Differential axial localization along the mouse brain vascular tree of luminal sodium-dependent glutamine transporters Snat1 and Snat3.

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  • Author(s): Ruderisch N;Ruderisch N; Virgintino D; Makrides V; Verrey F
  • Source:
    Journal of cerebral blood flow and metabolism : official journal of the International Society of Cerebral Blood Flow and Metabolism [J Cereb Blood Flow Metab] 2011 Jul; Vol. 31 (7), pp. 1637-47. Date of Electronic Publication: 2011 Mar 02.
  • Publication Type:
    Journal Article; Research Support, Non-U.S. Gov't
  • Language:
    English
  • Additional Information
    • Source:
      Publisher: SAGE Publications Country of Publication: United States NLM ID: 8112566 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1559-7016 (Electronic) Linking ISSN: 0271678X NLM ISO Abbreviation: J Cereb Blood Flow Metab Subsets: MEDLINE
    • Publication Information:
      Publication: 2016- : Thousand Oaks, CA : SAGE Publications
      Original Publication: New York : Raven Press, c1981-
    • Subject Terms:
      Amino Acid Transport System A/*analysis ; Amino Acid Transport Systems, Neutral/*analysis ; Blood-Brain Barrier/*cytology ; Brain/*blood supply ; Endothelial Cells/*metabolism; Amino Acid Transport System A/metabolism ; Amino Acid Transport Systems, Neutral/metabolism ; Animals ; Blood-Brain Barrier/metabolism ; Blood-Brain Barrier/ultrastructure ; Brain/metabolism ; Endothelial Cells/ultrastructure ; Female ; Mice ; Mice, Inbred C57BL
    • Abstract:
      A specialized brain vasculature is key for establishing and maintaining brain interstitial fluid homeostasis, which for most amino acids (AAs) are ∼10% plasma levels. Indeed, regulation of AA homeostasis seems critical for normal central nervous system functions, and disturbances in brain levels have both direct and indirect roles in several neuropathologies. One mechanism contributing to the plasma to brain AA gradients involves polarized expression of solute carrier (SLC) family transporters on blood-brain barrier (BBB) endothelial cells. Of particular interest is the localization of sodium-dependent transporters that can actively move substrates against their concentration gradient. In this study, the in vivo endothelial membrane localization of the sodium-dependent glutamine transporters Snat3 (Slc38a3) and Snat1 (Slc38a1) was investigated in the mouse brain microvasculature using immunofluorescent colocalization with cellular markers. In addition, luminal membrane expression was probed by in vivo biotinylation. A portion of both Snat3 and Snat1 vascular expressions was localized on luminal membranes. Importantly, Snat1 expression was restricted to larger cortical microvessels, whereas Snat3 was additionally expressed on BBB capillary membranes. This differential expression of system A (Snat1) versus system N (Snat3) transporters suggests distinct roles for Snats in the cerebral vasculature and is consistent with Snat3 involvement in net transendothelial BBB AA transport.
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    • Accession Number:
      0 (Amino Acid Transport System A)
      0 (Amino Acid Transport Systems, Neutral)
      0 (Slc38a1 protein, mouse)
      0 (system N protein 1)
    • Publication Date:
      Date Created: 20110303 Date Completed: 20110912 Latest Revision: 20211020
    • Publication Date:
      20221213
    • Accession Number:
      PMC3137466
    • Accession Number:
      10.1038/jcbfm.2011.21
    • Accession Number:
      21364602