4.6 Article

Deletion of aquaporin-4 changes the perivascular glial protein scaffold without disrupting the brain endothelial barrier

Journal

GLIA
Volume 60, Issue 3, Pages 432-440

Publisher

WILEY
DOI: 10.1002/glia.22277

Keywords

AQP4; astrocytes; blood-brain barrier; endfeet; syntrophin

Categories

Funding

  1. US National Institutes of Health (NIH) [NS33145]
  2. Research Council of Norway
  3. Letten Foundation

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Expression of the water channel aquaporin-4 (AQP4) at the bloodbrain interface is dependent upon the dystrophin associated protein complex. Here we investigated whether deletion of the Aqp4 gene affects the molecular composition of this protein scaffold and the integrity of the bloodbrain barrier. High-resolution immunogold cytochemistry revealed that perivascular expression of a-syntrophin was reduced by 60% in Aqp4-/- mice. Additionally, perivascular AQP4 expression was reduced by 88% in a-syn-/- mice, in accordance with earlier reports. Immunofluorescence showed that Aqp4 deletion also caused a modest reduction in perivascular dystrophin, whereas beta-dystroglycan labeling was unaltered. Perivascular microglia were devoid of AQP4 immunoreactivity. Deletion of Aqp4 did not alter the ultrastructure of capillary endothelial cells, the expression of tight junction proteins (claudin-5, occludin, and zonula occludens 1), or the vascular permeability to horseradish peroxidase and Evans blue albumin dye. We conclude that Aqp4 deletion reduces the expression of perivascular glial scaffolding proteins without affecting the endothelial barrier. Our data also indicate that AQP4 and a-syntrophin are mutually dependent upon each other for proper perivascular expression. (C) Wiley Periodicals, Inc.

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