Beta-1,4-galactosylation of N-glycans is a complex process

Biochim Biophys Acta. 1999 Dec 6;1473(1):54-66. doi: 10.1016/s0304-4165(99)00169-5.

Abstract

Most beta-1,4-galactosyltransferase (beta-1,4-GalT)-knockout mice die after birth. Although several defects were found transiently in these animals, the primary cause of death is obscure. Not only beta-1,4-linked galactose residues on N-glycans, but also beta-1, 4-GalT activities were found in some of the tissues. Recently, five human genes which encode beta-1,4-GalTs have been cloned, and the possible presence of such novel beta-1,4-GalTs in mice is considered to bring about survival of the mutant animal beyond birth. In order to understand the semi-lethal nature of this animal, it is inevitable to clarify how individual novel beta-1,4-GalTs are involved in the biosynthesis of glycoconjugates based on their acceptor-substrate specificities.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Amidohydrolases / metabolism
  • Amino Acid Sequence
  • Amino Sugars / biosynthesis
  • Animals
  • Brain / metabolism
  • Carbohydrate Sequence
  • Galactosyltransferases / genetics
  • Galactosyltransferases / metabolism*
  • Glycoproteins / biosynthesis
  • Humans
  • Mice
  • Mice, Knockout
  • Molecular Sequence Data
  • Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase
  • Sequence Alignment
  • Sialic Acids / metabolism
  • Substrate Specificity

Substances

  • Amino Sugars
  • Glycoproteins
  • Sialic Acids
  • polysialic acid
  • N-acetyllactosamine
  • Galactosyltransferases
  • beta-1,4-galactosyltransferase I
  • beta-1,4-galactosyltransferase IV
  • glucosylceramide beta-1-4-galactosyltransferase
  • Amidohydrolases
  • Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase