Lectin binding sites in normal and phenobarbitale/halothane treated rat liver. A histochemical study

Histochemistry. 1989;90(5):391-7. doi: 10.1007/BF00508318.

Abstract

The content of carbohydrate residues of both normal and phenobarbitale-halothane-hypoxia exposed rat liver has been examined by means of lectin histochemistry. Eight biotinylated lectins specific to galactose, N-acetyl-galactosamine, N-acetyl-glucosamine, fucose and mannose were applied to paraffin sections of rat liver at light microscopic level. The most distinct binding was observed at the structures of the "perisinusoidal functional unit": Kupffer cells are bound by S-WGA, SBA and PNA. Bile canaliculi display binding sites for RCA I and WGA. Cytoplasm of hepatocytes appears lectin-negative, except for PSA. The enhanced reaction of S-WGA, PNA and SBA after the preincubation of the sections with neuraminidase indicates the occurrence of sialic acid in Kupffer cells. The phenobarbitale-halothane-hypoxia exposed rat liver shows centrolobular degeneration of hepatocytes with a diminished amount of hepatocyte and Kupffer cells as well. The lectin binding pattern of sinusoidal walls, membranes of hepatocytes and bile canaliculi remains the same compared to that of normal rat liver. This finding suggests that at least the carbohydrate content of membranes in the liver resists severe destruction under phenobarbitale-halothane-hypoxia. It is assumed that there exists a connection between intact carbohydrate residues and the regeneration of liver parenchyma.

Publication types

  • Comparative Study

MeSH terms

  • Animals
  • Bile Canaliculi / anatomy & histology
  • Binding Sites
  • Glycoconjugates / analysis
  • Halothane / pharmacology*
  • Histocytochemistry
  • Kupffer Cells / anatomy & histology
  • Lectins / metabolism*
  • Liver / analysis*
  • Liver / cytology
  • Liver / drug effects
  • Male
  • Phenobarbital / pharmacology*
  • Rats
  • Rats, Inbred Strains

Substances

  • Glycoconjugates
  • Lectins
  • Halothane
  • Phenobarbital