Glycobiology Advance Access originally published online on September 2, 2009
Glycobiology 2009 19(12):1547-1553; doi:10.1093/glycob/cwp134
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Stability of N-glycan profiles in human plasma
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2 University of Zagreb, Faculty of Pharmacy and Biochemistry, Ante Kova
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a 1, 10000 Zagreb
3 University of Osijek, School of Medicine, Josipa Huttlera 4, 31000 Osijek
4 Genos Ltd, Glycobiology Division, Planinska 1, 10000 Zagreb, Croatia
1 To whom correspondence should be addressed: Tel: +385-1-639-4467; Fax: +385-1-639-4400; e-mail: glauc{at}pharma.hr
Received on June 25, 2009; revised on August 18, 2009; accepted on August 28, 2009
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.
Key words: glycan analysis / human plasma / glycome stability / N-glycans / protein glycosylation