N-glycomic changes in serum proteins during human aging

Valerie Vanhooren, Liesbeth Desmyter, Xue En Liu, Maurizio Cardelli, Claudio Franceschi, Antonio Federico, Claude Libert, Wouter Laroy, Sylviane Dewaele, Roland Contreras, Cuiying Chen

Research output: Contribution to journalArticlepeer-review


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.

Original languageEnglish
Pages (from-to)521-531
Number of pages11
JournalRejuvenation Research
Issue number4
Publication statusPublished - Dec 1 2007

ASJC Scopus subject areas

  • Ageing


Dive into the research topics of 'N-glycomic changes in serum proteins during human aging'. Together they form a unique fingerprint.

Cite this