Liver cell heterogeneity. The distribution of fructose-bisphosphatase in fed and fasted rats and in man.
Periportal and perivenous hepatocytes were isolated by microdissection from lyophilized liver slices (16 micrometer) from fed and fasted rats and from a human patient. NADP/NADPH cycling was used to determine fructose-1,6-bisphosphatase activity in the isolated hepatocytes (10 ng dry weight). The periportal hepatocytes contain 3 times as much fructose-1,6-bisphosphatase activity as the perivenous hepatocytes. A 24 h fast led to two-fold increase in the activity in the periportal hepatocytes and a four-fold increase in the perivenous hepatocytes. Fructose-1,6-bisphosphatase parallels closely with the key enzyme phosphoenolpyruvate carboxykinase, and therefore can be considered a suitable marker for gluconeogenic capacity.
D000818:Animals; D005215:Fasting; D006597:Fructose-Bisphosphatase / Q000378:metabolism*; D006651:Histocytochemistry; D008099:Liver / Q000166:cytology / Q000201:enzymology*; D008297:Male; D009249:NADP / Q000378:metabolism; D051381:Rats
D009249:NADP; D006597:Fructose-Bisphosphatase