title: Increased glycosylation capacity in regenerating rat liver is paralleled by decreased activities of CMP-N-acetylneuraminate hydrolase and UDP-galactose pyrophosphatase.
abstract: In regenerating rat liver the activities of CMP-N-acetylneuraminate hydrolase and UDP-galactose pyrophosphatase were decreased to 40-50% of control values within 35 h after partial hepatectomy. In the same time period the activities of sialyltransferase and galactosyltransferase were increased, and the initial sharp decrease in the carbohydrate content of liver and serum glycoproteins was largely restored. The antiparallel nature of these events is suggestive of an involvement of nucleotide-sugar-hydrolysis enzymes in rat liver glycoprotein biosynthesis.
mesh_terms: D000818:Animals; D050260:Carbohydrate Metabolism; D002462:Cell Membrane / Q000378:metabolism; D006023:Glycoproteins / Q000097:blood; D008099:Liver / Q000201:enzymology / Q000378:metabolism*; D008115:Liver Regeneration; D008297:Male; D009713:Nucleotidyltransferases / Q000378:metabolism*; D009929:Organ Size; D010727:Phosphoric Diester Hydrolases / Q000378:metabolism*; D051381:Rats; D011919:Rats, Inbred Strains; D005694:UTP-Hexose-1-Phosphate Uridylyltransferase / Q000378:metabolism*
chemical_list: D006023:Glycoproteins; D009713:Nucleotidyltransferases; D005694:UTP-Hexose-1-Phosphate Uridylyltransferase; D010727:Phosphoric Diester Hydrolases; C010265:CMP-N-acylneuraminate phosphodiesterase