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An. R. Acad. Nac. Farm., 2007, 73: 537-566

                                      Sesiones

       Ecto-nucleotidases, molecular properties
                     and functional impact

                        Recibido el 15 de marzo de 2007

         HERBERT ZIMMERMANN *, SANTOSH K. MISHRA,
      VARSHA SHUKLA, DAVID LANGER, KRISTINE GAMPE,

         IVETTE GRIMM, JASMIN DELIC, NORBERT BRAUN
      Institute for Cell Biology and Neuroscience. Biocenter, J. W.

              Goethe-University. Frankfurt am Main, Germany.

                                                   ABSTRACT

    Ecto-nucleotidases hydrolyze extracellular nucleotides. Nucleotides are amongst
the most ubiquitous messenger substances in the vertebrate body. Receptors for
nucleotides are expressed on the surface of essentially every cell and many cells
carry several types of nucleotide receptors. Several families of ecto-nucleotidases
have been identified that differ in tissue distribution and functional properties.
They modulate ligand availability at nucleotide and adenosine receptors. Ecto-
nucleotidases were first identified in the 1940ies. Work of the past two decades has
unraveled molecular identities and important functional properties. Using targeted
gene deletion clear examples highlighting the importance of ecto-nucleotidases in

    Discurso de ingreso como Académico Correspondiente de la Real Academia Nacio-
nal de Farmacia.

    * Contact Information:
    Dr. Herbert Zimmermann.
    Institute for Cell Biology and Neuroscience. Biocenter, J.W. Goethe-University. Max-
von-Laue-Str. 9. D-60438 Frankfurt am Main, Germany. Tel: 069 798 29602. FAX: 069
798 29606.
    E-mail: h.zimmermann@bio.uni-frankurt.de
    Abbreviations: ApnA, dinucleoside polyphosphate; ART, ADP-ribosyltransferase;
NADase, NAD glycohydrolases; E-NTPDase, ecto-nucleoside triphosphate diphospho-
hydrolase; E-NPP, ecto-nucleotide pyrophosphatase/phosphodiesterase; IAP, intestinal
alkaline phosphatase; PC-1, plasma cell differentiation antigen-1; SVZ, subventricular
zone; TNAP, tissue nonspecific form of alkaline phosphatase.

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