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Glycoproteomic identification of galectin-3 and -8 ligands in bronchoalveolar lavage of mild asthmatics and healthy subjects.

Journal article
Authors Cecilia Cederfur
Johan Malmström
Kristian Nihlberg
Mattias Block
Michael Breimer
Leif Bjermer
Gunilla Westergren-Thorsson
Hakon Leffler
Published in Biochimica et biophysica acta
Volume 1820
Issue 9
Pages 1429-1436
ISSN 0006-3002
Publication year 2012
Published at Institute of Clinical Sciences, Department of Surgery
Institute of Biomedicine, Department of Pathology
Pages 1429-1436
Language en
Links dx.doi.org/10.1016/j.bbagen.2011.12...
Subject categories Surgery, Physiology

Abstract

BACKGROUND: Galectins, a family of small carbohydrate binding proteins, have been implicated in regulation of inflammatory reactions, including asthma and fibrosis in the lungs. Galectins are found in cells of the airways and in airway secretions, but their glycoprotein ligands there have only been studied to a very limited extent. METHODS: Bronchoalveolar lavage (BAL) fluid from mild asthmatics and healthy volunteers were fractionated by affinity chromatography on the immobilized galectins. Total (10-30μg) and galectin bound (~1-10μg) protein fractions were identified, quantified and compared using shot-gun proteomics and spectral counts. RESULTS: About 175 proteins were identified in unfractionated BAL-fluid, and about 100 bound galectin-3 and 60 bound galectin-8. These included plasma glycoproteins, and typical airway proteins such as SP-A2, PIGR and SP-B. The concentration of galectin-binding proteins was 100-300 times higher than the concentration of galectins in BAL. CONCLUSION: The low relative concentration of galectins in BAL makes it likely that functional interactions with glycoproteins occur at sites rich in galectin, such as cells of the airways, rather than the extracellular fluid itself. The profile of galectin bound proteins differed between samples from asthma patients and healthy subjects and correlated with the presence of fibroblasts or eosinophils. This included appearance of a specific galectin-8-binding glycoform of haptoglobin, previously shown to be increased in serum in other inflammatory conditions. GENERAL SIGNIFICANCE: It is technically feasible to identify galectin-binding glycoproteins in low concentration patient samples such as BAL-fluid, to generate biomedically interesting results. This article is part of a Special Issue entitled Glycoproteomics.

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