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Atypical localization of cytoskeletal and anchoring proteins in the choroid plexus of normal and slc4a10 knockout mice
Author(s) -
Damkier Helle Hasager,
Praetorius Jeppe
Publication year - 2013
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.27.1_supplement.730.12
Subject(s) - ankyrin , spectrin , cytoskeleton , microbiology and biotechnology , epithelial polarity , ezrin , membrane protein , knockout mouse , choroid plexus , biology , apical membrane , chemistry , membrane , biochemistry , receptor , endocrinology , gene , cell , central nervous system
The cellular distribution of membrane proteins in the choroid plexus (CP) is known to differ from other transporting epithelia. The Na,K‐ATPase is atypically located in the luminal membrane and AQP1 is located in both membranes. Genetic deletion of slc4a10 , which encodes the key basolateral Na + loader Ncbe, is known to decrease the abundance of AQP1 and Na, K ATPase and cause a redistribution of ezrin that anchors certain membrane proteins to the cytoskeleton. The aim of the present study was to determine the distribution of known anchoring proteins and cytoskeletal components in CP of normal and NCBE knockout mice by immunohistochemical analysis. A known binding partner of AQP1, β‐catenin, was located only near the basolateral membrane and was less abundant in the NCBE knockout mouse. Ankyrin 3, a known Na,K ATPase anchor in CP was localized near the luminal membrane, but was less abundant in the NCBE knockout mouse. Spectrin cytoskeleton was localized close to the luminal membrane and is known to bind to Ankyrin 3. In the NCBE knockout mouse, spectrin labelling was observed in both membrane domains, however, but predominantly basolaterally. In conclusion, AQP1 in the luminal membrane of CP is not anchored to β‐catenin. Furthermore, the removal of the key Na + loader, NCBE, causes not only a decrease in abundance of the Na, K ATPase binding partner Ankyrin 3, but also a redistribution of the spectrin‐cytoskeleton.