Elsevier

Neuropharmacology

Volume 36, Issue 9, September 1997, Pages 1277-1283
Neuropharmacology

Review
Tissue distribution of the P2X7 receptor

https://doi.org/10.1016/S0028-3908(97)00140-8Get rights and content

Abstract

The P2X7 receptor is a bifunctional molecule. The binding of ATP induces within milliseconds the opening of a channel selective for small cations, and within seconds a larger pore opens which allows permeation by molecules as large as propidium dyes (629 Da). In situ hybridization using a digoxigeninlabelled riboprobe, and immunohistochemistry using an antibody raised against a C-terminal peptide sequence, were used to determine the distribution of the P2X7 receptor mRNA and protein in rat and mouse tissues and cell lines. The brain of newborn rats showed a 6 kb RNA by Northern blotting, but this was not detectable in adult brain. By in situ hybridization and immunohistochemistry, there was heavy labelling of ependymal cells in both newborn and adult brain, but the brain parenchyma showed no labelling. However, P2X7 receptor-immunoreactive cells appeared in the penumbral region around an area of necrosis evoked by prior occlusion of the middle cerebral artery, suggesting expression of the receptor by activated microglia. NTW8 cells, a mouse microglial cell line, strongly expressed the P2X7 receptor mRNA and protein. The P2X7 receptor mRNA and protein were also observed in the majority of bone marrow cells, including those separately identified by their expression of other antigens as granulocytes, monocyte/macrophages and B lymphocytes. The expression of P2X7 receptor by brain macrophages rather than neurons would be consistent with a role in brain repair following inflammation, infarction or immune insult.

References (33)

  • G. Buell et al.

    An antagonist-insensitive P2X receptor expressed in epithelia and brain

    EMBO Journal

    (1996)
  • S. Cockcroft et al.

    ATP induces nucleotide permeability in rat mast cells

    Nature

    (1979)
  • G. Collo et al.

    Cloning of P2X5 and P2X6 receptors, and the distribution and properties of an extended family of ATP-gated ion channels

    Journal of Neuroscience

    (1996)
  • R. Dahlqvist et al.

    Interactions of ATP and calcium on the rat mast cell: effects on histamine release

    Acta Physiologica Scandinavia

    (1974)
  • R.J. Evans et al.

    Pharmacological characterization of heterologously expressed ATP-gated cation channels (P2X-purinoceptors)

    Molecular Pharmacology

    (1995)
  • S. Falzoni et al.

    The purinergic receptor P2Z of human macrophage cells. Characterization and possible physiological role

    Journal of Clinical Investigation

    (1995)
  • Cited by (0)

    View full text