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The Protein Journal

, Volume 38, Issue 1, pp 23–29 | Cite as

Changes Due to Ageing in the Glycan Structure of Alpha-2-Macroglobulin and Its Reactivity with Ligands

  • Miloš ŠunderićEmail author
  • Martina Križáková
  • Vesna Malenković
  • Danica Ćujić
  • Jaroslav Katrlík
  • Olgica Nedić
Article
  • 73 Downloads

Abstract

Alpha-2-macroglobulin (α2M) is a molecule generally associated with inflammation, and chronic inflammation is associated with ageing and cancer. The degree of inflammation was recently proposed to be considered as a biomarker of biological ageing. In this study, glycans attached to α2M were analysed in a human population of different ages by lectin-based protein microarray. Higher reactivity of α2M with several lectins was detected in older individuals indicating an increased content of specific monosaccharides: α2,6 sialic acid, mannose and N-acetylglucosamine, and multiantennary complex type N-glycans. The increased glycosylation of α2M was accompanied by reduced binding of Zn ions and insulin-like growth factor-binding protein 2 (IGFBP-2). Glycosylation of α2M and its reactivity with IGFBP-2 is similarly affected by ageing and incidence of colon cancer, but the reactivity of α2M with Zn ions is differently affected, as the binding of Zn ions remains unaltered in patients with colon cancer compared to healthy middle-aged individuals. Thus, the binding of IGFBP-2 to α2M seems to be related to structural changes in the glycan moieties of α2M, whereas binding of Zn ions, most likely, is not.

Keywords

α2M Age Glycosylation Ligand binding Cancer 

Abbreviations

α2M

Alpha-2-macroglobulin

IGFBP-2

Insulin-like growth factor-binding protein-2

SNA

Sambucus nigra agglutinin

ConA

Concanavalin A

MAL-II

Maackia amurensis lectin-II

PHA-E

Phaseolus vulgaris erythroagglutinin

WGA

Wheat germ agglutinin

LCA

Lens culinaris agglutinin

AAL

Aleuria aurantia lectin

RCA-I

Ricinus communis-I

LBPM

Lectin-based protein microarray

IMAC

Immobilised metal-affinity chromatography

DU

Densitometric unit

Notes

Acknowledgements

This work was supported by the bilateral cooperation Grants (451-03-545/2015-09/01, SK-SRB-2016-0023), APVV SK-SRB-2013-0028 and APVV SK-SRB-2016-0023, and by national Grant Nos. 173042 (Ministry of Education, Science and Technological Development of the Republic of Serbia), VEGA 2/0162/14 and APVV-14-0753. The authors would like to thank Dr Judith Anna Nikolić, a native English speaker for language corrections.

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© Springer Science+Business Media, LLC, part of Springer Nature 2018

Authors and Affiliations

  1. 1.Institute for the Application of Nuclear Energy (INEP)University of BelgradeBelgradeSerbia
  2. 2.Department of Glycobiotechnology, Institute of ChemistrySlovak Academy of SciencesBratislavaSlovakia
  3. 3.Clinical-Medical Centre “Bežanijska Kosa”BelgradeSerbia

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