title: Histochemical data on the liver of the marmoset (Callithrix jacchus).
abstract: The histochemistry of the hepatic parenchymal cells was studied in four Callithrix jacchus. A large amount of glycogen was noted throughout the lobules while the UDPG-GT and the phosphorylases were found unevenly distributed by the hepatic strands with different degrees of reactivity. Near the central vein one of the livers showed PAS-positive nuclear corpuscles that were more conspicuous in the hepatic cells with a larger amount of cytoplasmic glycogen and weaker UDPG-GT and phosphorylase reactivities. G-6PA (in a larger amount) and LDH (in a moderate amount) were found evenly distributed in the hepatic strands. F-1-6PA was seen sometimes with a stronger reactivity at the peripheral part of the lobules. The enzymes of the pentose shunt (G-6PDH, 6-PGDH and NADPH-2-TR) reacted strongly and as a rule evenly distributed near the hepatic lobules. Occasionally they reacted more intensely in the row of hepatic cells disposed just around the central vein. Cytochrome oxidase showed a very faint reaction. Cis-aconitase and ICDH were weak or moderate. NADH-2-TR more than SDH more than MDH were seen frequently diffused near the hepatic strands. SDH and MDH in some instances showed a stronger reactivity in the row or group of hepatic cells around the central vein. ATPase at pH 6.3 was negative in the marmoset liver; ATPase at pH 7.4 was mainly found in the wall of the portal area vessels; ATPase at pH 8.5 showed a stronger reactivity in the cytoplasm of the hepatic cells and ATPase at pH 9.4 was more abundant in the bile capillaries. The reactivity of the lipid metabolism enzymes was moderate with regard to alpha-GPDH or negligible with regard to beta-OHBDH. Acid phosphatase showed a stronger reaction, but almost limited to the Kupffer cells. The hepatic cells showed only a moderate amount of RNA. Some enzymes of the protein metabolism, such as GDH and leucine aminopeptidase showed a stronger reactivity while some others, such as alanyl aminopeptidase and MAO, were seen diffused near the hepatic lobules in a small amount. Enzymes of the mucopolysaccharide metabolism were not found at all (beta-glucuronidase) or showed only a weak reactivity, such as xylitol dehydrogenase.
mesh_terms: D000135:Acid Phosphatase / Q000032:analysis; D000251:Adenosine Triphosphatases / Q000032:analysis; D000818:Animals; D002143:Callitrichinae / Q000378:metabolism*; D003576:Electron Transport Complex IV / Q000032:analysis; D005952:Glucose-6-Phosphatase / Q000032:analysis; D007770:L-Lactate Dehydrogenase / Q000032:analysis; D008099:Liver / Q000201:enzymology*; D008112:Liver Glycogen / Q000032:analysis; D010088:Oxidoreductases / Q000032:analysis; D010429:Pentoses; D006005:Phosphorylases / Q000032:analysis; D014166:Transferases / Q000032:analysis; D014532:Uridine Diphosphate Glucose
chemical_list: D008112:Liver Glycogen; D010429:Pentoses; D010088:Oxidoreductases; D007770:L-Lactate Dehydrogenase; D003576:Electron Transport Complex IV; D014166:Transferases; D006005:Phosphorylases; D000135:Acid Phosphatase; D005952:Glucose-6-Phosphatase; D000251:Adenosine Triphosphatases; D014532:Uridine Diphosphate Glucose