TY - JOUR
T1 - N-glycomic changes in serum proteins during human aging
AU - Vanhooren, Valerie
AU - Desmyter, Liesbeth
AU - Liu, Xue En
AU - Cardelli, Maurizio
AU - Franceschi, Claudio
AU - Federico, Antonio
AU - Libert, Claude
AU - Laroy, Wouter
AU - Dewaele, Sylviane
AU - Contreras, Roland
AU - Chen, Cuiying
PY - 2007/12/1
Y1 - 2007/12/1
N2 - N-glycan profiling of the human serum glycoproteins including immunoglobulin fraction on different age groups of healthy persons shows substantial changes with increasing age in three major N-glycan structures. In individuals more than 40-50 years of age, there is an increase in under-galactosylated glycans and a decrease in the core α-1,6-fucosylated bi-galactosylated biantennary structure. These three glycan structures are also substantially changed in a Werner syndrome patient, to a level comparable or even more pronounced than those observed in a healthy Italian centenarian population. These data show that the glycosylation machineries in both liver cells and B-cells are affected in a similar way by the aging process despite their highly different nature. The observed changes in the glycan structures are indicative that biosynthetic processes are at the basis of the changes, possibly together with changes in serum clearing of glycan-altered proteins. Our data suggest that measurement of the N-glycan level changes could provide a noninvasive surrogate marker for general health or for age-related disease progression, and for monitoring the improvement of health after therapy.
AB - N-glycan profiling of the human serum glycoproteins including immunoglobulin fraction on different age groups of healthy persons shows substantial changes with increasing age in three major N-glycan structures. In individuals more than 40-50 years of age, there is an increase in under-galactosylated glycans and a decrease in the core α-1,6-fucosylated bi-galactosylated biantennary structure. These three glycan structures are also substantially changed in a Werner syndrome patient, to a level comparable or even more pronounced than those observed in a healthy Italian centenarian population. These data show that the glycosylation machineries in both liver cells and B-cells are affected in a similar way by the aging process despite their highly different nature. The observed changes in the glycan structures are indicative that biosynthetic processes are at the basis of the changes, possibly together with changes in serum clearing of glycan-altered proteins. Our data suggest that measurement of the N-glycan level changes could provide a noninvasive surrogate marker for general health or for age-related disease progression, and for monitoring the improvement of health after therapy.
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U2 - 10.1089/rej.2007.0556
DO - 10.1089/rej.2007.0556
M3 - Article
C2 - 18047421
AN - SCOPUS:37549057294
VL - 10
SP - 521
EP - 531
JO - Rejuvenation Research
JF - Rejuvenation Research
SN - 1549-1684
IS - 4
ER -