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Biochemical Effects of High Hydrostatic Pressure on the Lysosome and Proteases Involved in It
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1992
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Protein SecretionHigh Hydrostatic PressureCytoskeletonProtein Phase SeparationBiochemical EffectsAcid PhosphataseProtein FoldingHigh PressureProteomicsProteases InvolvedBiophysicsBiochemistryLiver PhysiologyLysosome BiologyBiophysical AspectProtein PhosphorylationNatural SciencesPhysiologyCellular BiochemistryMetabolismMedicineLysosome Membranes
High pressure at 101.3 to 506.6 MPa was applied to bovine liver and fractioned lysosomes to examine its effects on the lysosomes and the enzymes involved. Carboxypeptidase was completely inactivated at 405.3 MPa. The activities of about 60, 70, 30, and 50% of acid phosphatase and cathepsins B, D, and H, respectively, remained after pressurization at 506.6 MPa. Pressurization of the liver at 506.6 MPa or lower caused changes in the subcellular distribution of lysosomal enzymes. Acid phosphatase and cathepsins B and H were released from fractioned lysosome by treatment higher than 202.7 MPa and cathepsin D at 101.3 MPa. These findings indicate that high pressure at 101.3 to 202.7 MPa induces destruction of the lysosome membranes and leakage of the lysosomal enzymes.