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CD39 as a Caveolar-Associated Ectonucleotidase

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Abstract

CD39 is a human lymphoid cell activation antigen, (also referred to E-ATPDase or apyrase) that hydrolyzes extracellular ATP and ADP. Although it has been widely studied, its physiological role, however, still remains unclear. This ectonucleotidase generally is said to be evenly distributed in the membrane of the cells. However, we observed that in cell types which possess caveolae, specialised membrane invaginations involved in signalling, CD39 is preferentially targeted to these membrane microdomains. Since all molecules involved in signalling (eNOS, G-proteins, receptors) which are targeted to the caveolae undergo posttranslational modifications (e.g., palmitoylation) we hypothesize the same to be the case for CD39. Furthermore, its presence in the caveolae supports its participation in signalling events.

References (29)

  • T.F. Wang et al.

    Brain Res.

    (1998)
  • B. Sperlágh et al.

    Neuroscience

    (1995)
  • L. Plesner

    Int. Rev. Cytol.

    (1995)
  • A.J. Marcus et al.

    J. Lipid. Res.

    (1993)
  • M. Komoszynski et al.

    Biochim. Biophys. Acta

    (1996)
  • E. Kaczmarek et al.

    J. Biol. Chem.

    (1996)
  • A.L. Kiss et al.

    Cell Biol. Int.

    (1995)
  • O. Feron et al.

    J. Biol. Chem.

    (1996)
  • O. Feron et al.

    J. Biol. Chem.

    (1998)
  • O. Feron et al.

    Life Sci.

    (1999)
  • J.A. Engelman et al.

    FEBS Lett.

    (1998)
  • J. Couet et al.

    J. Biol. Chem.

    (1997)
  • O. Feron et al.

    J. Biol. Chem.

    (1997)
  • Y. Kim et al.

    Biochim. Biophys. Acta

    (1999)
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    Abbreviations used: ecto-NTPDase, ecto-nucleoside-triphosphate-diphosphohydrolase; E-ATPDase, ecto-adenosine-triphosphate-diphosphohydrolase; E-ATPase, ecto-adenosine-triphosphatase; HUVEC, human umbilical vein endothelial cell; eNOS, endothelial nitrogen-monoxide synthase

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