ACINAR ZONATION OF CYTOSOLIC BUT NOT ORGANELLE-BOUND ACTIVITIES OF PHOSPHOENOLPYRUVATE CARBOXYKINASE AND ASPARTATE-AMINOTRANSFERASE IN GUINEA-PIG LIVER

In human liver, unlike in rat liver, there is no apparent acinar heterogeneity of total cellular activity of phosphoenopyruvate carboxykinase [Wimmer, Luttringer and Columbi (1990) Histochemistry 93, 409-415]. Since the intracellular compartmentation of phosphoenolpyruvate carboxykinase differs in rat and human liver, we examined the acinar heterogeneity of cytosolic and organelle-bound activities of this enzyme in the guinea pig, which shows a more similar intracellular compartmentation of enzyme activity to human liver than does the rat. Cytosolic phosphoenolpyruvate carboxykinase activity was higher in periportal than in perivenous hepatocytes, whereas the organelle-bound activity was similar in the two cell populations. Aspartate aminotransferase and alanine aminotransferase activities showed a similar distribution to phosphoenolpyruvate carboxykinase, with a higher cytosolic activity in periportal than in perivenous hepatocytes but a similar organelle-bound activity in the two cell populations. Data on the acinar zonation of enzymes determined in whole cells or tissue should be interpreted cautiously if the enzyme activity is present in more than one subcellular compartment.