Abstract
Upon permeabilization of Swiss mouse 3T3 fibroblasts, an isoform of phosphatidylinositol transfer protein (PI-TP) was preferentially retained, a major part of which was associated with the perinuclear Golgi system (K. J. de Vries, A. Momchilova-Pankova, G. T. Snoek, and K. W. A. Wirtz,Exp. Cell Res.215, 109–113, 1994). In the present study, the intracellular localization of this isoform (PI-TPβ) and the regular form (PI-TPα) was investigated in fetal bovine heart endothelial cells by microinjection of fluorescently labeled analogs followed by confocal laser scanning microscopy. The PI-TPα and PI-TPβ used were purified from bovine brain cytosol and covalently labeled with sulfoindocyanine dyes. By this novel method it was found that PI-TPβ was preferentially associated with perinuclear membrane structures whereas PI-TPα was predominantly present in the nucleus and in the cytoplasm. This intracellular localization was confirmed by indirect immunofluorescence indicating that the fluorescently labeled PI-TPα and PI-TPβ were targeted to the same sites as their endogeneous counterparts.
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