Heterogenous zonal distribution of lysosomal enzymes in rat liver.
The activities of beta-N-acetylglucosaminidase, beta-glucuronidase, alpha-L-iduronidase and acid phosphatase were all significantly higher in the cell lysates from the periportal than from the perivenous region obtained by the regioselective digitonin treatment of the perfused liver. The activities of cathepsins B, H and L were only slightly higher in the periportal than in the perivenous cell lysates. These results support the view that there is little zonation of lysosomal degradation of proteins, whereas the enzymatic capacity for degradation of glycosaminoglycans may be more active in the periportal region.
Pösö
A R
AR
Department of Biochemistry, College of Veterinary Medicine, Helsinki, Finland.
Penttilä
K E
KE
Lindros
K O
KO
D000135:Acid Phosphatase / Q000378:metabolism; D000818:Animals; D002403:Cathepsins / Q000378:metabolism; D006026:Glycoside Hydrolases / Q000378:metabolism; D008099:Liver / Q000201:enzymology*; D008247:Lysosomes / Q000201:enzymology*; D008297:Male; D010477:Perfusion; D011169:Portal Vein; D051381:Rats; D013347:Subcellular Fractions / Q000201:enzymology; D014018:Tissue Distribution
D000135:Acid Phosphatase; D006026:Glycoside Hydrolases; D002403:Cathepsins