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5 results on '"Mészáros, Brigitta"'

4. N-Glycosylation Alteration of Serum and Salivary Immunoglobulin a Is a Possible Biomarker in Oral Mucositis

Author

Gebri, Enikő, Kovács, Zsuzsanna, Mészáros, Brigitta, Tóth, Ferenc, Simon, Ádám, Jankovics, Hajnalka, Vonderviszt, Ferenc, Kiss, Attila, Guttman, András, and Hortobágyi, Tibor

Subjects
glycoprotein, lcsh:R, immunoglobulins, oral immunity, lcsh:Medicine, autologous peripheral stem-cell transplantation (APSCT), Article, IgA, glycomics, oral mucositis
Abstract

Background: Oral and enteral mucositis due to high-dose cytostatic treatment administered during autologous and allogeneic stem-cell transplantation increases mortality. Salivary secretory immunoglobulin A (sIgA) is a basic pillar of local immunity in the first line of defense. Altered salivary sialoglycoprotein carbohydrates are important in the pathologies in the oral cavity including inflammation, infection and neoplasia. Therefore, we assessed whether changes in the salivary and serum IgA glycosylation correlated with development and severity of oral mucositis. Methods: Using capillary electrophoresis, comparative analysis of serum and salivary IgA total N-glycans was conducted in 8 patients with autologous peripheral stem-cell transplantation (APSCT) at four different stages of transplantation (day &minus, 3/&minus, 7, 0, +7, +14) and in 10 healthy controls. Results: Fourteen out of the 31 structures identified in serum and 6 out of 38 in saliva showed significant changes upon transplantation compared with the control group. Only serum core fucosylated, sialylated bisecting biantennary glycan (FA2BG2S2) showed significant differences between any two stages of transplantation (day &minus, 7 and day +14, p = 0.0279). Conclusion: Our results suggest that changes in the serum IgA total N-glycan profile could serve as a disease-specific biomarker in patients undergoing APSCT, while analysis of salivary IgA N-glycan reflects the effect of APSCT on local immunity.

Published
2020

5. Modeling of the Desialylated Human Serum N-glycome for Molecular Diagnostic Applications in Inflammatory and Malignant Lung Diseases.

Author

Farkas A, Mészáros B, Szarka M, Szigeti M, Kappelmayer J, Szabó M, Csánky E, and Guttman A

Subjects
Aged, Case-Control Studies, Female, Glycomics, Glycosylation, Humans, Lung Neoplasms blood, Male, Middle Aged, Pulmonary Disease, Chronic Obstructive, Biomarkers blood, Lung Neoplasms diagnosis, Models, Biological, Polysaccharides blood, Sialic Acids chemistry
Abstract

Background: Immunoglobulin G and A, transferrin, haptoglobin and alpha-1- antitrypsin represent approximately 85% of the human serum glycoproteome and their N-glycosylation analysis may lead to the discovery of important molecular disease markers. However, due to the labile nature of the sialic acid residues, the desialylated subset of the serum N-glycoproteome has been traditionally utilized for diagnostic applications., Objective: Creating a five-protein model to deconstruct the overall N-glycosylation fingerprints in inflammatory and malignant lung diseases., Methods: The N-glycan pool of human serum and the five high abundant serum glycoproteins were analyzed. Simultaneous endoglycosidase/sialidase digestion was followed by fluorophore labeling and separation by CE-LIF to establish the model. Pooled serum samples from patients with COPD, lung cancer (LC) and their comorbidity were all analyzed., Results: Nine significant (>1%) asialo-N-glycan structures were identified both in human serum and the standard protein mixture. The core-fucosylated-agalacto-biantennary glycan differentiated COPD and LC and both from the control and the comorbidity groups. Decrease in the core-fucosylated-agalacto-biantennary-bisecting, monogalacto and bigalacto structures differentiated all disease groups from the control. The significant increase of the fucosylated-galactosylated-triantennary structure was highly specific for LC, to a medium extent for COPD and a lesser extent for comorbidity. Also, some increase in the afucosylated-galactosylated-biantennary structure in all three disease types and afucosylated-galactosylated-triantennary structures in COPD and LC were observed in comparison to the control group., Conclusion: Our results suggested that changes in the desialylated human serum Nglycome hold glycoprotein specific molecular diagnostic potential for malignant and inflammatory lung diseases, which can be modeled with the five-protein mixture., (Copyright© Bentham Science Publishers; For any queries, please email at epub@benthamscience.net.)

Published
2020
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