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.
Inoue
Y
Y
Department of Biochemical Science and Technology, Faculty of Agriculture, Kagoshima University, Kagoshima, Japan. inoue@chem.agri.kagoshima-u.ac.jp
Ose
T
T
Mukai
S
S
Ehira
S
S
Yonekura
M
M
Hou
D X
DX
Fujii
M
M
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