COEXPRESSION OF PERIPORTAL AND PERIVENOUS ENZYMES IN RAT HEPATOCYTES AFTER EXPERIMENTAL BILE-DUCT LIGATION - COMPARISON WITH INTRASPLENICALLY TRANSPLANTED HEPATOCYTES
L. Racinesamson et al., COEXPRESSION OF PERIPORTAL AND PERIVENOUS ENZYMES IN RAT HEPATOCYTES AFTER EXPERIMENTAL BILE-DUCT LIGATION - COMPARISON WITH INTRASPLENICALLY TRANSPLANTED HEPATOCYTES, HISTOCHEM C, 105(4), 1996, pp. 319-329
The coexpression of normally periportal and perivenous markers has bee
n described in heterotopically transplanted hepatocytes. To determine
whether such a coexpression might also occur in hepatocytes retaining
their original intrahepatic location, we compared in bile-duct-ligated
livers and intrasplenically transplanted hepatocytes, the expression
and distribution of the predominantly periportal glucose-6-phosphatase
, succinate dehydrogenase, and lactate dehydrogenase, the predominantl
y perivenous glutamate dehydrogenase, NADPH-dehydrogenase, and beta-hy
droxybutyrate dehydrogenase, and the strictly perivenous glutamine syn
thetase. The coexpression of high levels of the two periportal markers
glucose-6-phosphatase and lactate dehydrogenase and of the perivenous
marker NADPH dehydrogenase was observed in two situations: in cluster
s of hepatocytes isolated within the ductular proliferation in bile-du
ct-ligated livers and the majority of intrasplenically transplanted he
patocytes. The expression of glutamine synthetase was different accord
ing to the site. The protein was observed in certain intrasplenically
transplanted hepatocytes bordering the splenic vessels but was never d
etected in hepatocyte clusters found in bile-duct-ligated livers. Our
study therefore suggests that the coexpression of periportal and periv
enous markers in the same hepatocytes is likely to be a non-specific c
onsequence of the loss of the normal connections of hepatocytes with t
he normal liver microcirculation.