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Alpha-(1,6)-fucosyltransferase (EC (Alpha1-6FucT) (Fucosyltransferase 8) (GDP-L-Fuc:N-acetyl-beta-D-glucosaminide alpha1,6-fucosyltransferase) (GDP-fucose--glycoprotein fucosyltransferase) (Glycoprotein 6-alpha-L-fucosyltransferase)


Alteration in N-glycomics during mouse aging: a role for FUT8.

We recently reported that N-glycosylation changes during human aging. To further investigate the molecular basis determining these alterations, the aging process in mice was studied. N-glycan profiling of mouse serum glycoproteins in different age groups of healthy C57BL/6 mice showed substantial age-related changes in three major N-glycan structures: under-galactosylated biantennary (NGA2F), biantennary (NA2), and core α-1,6-fucosylated -β-galactosylated biantennary structures (NA2F). Mice defective in klotho gene expression (kl/kl), which have a shortened lifespan, displayed a similar but accelerated trend. Interestingly, the opposite trend was observed in slow-aging Snell Dwarf mice (dw/dw) and in mice fed a calorically restricted diet. We also discovered that increased expression and activity of α-1,6-fucosyltransferase (FUT8) in the liver are strongly linked to the age-related changes in glycosylation and that this increased FUT8 and fucosylation influence IGF-1 signaling. These data demonstrate that the glycosylation machinery in liver cells is significantly affected during aging and that age-related increased FUT8 activity could influence the aging process by altering the sensitivity of the IGF-1R signaling pathway.

MeSH Terms

  • Aging
  • Animals
  • Blood Proteins
  • Caloric Restriction
  • Fucose
  • Fucosyltransferases
  • Gene Expression
  • Glucuronidase
  • Glycomics
  • Glycoproteins
  • Glycosylation
  • Insulin-Like Growth Factor I
  • Liver
  • Male
  • Mice
  • Mice, Inbred C57BL
  • Mice, Transgenic
  • Polysaccharides
  • Receptor, IGF Type 1
  • Signal Transduction