ecto-nucleotidases and also of the sequenced but uncharacterized potential ecto-nucleotidases need to be investigated. An evaluation of their role in defined signaling pathways requires that the cellular location of the enzymes is determined. Knock-out mice in which individual ecto-nucleotidases have been deleted from the germline promise to be important tools to unravel their functional roles in the nervous system and also in other tissues.

References (93)

  • D. Ferrari et al.

    ATP-mediated cytotoxicity in microglial cells

    Neuropharmacology

    (1997)
  • L. Glaser et al.

    Uridine diphosphate sugar hydrolase. Purification of enzyme and protein inhibitor

    J. Biol. Chem.

    (1967)
  • E.J.M. Grondal et al.

    Monospecific antiserum against 5′-nucleotidase from Torpedo electric organ: Immunocytochemical destribution of the enzyme and its association with Schwann cell membranes

    Neuroscience

    (1988)
  • M. Handa et al.

    Purification and cloning of a soluble ATP-diphosphohydrolase (apyrase) from potato tubers (Solanum tuberosum)

    Biochem. Biophys. Res. Commun.

    (1996)
  • P. Jin-Hua et al.

    Molecular cloning and chromosomal localization of PD-Ib (PDNP3), a new member of the human phosphodiesterase I genes

    Genomics

    (1997)
  • E. Kaczmarek et al.

    Identification and characterization of CD39 vascular ATP diphosphohydrolase

    J. Biol. Chem.

    (1996)
  • H. Kawagoe et al.

    Molecular cloning and chromosomal assignment of the humans brain-type phosphodiesterase I/nucleotide pyrophosphatase gene

    (PDNP2). Genomics

    (1995)
  • E.J. Kidd et al.

    Evidence for P2X3 receptors in the developing rat brain

    Neuroscience

    (1998)
  • T.L. Kirley

    Complementary DNA cloning and sequencing of the chicken muscle Ecto-ATPase—Homology with the lymphoid cell activation antigen CD39

    J. Biol. Chem.

    (1997)
  • K. Kohring et al.

    Upregulation of ecto-5′-nucleotidase in human neuroblastoma SH-SY5Y cells on differentiation by retinoic acid or phorbolester

    Neurosci. Lett.

    (1998)
  • J.F. Laliberte et al.

    Sequential hydrolysis of the γ- and β-phosphate groups of ATP by the ATP diphosphohydrolase from pig pancreas

    Biochim. Biophys. Acta

    (1983)
  • H.Y. Lee et al.

    Stimulation of tumor cell motility linked to phosphodiesterase catalytic site of autotaxin

    J. Biol. Chem.

    (1996)
  • J. Murata et al.

    cDNA cloning of the human motility-stimulating protein, autotaxin, reveals a homology with phosphodiesterases

    J. Biol. Chem.

    (1994)
  • W. Nacimiento et al.

    Cytochemistry of 5′-nucleotidase in the superior cervical ganglion of the rat: Effects of pre- and postganglionic axotomy

    Exptl. Neurol.

    (1990)
  • A.K. Nagy et al.

    Molecular cloning of the chicken oviduct ecto-ATP-diphosphohydrolase

    J. Biol. Chem.

    (1998)
  • M. Narita et al.

    Molecular cloning, expression and localization of a brain-specific phosphodiesterase I/nucleotide pyrophosphatase (PD-Iα) from rat brain

    J. Biol. Chem.

    (1994)
  • M. Picher et al.

    Hydrolysis of P2-purinoceptor agonists by a purified ectonucleotidase from the bovine aorta, the ATP- diphosphohydrolase

    Biochem. Pharmacol.

    (1996)
  • L. Plesner

    Ecto-ATPases: Identities and functions

    Int. Rev. Cytol.

    (1995)
  • S.W. Schoen et al.

    Synaptic 5′-nucleotidase activity reflects lesion-induced sprouting within the adult dentate gyrus

    Exp. Neurol.

    (1994)
  • S.W. Schoen et al.

    Evidence that 5′-nucleotidase is associated with malleable synapses—An enzyme cytochemical investigation of the olfactory bulb of adult rats

    Neuroscience

    (1995)
  • S.W. Schoen et al.

    5′-Nucleotidase in postnatal ontogeny of rat cerebellum: A marker for migrating nerve cells?

    Develop. Brain. Res.

    (1988)
  • T.M. Smith et al.

    Cloning, sequencing and expression of a human brain ecto-apyrase related to both the ecto-ATPases and CD39 ecto-apyrases

    Biochim. Biophys. Acta

    (1998)
  • Z.M. Song et al.

    Characterization of alkaline phosphatase-reactive neurons in the guinea-pig small intestine

    Neuroscience

    (1994)
  • B. Sperlagh et al.

    ATP acts as fast neurotransmitter in rat habenula: Neurochemical and enzymecytochemical evidence

    Neuroscience

    (1995)
  • U. Stochaj et al.

    Evidence for the direct interaction af chicken gizzard 5′-nucleotidase with laminin and fibronectin

    Biochim. Biophys. Acta

    (1989)
  • M.L. Stracke et al.

    Identification, purification and partial sequence analysis of autotaxin, a novel motility-stimulating protein

    J. Biol. Chem.

    (1992)
  • H. Takemoto et al.

    Conditioned media of glial cell lines induce alkaline phosphatase activity in cultured artery endothelial cells—Identification of interleukin-6 as an induction factor

    FEBS. Lett.

    (1994)
  • J.A. Thorn et al.

    Adenosine transporters

    Gen. Pharmacol.

    (1996)
  • T.F. Wang et al.

    CD39 is an ecto-(Ca2+,Mg2+)-apyrase

    J. Biol. Chem.

    (1996)
  • T.F. Wang et al.

    Golgi localization and functional expression of human uridine diphosphatase

    J. Biol. Chem.

    (1998)
  • T.F. Wang et al.

    Characterization of brain ecto-apyrase: Evidence for only one ecto-apyrase (CD39) gene

    Mol. Brain. Res.

    (1997)
  • P. Willadsen et al.

    The nucleotidase of Boophilus microplus and its relationship to enzymes from the rat and Escherichia coli

    Insect. Biochem. Mol. Biol.

    (1993)
  • S. Zhuo et al.

    Mutational analysis of a Ser/Thr phosphatase—Identification of residues important in phosphoesterase substrate binding and catalysis

    J. Biol. Chem.

    (1994)
  • H. Zimmermann

    Biochemistry, localization and functional roles of ecto-nucleotidases in the nervous system

    Prog. Neurobiol.

    (1996)
  • C. Abeijon et al.

    Guanosine diphosphatase is required for protein and sphingo-lipid glycosylation of Saccharomyces cerevisiae

    J. Cell. Biol.

    (1993)
  • Y. Bailly et al.

    5′-Nucleotidase activity as a synaptic marker of parasagittal compartmentation in the mouse cerebellum

    J. Neurocytol.

    (1995)
  • Cited by (0)

    View full text