Regulatory mechanisms of intracellular proteolysis in mammalian cells.
Low molecular weight phosphoryl compounds, such as carbamoyl phosphate, 2,3-diphosphoglycerate and phytic acid protect, to different extents, mitochondrial and cytosolic proteins such as ornithine transcarbamoylase (OTC), carbamoyl phosphate synthetase (CPS), glutamate dehydrogenase (GDH) and glyceraldehyde 3-phosphate dehydrogenase (GAPDH), from proteolytic inactivation (rat liver lysosomal extracts, pronase, elastase). Given the wide variety and common occurrence of low molecular weight reagents such as typified here, it seems that this kind of inhibition may be important in the regulation of protein turnover. Regulation of intracellular proteolysis can also occur via the proteolytic systems. Immunocytochemical procedures for mitochondrial enzymes (CPS, GDH, OTC), show intracellular homogeneity, but intercellular heterogeneity in rat liver, compatible with a role of the autophagic-lysosomal system in degrading these proteins. However, degradation of short-lived proteins occurs by other mechanisms. Using centrifugation of cultured cells, we find that the Golgi apparatus takes part in the degradation of these proteins, probably by controlling the traffic of proteins or proteases to the degradation site.
D000818:Animals; D001711:Biotransformation; D002478:Cells, Cultured; D006056:Golgi Apparatus / Q000378:metabolism; D006367:HeLa Cells; D006801:Humans; D006868:Hydrolysis; D007120:Immunochemistry; D008854:Microscopy, Electron; D010447:Peptide Hydrolases / Q000378:metabolism*; D011506:Proteins / Q000378:metabolism; D051381:Rats
D011506:Proteins; D010447:Peptide Hydrolases