Analysis of haptoglobin N-glycome alterations in inflammatory and malignant lung diseases by capillary electrophoresis

Csaba Váradi, Stefan Mittermayr, Ákos Szekrényes, János Kádas, Laszlo Takacs, István Kurucz, A. Guttman

Research output: Contribution to journalArticle

23 Citations (Scopus)

Abstract

A CE-based method was introduced to compare the N-glycosylation profile of haptoglobin in normal and pathologic conditions. To assess the biomarker potential of glycosylation changes in various lung diseases, haptoglobin was isolated from plasma samples of healthy, pneumonia, chronic obstructive pulmonary disease, and lung cancer patients by means of two haptoglobin-specific monoclonal antibodies. Haptoglobin N-glycans were then enzymatically released, fluorescently labeled, and profiled by CE. Disease-associated changes of core and antennary fucosylation were identified by targeted exoglycosidase digestions and their levels were compared in the different patient groups. Terms such as core- and arm-fucosylation degree, as well as branching degree, were introduced for easier characterization of the changes and statistical analysis was used to examine which structures were responsible for the observed differences. Increased level of α1-6 fucosylated tri-antennary glycans was found in all disease groups compared to the control. Elevated amounts of core- and arm-fucosylation on tetra-antennary glycans were detected in the lung cancer group compared to the chronic obstructive pulmonary disease group. A larger scale study is necessary to confirm and validate these preliminary findings in the glycosylation changes of haptoglobin, so could then be used as biomarkers in the diagnosis of malignant and inflammatory lung diseases.

Original languageEnglish
Pages (from-to)2287-2294
Number of pages8
JournalElectrophoresis
Volume34
Issue number16
DOIs
Publication statusPublished - Aug 2013

Fingerprint

Capillary electrophoresis
Pulmonary diseases
Haptoglobins
Capillary Electrophoresis
Lung Diseases
Glycosylation
Polysaccharides
Lung Neoplasms
Biomarkers
Chronic Obstructive Pulmonary Disease
Glycoside Hydrolases
Digestion
Pneumonia
Statistical methods
Monoclonal Antibodies
Plasmas

Keywords

  • Biomarkers
  • Capillary electrophoresis
  • Exoglycosidase array
  • Fucosylation in cancer
  • Glycan analysis

ASJC Scopus subject areas

  • Biochemistry
  • Clinical Biochemistry

Cite this

Analysis of haptoglobin N-glycome alterations in inflammatory and malignant lung diseases by capillary electrophoresis. / Váradi, Csaba; Mittermayr, Stefan; Szekrényes, Ákos; Kádas, János; Takacs, Laszlo; Kurucz, István; Guttman, A.

In: Electrophoresis, Vol. 34, No. 16, 08.2013, p. 2287-2294.

Research output: Contribution to journalArticle

Váradi, Csaba ; Mittermayr, Stefan ; Szekrényes, Ákos ; Kádas, János ; Takacs, Laszlo ; Kurucz, István ; Guttman, A. / Analysis of haptoglobin N-glycome alterations in inflammatory and malignant lung diseases by capillary electrophoresis. In: Electrophoresis. 2013 ; Vol. 34, No. 16. pp. 2287-2294.
@article{7f8427cbdd5d42b0a7f180e83cbf0a2b,
title = "Analysis of haptoglobin N-glycome alterations in inflammatory and malignant lung diseases by capillary electrophoresis",
abstract = "A CE-based method was introduced to compare the N-glycosylation profile of haptoglobin in normal and pathologic conditions. To assess the biomarker potential of glycosylation changes in various lung diseases, haptoglobin was isolated from plasma samples of healthy, pneumonia, chronic obstructive pulmonary disease, and lung cancer patients by means of two haptoglobin-specific monoclonal antibodies. Haptoglobin N-glycans were then enzymatically released, fluorescently labeled, and profiled by CE. Disease-associated changes of core and antennary fucosylation were identified by targeted exoglycosidase digestions and their levels were compared in the different patient groups. Terms such as core- and arm-fucosylation degree, as well as branching degree, were introduced for easier characterization of the changes and statistical analysis was used to examine which structures were responsible for the observed differences. Increased level of α1-6 fucosylated tri-antennary glycans was found in all disease groups compared to the control. Elevated amounts of core- and arm-fucosylation on tetra-antennary glycans were detected in the lung cancer group compared to the chronic obstructive pulmonary disease group. A larger scale study is necessary to confirm and validate these preliminary findings in the glycosylation changes of haptoglobin, so could then be used as biomarkers in the diagnosis of malignant and inflammatory lung diseases.",
keywords = "Biomarkers, Capillary electrophoresis, Exoglycosidase array, Fucosylation in cancer, Glycan analysis",
author = "Csaba V{\'a}radi and Stefan Mittermayr and {\'A}kos Szekr{\'e}nyes and J{\'a}nos K{\'a}das and Laszlo Takacs and Istv{\'a}n Kurucz and A. Guttman",
year = "2013",
month = "8",
doi = "10.1002/elps.201300041",
language = "English",
volume = "34",
pages = "2287--2294",
journal = "Electrophoresis",
issn = "0173-0835",
publisher = "Wiley-VCH Verlag",
number = "16",

