Two-dimensional gel electrophoresis of human lens epithelium: a study of spatial protein patterns and aging.
The polypeptides in portions of human lens epithelium from individuals of various ages were resolved by two-dimensional (2D) gel electrophoresis. The epithelium was divided into a central area of 12.5 mm2, a surrounding area of 50.2 mm2, and an area which was outside of this region. The proteins were solubilized in urea and run on gels to determine if differences existed in the major polypeptides of the lens epithelium with regard to position in the lens as well as if differences might occur with age. The patterns obtained were remarkably similar in regions of the epithelium examined. The results also demonstrated that the composition of the major polypeptides were not substantially altered in the adult epithelium with age. Two-dimensional gels of proteins from a 3-month-old specimen prepared in a manner similar to that used during extracapsular cataract extraction were also similar to the other samples; however, this sample contained slightly increased staining of proteins greater than 30 kD.
Russell
P
P
National Eye Institute, National Institutes of Health, Bethesda, MD 20892.
D000328:Adult; D000368:Aged; D000369:Aged, 80 and over; D000375:Aging / Q000378:metabolism*; D015153:Blotting, Western; D003459:Crystallins / Q000032:analysis*; D015180:Electrophoresis, Gel, Two-Dimensional; D004848:Epithelium / Q000737:chemistry; D006801:Humans; D007223:Infant; D007908:Lens, Crystalline / Q000737:chemistry*; D008875:Middle Aged; D010455:Peptides / Q000032:analysis
D003459:Crystallins; D010455:Peptides