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Buchner, Johannes

Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board Member: Buchner, Johannes / Lei, Ming / Ludwig, Stephan / Sies, Helmut / Turk, Boris / Wittinghofer, Alfred

SCImago Journal Rank (SJR) 2015: 1.607
Source Normalized Impact per Paper (SNIP) 2015: 0.751
Impact per Publication (IPP) 2015: 2.609

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Quantitative determination of haptoglobin glycoform variants in psoriasis

Bernardetta Maresca1 / Luisa Cigliano2 / Maria M. Corsaro3 / Giuseppina Pieretti3 / Massimo Natale4 / Enrico M. Bucci4 / Fabrizio Dal Piaz5 / Nicola Balato1 / Massimiliano Nino1 / Fabio Ayala1 / Paolo Abrescia2

1Dipartimento di Patologia Sistematica – Sezione di Dermatologia, Università di Napoli Federico II, via Pansini 5, I-80131 Napoli, Italy

2Dipartimento delle Scienze Biologiche, Università di Napoli Federico II, via Mezzocannone 8, I-80134 Napoli, Italy

3Dipartimento di Chimica Organica e Biochimica, Università di Napoli Federico II, Complesso Universitario M.S. Angelo, via Cinthia 4, I-80126 Napoli, Italy

4BioDigitalValley Ltd, corso Vercelli 117, I-10015 Ivrea (Torino), Italy

5Dipartimento di Scienze Farmaceutiche, Università degli Studi di Salerno, via Ponte don Melillo, I-84084 Fisciano (Salerno), Italy

Corresponding author

Citation Information: Biological Chemistry. Volume 391, Issue 12, Pages 1429–1439, ISSN (Online) 1437-4315, ISSN (Print) 1431-6730, DOI: https://doi.org/10.1515/bc.2010.146, November 2010

Publication History

Published Online:


Haptoglobin is an acute phase glycoprotein, secreted by hepatocytes and other types of cells including keratinocytes. Haptoglobin has been suggested to impair the immune response, inhibit gelatinases in the extracellular matrix and promote angiogenesis, but its role in psoriasis is obscure to date. Changes in haptoglobin glycan structure were observed in several diseases. The aim of this study was to investigate whether haptoglobin displays glycan variations in psoriasis. We found that the pattern of plasma haptoglobin glycoforms, following two-dimensional electrophoresis, exhibited significant quantitative differences in spot intensities between patients and controls. Quantitative and qualitative differences in glycan mass, between patients and controls, were found by mass spectrometry of glycopeptides from tryptic digests of protein isolated from both patients and controls. The number of distinct fucosylated glycoforms of peptides NLFLNHSENATAK and MVSHHNLTTGATLINEQWLLTTAK was higher in patients than in controls, but no fucosylated glycan was detected on peptide VVLHPNYSQ-VDIGLIK in either case. The number of peptides with distinct triantennary and tetraantennary glycans was higher in patients than in controls. Abundance or structure of specific glycans, which are present in haptoglobin from patients and are different or missing in normal haptoglobin, might be associated with disease activity.

Keywords: glycans; mass spectrometry; structure heterogeneity; two-dimensional electrophoresis

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