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Carbohydrate-binding proteins (plant/human lectins and autoantibodies from human serum) as mediators of release of lysozyme, elastase, and myeloperoxidase from human neutrophils

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Research in Experimental Medicine

Abstract

Analysis of cell surface glycosylation not only provides information about cell properties such as their state of differentiation or histogenetic lineage. The carbohydrate chains also provide potentially functional binding sites to endogenous carbohydrate-binding proteins. This interaction can elicit consequent signalling processes. Because of the importance of neutrophils in the host defence system, we monitored the effect of the binding of such sugar receptors to their cell surface on the release of the enzymatic activities of lysozyme, elastase, and myeloperoxidase. Besides the mannose-binding lectin concanavalin A and the immunomodulatory α/β-galactoside-binding lectin fromViscum album L., three preparations of human sugar receptors—β-galactoside-binding lectin (M r 14 kDa) and two affinity-purified polyclonal IgG fractions from serum with the capacity to recognize α- or β-galactosides, respectively—were used. Two animal lectins from chicken liver and intestine that bind β-galactosides, as well as the lectin-like human serum amyloid P component, were included in order to assess the importance of slight differences in ligand recognition. Cytochalasin B-enhanced enzyme release was invariably seen with the two plant lectins and the chicken liver β-galactoside-binding lectin, but the related intestinal lectin did not increase enzyme release. The mammalian homologue of these avian lectins triggered lysozyme secretion, and the lactoside-binding IgG fraction enhanced the amount of extracellular elastase activity slightly but significantly. Thus, the actual lectin, not the nominal specificity of sugar receptors, is crucial for elucidation of responses. Due to the highly stimulatory activity of the two plant lectins, neutrophils from patients with non-cancerous diseases and from patients with lung cancer were monitored for the extent of lectin-mediated enzyme release. Only the concanavalin A-mediated reactivity of the neutrophils was associated with the type of disease.

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Authors and Affiliations

  1. Department of Biophysics, Belarusian State University, Prospekt F. Skaryny 4, 220050, Minsk, Belarus

    A. V. Timoshenko

  2. Abteilung Pathologie, Thoraxklinik, Amalienstr. 5, D-69126, Heidelberg, Germany

    K. Kayser

  3. Abteilung Innere Medizin, Thoraxklinik, Amalienstr. 5, D-69126, Heidelberg, Germany

    P. Drings

  4. Institu für Physiologische Chemie, Tierärztliche Fakultät, Ludwig-Maximilians-Universität, Veterinärstr. 13, D-80539, München, Germany

    S. André, X. Dong, H. Kaltner, M. Schneller & H. -J. Gabius

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  1. A. V. Timoshenko
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  2. K. Kayser
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  3. P. Drings
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  4. S. André
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  7. M. Schneller
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  8. H. -J. Gabius
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Timoshenko, A.V., Kayser, K., Drings, P. et al. Carbohydrate-binding proteins (plant/human lectins and autoantibodies from human serum) as mediators of release of lysozyme, elastase, and myeloperoxidase from human neutrophils. Res. Exp. Med. 195, 153–162 (1995). https://doi.org/10.1007/BF02576784

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  • DOI: https://doi.org/10.1007/BF02576784

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