@article {45952, title = {Galectin-3 is associated with the plasma membrane of lens fiber cells.}, journal = {Investigative Ophthalmology \& Visual Science}, volume = {41}, year = {2000}, month = {2000 Jan}, pages = {199-203}, abstract = {

PURPOSE: To discover proteins that have the potential to contribute to the tight packing of fiber cells in the lens.

METHODS: Crude fiber cell membranes were isolated from ovine lens cortex. Proteins were separated by two-dimensional gel electrophoresis, and selected protein spots identified by micro-sequencing. The identification of galectin-3 was confirmed by immunoblotting with a specific antibody. The association of galectin-3 with the fiber cell plasma membrane was investigated using immunofluorescence microscopy, solubilization trials with selected reagents, and immunoprecipitation to identify candidate ligands.

RESULTS: A cluster of three protein spots with an apparent molecular weight of 31,000 and isoelectric points ranging between 7 and 8.5 were resolved and identified as galectin-3. This protein was associated peripherally with the fiber cell plasma membrane and interacted with MP20, an abundant intrinsic membrane protein that had been identified previously as a component of membrane junctions between fiber cells.

CONCLUSIONS: The detection of galectin-3 in the lens is a novel result and adds to the growing list of lens proteins with adhesive properties. Its location at the fiber cell membrane and its association with the junction-forming MP20 is consistent with a potential role in the development or maintenance of the tightly packed lens tissue architecture.

}, keywords = {Amino Acid Sequence, Animals, Antigens, Differentiation, Cell Membrane, Chromatography, High Pressure Liquid, Electrophoresis, Gel, Two-Dimensional, Eye Proteins, Galectin 3, Immunoblotting, Lens Cortex, Crystalline, Ligands, Membrane Glycoproteins, Microscopy, Fluorescence, Molecular Sequence Data, Rabbits, Sequence Homology, Amino Acid, Sheep}, issn = {0146-0404}, author = {Gonen, T and Donaldson, P and Kistler, J} }