Distribution of plectin, an intermediate filament‐associated protein, in the adult rat central nervous system

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Abstract
Plectin is a high molecular weight protein originally identified and characterized as a major cytoskeletal component of the C6 rat glioma cell. Here we demonstrate by immunoblotting of crude intermediate filament (IF) protein preparations that plectin is a cytoskeleton‐associated component of the rat spinal cord. We then used avidin‐biotin peroxidase immunocytochemistry and indirect immunofluorescence to localize plectin within the adult rat central nervous system (CNS) and examine its distribution with respect to IF proteins. Plectin immunoreactivity is localized to all ependymal cells including the choroidal epithelial cells and tanycytes, Bergmann glial processes, radially oriented glial cells in the spinal cord, astrocytes in white matter, a subset of astrocytes in gray matter, a subset of motoneurons in the brainstem and spinal cord, and certain endothelial cells. Colocalization studies with neural If proteins show that plectin has a unique distribution pattern which most closely resembles, but is distinct from, that of vimentin. The few plectin positive neurons invariably also contain the neurofilament triplet proteins and peripherin, so that the ability of plectin to bind to the triplet proteins in vitro may reflect an in vivo interaction. The predominance of plectin at the inner ventricular boundaries of the nervous system as well as at the blood‐brain barrier is in line with the pattern of plectin expression in other tissues and suggests a general role for plectin in the maintenance of such junctional regions.