Phosphomannosyl receptors of lysosomal enzymes in cardiac and skeletal muscles of young and old mice

1. 1. The endogenous activity and the binding of high-uptake β-N-acetylglucosaminidase were assayed in the membranes of heart and skeletal muscles of young (2 months) and old (15 months) NMRI-mice (Mus musculus) to evaluate the age-related changes in the phosphomannosyl receptors of lysosomal enzymes in muscular membranes. 2. 2. The total activities of β-N-acctylglucosaminidase were significantly higher in cardiac and skeletal muscles of old than young mice. 3. 3. The total and the specific (inhibited by mannose 6-phosphate) binding of β-N-acetylglucosaminidase to the membranes of cardiac muscle, but not to those of skeletal muscle, were higher in old mice than in young ones. 4. 4. The endogenous activity of β-N-acetylglucosaminidase was significantly higher in the membranes of skeletal muscles of old mice than in those of young mice. The membranes of heart muscles did not show any difference in the endogenous activities. 5. 5. The saturation properties of the binding of β-N-acetylglucosaminidase to the phosphomannosyl receptors were very similar in the membranes of heart and skeletal muscles of both age groups. 6. 6. We conclude that during aging the number of phosphomannosyl receptors of lysosomal enzymes increases in the membranes of heart muscle while the occupancy of phosphomannosyl receptors with endogenous ligands increases in the membranes of skeletal muscle.