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N-glycomic Analysis of Z(IgA1) Partitioned Serum and Salivary Immunoglobulin A by Capillary Electrophoresis

Author(s):

Brigitta Meszaros, Zsuzsanna Kovacs, Eniko Gebri, Hajnalka Jankovics, Ferenc Vonderviszt, Attila Kiss, Adam Simon, Sarolta Botka, Tibor Hortobagyi* and Andras Guttman   Pages 1 - 8 ( 8 )

Abstract:


Aims: To apply 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 effective indicators of most inflammatory processes. Immunoglobulin A (IgA) is the second highest abundant of the immunoglobulins 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 hematological disorders.

Materials: 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.

Keywords:

Capillary electrophoresis, IgA, N-glycosylation, Oral mucositis, Serum, Saliva

Affiliation:

Horváth Csaba Memorial Laboratory of Bioseparation Sciences, Research Center for Molecular Medicine, Doctoral School for Medicine, Faculty of Medicine, University of Debrecen, Horváth Csaba Memorial Laboratory of Bioseparation Sciences, Research Center for Molecular Medicine, Doctoral School for Medicine, Faculty of Medicine, University of Debrecen, Department of Dentoalveolar Surgery and Dental Outpatient Care, Faculty of Dentistry, University of Debrecen, Debrecen, Research Institute of Biomolecular and Chemical Engineering, University of Pannonia, Veszprem, Research Institute of Biomolecular and Chemical Engineering, University of Pannonia, Veszprem, Department of Hematopoietic Transplantation Center, Faculty of Medicine, University of Debrecen, Debrecen, Horváth Csaba Memorial Laboratory of Bioseparation Sciences, Research Center for Molecular Medicine, Doctoral School for Medicine, Faculty of Medicine, University of Debrecen, BotFog Kft, Budapest, Cerebrovascular and Neurodegenerative Research Group, Department of Neurology, Faculty of Medicine, University of Debrecen, Debrecen, Horváth Csaba Memorial Laboratory of Bioseparation Sciences, Research Center for Molecular Medicine, Doctoral School for Medicine, Faculty of Medicine, University of Debrecen



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