}

TY - JOUR

T1 - Analysis of haptoglobin N-glycome alterations in inflammatory and malignant lung diseases by capillary electrophoresis

AU - Váradi, Csaba

AU - Mittermayr, Stefan

AU - Szekrényes, Ákos

AU - Kádas, János

AU - Takacs, Laszlo

AU - Kurucz, István

AU - Guttman, A.

PY - 2013/8

Y1 - 2013/8

N2 - A CE-based method was introduced to compare the N-glycosylation profile of haptoglobin in normal and pathologic conditions. To assess the biomarker potential of glycosylation changes in various lung diseases, haptoglobin was isolated from plasma samples of healthy, pneumonia, chronic obstructive pulmonary disease, and lung cancer patients by means of two haptoglobin-specific monoclonal antibodies. Haptoglobin N-glycans were then enzymatically released, fluorescently labeled, and profiled by CE. Disease-associated changes of core and antennary fucosylation were identified by targeted exoglycosidase digestions and their levels were compared in the different patient groups. Terms such as core- and arm-fucosylation degree, as well as branching degree, were introduced for easier characterization of the changes and statistical analysis was used to examine which structures were responsible for the observed differences. Increased level of α1-6 fucosylated tri-antennary glycans was found in all disease groups compared to the control. Elevated amounts of core- and arm-fucosylation on tetra-antennary glycans were detected in the lung cancer group compared to the chronic obstructive pulmonary disease group. A larger scale study is necessary to confirm and validate these preliminary findings in the glycosylation changes of haptoglobin, so could then be used as biomarkers in the diagnosis of malignant and inflammatory lung diseases.

AB - A CE-based method was introduced to compare the N-glycosylation profile of haptoglobin in normal and pathologic conditions. To assess the biomarker potential of glycosylation changes in various lung diseases, haptoglobin was isolated from plasma samples of healthy, pneumonia, chronic obstructive pulmonary disease, and lung cancer patients by means of two haptoglobin-specific monoclonal antibodies. Haptoglobin N-glycans were then enzymatically released, fluorescently labeled, and profiled by CE. Disease-associated changes of core and antennary fucosylation were identified by targeted exoglycosidase digestions and their levels were compared in the different patient groups. Terms such as core- and arm-fucosylation degree, as well as branching degree, were introduced for easier characterization of the changes and statistical analysis was used to examine which structures were responsible for the observed differences. Increased level of α1-6 fucosylated tri-antennary glycans was found in all disease groups compared to the control. Elevated amounts of core- and arm-fucosylation on tetra-antennary glycans were detected in the lung cancer group compared to the chronic obstructive pulmonary disease group. A larger scale study is necessary to confirm and validate these preliminary findings in the glycosylation changes of haptoglobin, so could then be used as biomarkers in the diagnosis of malignant and inflammatory lung diseases.

KW - Biomarkers

KW - Capillary electrophoresis

KW - Exoglycosidase array

KW - Fucosylation in cancer

KW - Glycan analysis

UR - http://www.scopus.com/inward/record.url?scp=84881612484&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84881612484&partnerID=8YFLogxK

U2 - 10.1002/elps.201300041

DO - 10.1002/elps.201300041

M3 - Article

C2 - 23580236

AN - SCOPUS:84881612484

VL - 34

SP - 2287

EP - 2294

JO - Electrophoresis

JF - Electrophoresis

SN - 0173-0835

IS - 16

ER -