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Diagnostic Potential of Transferrin Glycoforms-A Lectin-Based Protein Microarray Approach.

Authors
  • Penezić, Ana1
  • Križakova, Martina2
  • Miljuš, Goran1
  • Katrlik, Jaroslav2
  • Nedić, Olgica1
  • 1 Institute for the Application of Nuclear Energy (INEP), Banatska 31b, 11080, Belgrade, Serbia. , (Serbia)
  • 2 Slovak Academy of Sciences, Dúbravská cesta 9, 845 38, Bratislava, Slovak Republic.
Type
Published Article
Journal
PROTEOMICS - CLINICAL APPLICATIONS
Publisher
Wiley (John Wiley & Sons)
Publication Date
Sep 01, 2019
Volume
13
Issue
5
Identifiers
DOI: 10.1002/prca.201800185
PMID: 31050875
Source
Medline
Keywords
Language
English
License
Unknown

Abstract

Disease or a specific condition may cause alteration of human transferrin (hTf) glycosylation pattern. A specific analytical platform, lectin-based protein microarray, is designed and optimized for the investigation of hTf glycans, attached to the protein core in their native form. hTf molecules isolated from healthy persons of different age, diabetes mellitus type 2 (T2DM) or colorectal carcinoma (CRC) patients are used for method validation. Reliability of the results is ensured by three criteria for the evaluation of hTf-lectin interactions: i) signal-to-noise ratio above 3, ii) signal intensity above 250 arbitrary units, and iii) hTf concentration ensuring high sensitivity of the assay. Six lectins, out of fourteen tested, satisfy the criteria. hTf is spotted at concentration of 50 µg mL-L . When physiological samples (isolated hTf) are analyzed, the highest potential to differentiate between population groups expresses Aleuria aurantia (AAL), Triticum vulgaris (WGA) and Phaseolus vulgaris (PHA-E) lectins. The initial amount of hTf which can be analyzed is very low (75 pg). Results confirm that a very sensitive, high-throughput lectin-based protein microarray platform can be formulated to detect changes in hTf glycan structures which can be considered as biomarkers of ageing or a disease. © 2019 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

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