Human serum N-glycan profiles are age and sex dependent.

BACKGROUND

protein glycosylation varies with the physiological and pathological status of the cell. Consequently, analysis of protein-linked glycans has growing importance both in basic glycobiological research and as a potential tool for monitoring the physiological state in humans.

DESIGN, SETTING AND PARTICIPANTS: a total of 265 healthy northern Chinese men and women were grouped by age and gender. The mean age in males and females was similar.

OBJECTIVE

the study is aimed to evaluate the effects of the age and gender on the human serum N-glycans profiles in the clinical diagnose of ageing and disease.

METHODS

the 265 human serum N-glycan profiles were obtained by DNA sequencer-assisted fluorophore-assisted carbohydrate electrophoresis. Comparison of N-glycan profiles was carried out among the different genders and age groups and the data were analysed with the GeneMapper software.

RESULTS

age-related changes in the three N-glycan structures (NGA2F, NGA2FB and NA2F) were observed. Interestingly, fucosylation of N-glycans was significantly different (P < 0.0001) between men and women: more core-α-1,6-fucosylated glycans were detected in women, whereas more branching-α-1,3-fucosylated N-glycans were seen in men.

CONCLUSIONS

the N-glycome profile in serum is gender and age dependent. This should be taken into consideration in the development of serum glycome markers.