Changes in immunoelectron microscopic localization of cathepsin D in muscle induced by conditioning or high-pressure...

Changes in the localization of cathepsin D in postmortem and pressurized rabbit muscles were investigated by immunoelectron microscopy. The anti-cathepsin D monoclonal antibody strongly labeled a large vesicle in a subsarcolemmal part of the cell , which strongly suggests that this is the primary lysosome. The liberation of the cathepsin D entrapped in the lysosomes in the muscle prepared immediately after death proceeded with the progress of the conditioning. The release of almost all cathepsin D from the lysosomes and its absorption on the myofibrils were observed in the muscle conditioned for 14 days. The accumulation of lysosomes having various volumes and shapes accompanied with the disruption of myofibrillar structure was also observed. The liberation of cathepsin D from the lysosomes can be attributed to the modification of membranes permeability of the lysosomes during conditioning. When the muscle was pressurized at 100 MPa, the modification of the round shape of the lysosome was observed. With the increase of the pressure applied to the muscle, the release of cathepsin D from the lysosome due to the disruption of membrane was accelerated, and absorption of the released cathepsin D on the myofibrils was observed. From the results obtained, it was clear that the changes in the localization of cathepsin D accompanied with the modification of lysosomes induced by the brief exposure to high pressure were drastic in comparison with that in the muscle during conditioning.