期刊
GLYCOBIOLOGY
卷 19, 期 12, 页码 1547-1553出版社
OXFORD UNIV PRESS INC
DOI: 10.1093/glycob/cwp134
关键词
glycan analysis; human plasma; glycome stability; N-glycans; protein glycosylation
资金
- Croatian Ministry of Science, Education and Sport [309-0061194-2023]
- European Commission (EuroPharm grant)
- National Foundation for Science
- Higher Education and Technological Development of the Republic of Croatia
Glycan heterogeneity was shown to be associated with numerous diseases and glycan analysis has a great diagnostic potential. Recently, we reported high biological variability of human plasma N-glycome at the level of population. The observed variations were larger than changes reported to be associated with some diseases; thus, it was of great importance to examine the temporal constancy of human N-glycome before glycosylation changes could be routinely analyzed in diagnostic laboratories. Plasma samples were taken from 12 healthy individuals. The blood was drawn on seven occasions during 5 days. N-Linked glycans, released from plasma proteins, were separated using hydrophilic interaction high-performance liquid chromatography into 16 groups (GP1-GP16) and quantified. The results showed very small variation in all glycan groups, indicating very good temporal stability of N-glycome in a single individual. Coefficients of variation from 1.6% for GP8 to 11.4% for GP1 were observed. The average coefficient of variation was 5.6%. These variations were comparable to those observed when analytical procedure was tested for its precision. Good stability of plasma N-glycome in healthy individuals implies that glycosylation is under significant genetic control. Changes observed in glycan profiles are consequence of environmental influences and physiologic responses and therefore have a significant diagnostic potential.
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