The production of beta-amyloid precursor protein (beta-APP) in cultured oligodendrocytes isolated from adult bovine brains was examined by immunohistochemistry and immunoblotting. Immunostaining of oligodendrocytes with antibodies specific for the carboxy terminus of beta-APP demonstrated positive immunoreactivity of oligodendroglial cytoplasm. Immunoblot analysis of cellular extracts detected two distinct bands with estimated molecular weight of 118 and 105 kDa. The amount of these beta-APP subspecies increased considerably in response to their attachment to the poly-L-lysine substratum.