Alteration in N-glycomics during mouse aging: a role for FUT8
Autor: | Laurent Dollé, Claude Libert, Evgenia Makrantonaki, Naoyuki Taniguchi, Sylviane Dewaele, Valerie Vanhooren, Christos C. Zouboulis, Cuiying Chitty Chen, Makoto Kuro-o, Leo A. van Grunsven |
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Rok vydání: | 2011 |
Předmět: |
chemistry.chemical_classification
Aging medicine.medical_specialty Glycosylation Calorie restriction Cell Biology Biology carbohydrates (lipids) chemistry.chemical_compound Endocrinology chemistry Internal medicine Gene expression medicine Signal transduction Receptor Glycoprotein Klotho Fucosylation |
Zdroj: | Aging Cell. 10:1056-1066 |
ISSN: | 1474-9718 |
DOI: | 10.1111/j.1474-9726.2011.00749.x |
Popis: | 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 alpha-1,6-fucosylated-beta-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 alpha-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. |
Databáze: | OpenAIRE |
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