Abstract
Stimulation of resting Chang liver or monkey kidney cells, prelabeled with [ 3H]leucine, by epidermal growth factor (EGF), caused inhibition of cellular protein degradation and a parallel increased nuclear translocation of 3H-labeled non-histone proteins and DNA synthesis. Nuclear translocation of these proteins was independent of protein synthesis. Fractionation of the nuclear 3H-labeled non-histone proteins in a pH gradient of 2.5–6.5 showed that the protein fractions with a high degree of proteolysis in resting cells corresponded to the protein fractions with a high extent of translocation in stimulated cells, suggesting that degradation and translocation of these proteins may be related. EGF inhibited cellular uptake of [ 3H]chloroquine, suggesting that EGF inhibits non-histone protein degradation via the lysosomal pathway. These observations support the hypothesis that EGF induces non-histone protein translocation to the nucleus by inhibiting lysosomal degradation of these proteins.
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