Organisation of extracellular matrix proteins laminin and agrin in pericapillary basal laminae in mouse brain.

Organisation of extracellular matrix proteins laminin and agrin in pericapillary basal laminae in mouse brain. Brain Struct Funct. 2020 Feb 18;: Authors: Hoddevik EH, Rao SB, Zahl S, Boldt HB, Ottersen OP, Amiry-Moghaddam M Abstract Evidence suggests that extracellular matrix molecules of perivascular basal laminae help orchestrate the molecular assemblies at the gliovascular interface. Specifically, laminin and agrin are thought to tether the dystrophin-associated protein (DAP) complex to the astrocytic basal lamina. This complex includes α-syntrophin (α-Syn), which is believed to anchor aquaporin-4 (AQP4) to astrocytic endfoot membrane domains. We have previously shown that the size of the perivascular AQP4 pool differs considerably between brain regions in an α-Syn-dependent manner. Also, both AQP4 and α-Syn occur at higher densities in endfoot membrane domains facing pericytes than in endfoot membrane domains facing endothelial cells. The heterogeneous distribution of AQP4 at the regional and capillary level has been attributed to a direct interaction between AQP4 and α-Syn. This would be challenged (1) if the microdistributions of laminin and agrin fail to align with those of DAP and AQP4 and (2) if targeted deletion of α-Syn leads to a loss of laminin and/or agrin. Here, we provide the first detailed and quantitative analysis of laminin and agrin in brain basal laminae of mice. We show that the microdistributions of these...
Source: Brain Structure and Function - Category: Neuroscience Authors: Tags: Brain Struct Funct Source Type: research