Effect of starvation on degradation of rat liver nuclear proteins.
Starvation is characterized by rapid loss in liver weight and proteins. The loss in liver protein is reflected in loss of protein in most organelles including mitochondria, microsomes, and cytosol, with the exception of nuclei. The nuclear proteins increase per unit weight of liver during starvation and this holds true for both histone and non-histone fractions. Comparison of degradation pattern of histone and non-histone fractions with microsomal fraction indicates a significantly different profile. The nuclear proteins reflect a pattern of decreased degradation during starvation. The increase in the activity of lysosomal enzyme cathepsin D measured during this period was indicative of general increase in catabolic processes. However, the nuclear protease activity decreased during this period, suggesting an organelle compartmentation of degradation process.
D000818:Animals; D001639:Bicarbonates / Q000378:metabolism; D002402:Cathepsin D / Q000378:metabolism; D002467:Cell Nucleus / Q000378:metabolism*; D004247:DNA / Q000378:metabolism; D006657:Histones / Q000378:metabolism; D008099:Liver / Q000378:metabolism*; D008297:Male; D008862:Microsomes, Liver / Q000378:metabolism; D010447:Peptide Hydrolases / Q000378:metabolism; D011506:Proteins / Q000378:metabolism*; D051381:Rats; D013217:Starvation / Q000378:metabolism*
D001639:Bicarbonates; D006657:Histones; D011506:Proteins; D004247:DNA; D010447:Peptide Hydrolases; D002402:Cathepsin D