Two-Dimensional Electrophoretic Analysis of Nuclear Acidic Proteins in Senescent Human Diploid Cells

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Abstract
Nuclear acidic proteins solubilized from young and senescent human diploid fibroblasts were analyzed by 2-dimensional gel electrophoresis. The age-related increase in nuclear proteins was due mainly to the accumulation of residual acidic proteins. Differences in 7 major nuclear acidic proteins between young and senescent cells were observed. [35S]-methionine autoradiography showed that senescent cells had lost the ability to synthesize detectable amounts of 4 major proteins that are found in young cells. Senescent cells synthesized 2 new major proteins that were undetectable in young cells. The isoelectric point of a single polypeptide with the MW 37,000 seemed to shift from 5.3 to 5.8 with cellular aging.