Effect of Glycyrrhizin on Lysosomes Labilization by Phospholipase A2

1986 ◽  
Vol 14 (03n04) ◽  
pp. 131-137 ◽  
Author(s):  
Yasuko Shiki ◽  
Yo Ishikawa ◽  
Kohji Shirai ◽  
Yasushi Saito ◽  
Sho Yoshida
Keyword(s):  
Acid Phosphatase ◽  
Phospholipase A2 ◽  
Rat Liver ◽  
Lysosomal Membrane ◽  
Phospholipase A ◽  
Ph Optimum ◽  
Liver Lysosomes ◽  
Inhibited Acid ◽  
Rat Liver Lysosomes

The influence of glycyrrhizin on the effect of phospholipase A2 on lysosomes was studied. Treatment of rat liver lysosomes with venom phospholipase A2 caused release of acid phosphatase. This release of acid phosphatase was inhibited by 0.1 mM glycyrrhizin. Glycyrrhizin also inhibited acid phospholiase A2 with pH optimum of 4.5, which is thought to be present in the lysosomal membrane. These results suggests that glycyrrhizin stabilizes lysosomes by inhibiting phospholipase A2 activity in the lysosomal membrane.

scholarly journals The permeability of lysosomes to sugars. Effect of diethylstilbestrol on the osmotic activation of lysosomes induced by glucose

1989 ◽  
Vol 262 (3) ◽  
pp. 981-984 ◽  
Author(s):  
M Jadot ◽  
S Wattiaux-De Coninck ◽  
R Wattiaux
Keyword(s):  
Plasma Membrane ◽  
Glucose Transport ◽  
Rat Liver ◽  
Lysosomal Membrane ◽  
Liver Lysosomes ◽  
Unspecific Binding ◽  
Rat Liver Lysosomes

We have investigated the effect on the osmotic activation of rat liver lysosomes, by glucose penetration, of different substances known to inhibit the glucose transport through the plasma membrane. Diethylstilbestrol is the most efficient, particularly when purified lysosomes are used. It has no effect on osmotic activation induced by hypo-osmotic sucrose or by iso-osmotic KCl. It is proposed that diethylstilbestrol reacts with specific sites involved in the glucose translocation through the lysosomal membrane. These sites could not be identified by binding experiments, presumably owing to the considerable unspecific binding of the compound to the membrane.

Isolation and sequencing of a cDNA clone encoding acid phosphatase in rat liver lysosomes

1989 ◽  
Vol 162 (3) ◽  
pp. 1044-1053 ◽  
Author(s):  
Masaru Himeno ◽  
Hideaki Fujita ◽  
Youichiro Noguchi ◽  
Akira Kono ◽  
Keitaro Kato
Keyword(s):  
Acid Phosphatase ◽  
Rat Liver ◽  
Cdna Clone ◽  
Liver Lysosomes ◽  
Rat Liver Lysosomes

scholarly journals Further observations on the activation of lysosomal acid α-glucosidase by cortisone derivatives

1973 ◽  
Vol 132 (3) ◽  
pp. 435-438 ◽  
Author(s):  
E. J. Bourne ◽  
K. Clarke ◽  
J. B. Pridham ◽  
J. J. M. Rowe
Keyword(s):  
Acid Phosphatase ◽  
Rat Liver ◽  
Lysosomal Membrane ◽  
Cortisone Acetate ◽  
Lysosomal Acid ◽  
Liver Slices ◽  
Liver Lysosomes ◽  
Membrane Bound ◽  
Isolated Liver

1. Cortisone acetate activates the acid α-glucosidase in rat liver slices and in isolated liver lysosomes. 2. The reaction is steroid specific and moreover does not occur with lysosomal acid phosphatase or β-galactosidase. 3. After pretreatment of the lysosomes with cortisone, substrate (maltose) binding to the soluble lysosomal acid α-glucosidase is not affected, but the steroid does increase the Vmax. value. Membrane-bound enzyme is not activated by cortisone. 4. 4-[14C]Cortisone is preferentially bound to the lysosomal membrane and the possible involvement of this structure in the activation phenomenon is discussed.

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