Inhibition of the acid lipase activity by apolipoprotein A-I in the presence of lysosomal proteases.
It was found that the inhibition of the lysosomal acid lipase activity by rat apolipoprotein A-I (apo A-I) was increased with the degradation of apo A-I by the lysosomal proteases. We demonstrated that apo A-I could effectively inhibit the acid lipase activity even in the presence of the lysosomal proteases using the hepatic lysosomal fraction.
Department of Biochemical Science and Technology, Faculty of Agriculture, Kagoshima University, Kagoshima, Japan. inoue@chem.agri.kagoshima-u.ac.jp
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Y
Inoue
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Ose
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Mukai
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Ehira
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Yonekura
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Hou
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Fujii
D000818:Animals; D016632:Apolipoprotein A-I / Q000097:blood / Q000502:physiology*; D002852:Chromatography, Ion Exchange; D004591:Electrophoresis, Polyacrylamide Gel; D010450:Endopeptidases / Q000378:metabolism*; D008049:Lipase / Q000037:antagonists & inhibitors*; D008247:Lysosomes / Q000201:enzymology*; D051381:Rats
D016632:Apolipoprotein A-I; D008049:Lipase; D010450:Endopeptidases