N-glycomic Analysis of Z(IgA1) Partitioned Serum and Salivary Immunoglobulin A by Capillary Electrophoresis.
Adult
Blood Proteins
/ metabolism
Case-Control Studies
Electrophoresis, Capillary
Female
Glycomics
Glycosylation
Hematologic Diseases
/ complications
Humans
Immunoglobulin A
/ chemistry
Male
Middle Aged
Mouth Diseases
/ diagnosis
Mouth Mucosa
/ metabolism
Polysaccharides
/ chemistry
Saliva
/ chemistry
Salivary Proteins and Peptides
/ metabolism
Capillary electrophoresis
IgA
N-glycosylation
Oral mucositis
Saliva
Serum
hematological diseases
Journal
Current molecular medicine
ISSN: 1875-5666
Titre abrégé: Curr Mol Med
Pays: Netherlands
ID NLM: 101093076
Informations de publication
Date de publication:
2020
2020
Historique:
received:
24
02
2019
revised:
19
03
2020
accepted:
25
03
2020
pubmed:
14
4
2020
medline:
23
11
2021
entrez:
14
4
2020
Statut:
ppublish
Résumé
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. 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. 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. 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. 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. 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.
Sections du résumé
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 hematological disorders.
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.
Identifiants
pubmed: 32282299
pii: CMM-EPUB-105777
doi: 10.2174/1566524020666200413114151
doi:
Substances chimiques
Blood Proteins
0
Immunoglobulin A
0
Polysaccharides
0
Salivary Proteins and Peptides
0
glycosylated IgA
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
781-788Informations de copyright
Copyright© Bentham Science Publishers; For any queries, please email at epub@benthamscience.net.