Glycolipid-binding proteins.

Proteins which bind glycolipids with high specificity are tentatively divided into two groups. One group consists of activator proteins involved in the catabolism of glycolipids by acid lysosomal hydrolases. Two activator proteins, GM2-activator and sphingolipid activator protein-1, are critically appraised on their glycolipid-binding properties and on their activity to facilitate the transfer of glycolipids. These proteins are glycoproteins localized in the lysosomes. Their molecular weights are in a range of 21 000-27 000, and isoelectric points are 4-5. Glycolipid transfer protein (GLTP) is included in the other group. GLTP purified from pig brain has a molecular weight of about 20 000 and an isoelectric point of 8.3. GLTP facilitates the transfer of various glycosphingolipids and glyceroglycolipids between membranes. The protein does not facilitate the transfer of phospholipids or cholesterol. GLTP binds galactosylceramide. The galactosylceramide-GLTP complex participates in the transfer reaction as the intermediate. Each protein in both groups binds glycolipids with a characteristic specificity to the sugar moiety. A stoichiometry of 1 mol of lipid per mol of protein has been found in all three proteins. Proteins in both groups seem to have a hydrophobic region on their surface, since all three proteins have been efficiently purified by hydrophobic chromatography.