Tissue distribution, purification and characterization of rat phosphatidylinositol transfer protein.

Phosphatidylinositol transfer activity is measured in cytosol fractions prepared from 13 rat tissues; specific activity is highest in brain and lowest in adipose and skeletal muscle. Based upon electrophoretic analysis phosphatidylinositol transfer protein is purified to homogeneity from whole rat brain. The protein has a molecular weight of 36,000 and exists as a mixture of species having isoelectric points of 4.9 and 5.3. In a vesicle-vesicle assay system, the intermembrane transfer rate is greatest for phosphatidylinositol and less by a factor of 2 for phosphatidylcholine; transfer of phosphatidylethanolamine, phosphatidylserine or sphingomyelin is not observed. Using a polyclonal rabbit antibody against bovine phosphatidylinositol transfer protein, immunologic cross-reactivity is noted between the rat protein and other mammalian phosphatidylinositol transfer proteins. A strong correlation is established between a tissue's capacity for phosphatidylinositol transfer and the amount of immunoreactive transfer protein seen in that tissue. Purified phosphatidylinositol transfer protein is capable of transporting newly synthesized phosphatidylinositol molecules from rat brain microsomes to small unilamellar phospholipid vesicles. The results are discussed within the context of cellular phosphoinositide metabolism and the maintenance of the metabolically responsive pool of phosphatidylinositol in the plasma membrane.