Aims: Application of capillary electrophoresis with laser induced fluorescence
detection (CE-LIF) to identify the N-glycosylation structures of serum and saliva IgA from
healthy controls and patients with malignant hematological diseases having cytostatic
treatment induced mild oral mucosal lesions.
Background: Altered N-glycosylation of body fluid glycoproteins can be an effective
indicator of most inflammatory processes. Immunoglobulin A (IgA) is the second highest
abundant immunoglobulin and has a major role in the immune-defense against potential
pathogen attacks. While IgA is abundant in serum, secretory immunoglobulin A (sIgA) is
one of the most prevalent proteins in mucosal surfaces, such as in saliva.
Objective: Our aim was to investigate the changes of IgA glycosylation in serum and
saliva as a response to an administered cytostatic treatment in patients with malignant
Methods: Capillary electrophoresis with laser induced fluorescent detection (CE-LIF)
was used to analyze the N-glycosylation profiles of Z(IgA1) partitioned immunoglobulin A
in pooled serum and saliva of 10 control subjects and 8 patients with malignant
hematological diseases having cytostatic treatment induced mild oral mucosal lesions.
Results: Eight of 31 and four of 38 N-glycans in serum and saliva, respectively, showed
significant (p<0.05) differences upon comparison to the control group. Thirteen glycans
were present in the saliva but not in the serum, on the other hand, six structures were
found in the serum samples not present in the saliva.
Conclusion: The developed Z(IgA1) partitioning and the high resolution CE-LIF based
glyocoanalytical methods provided an efficient and sensitive workflow to detect and
monitor IgA glycosylation alterations in serum and saliva with the scope for widespread
molecular medicinal use.