Abstract
The modulatory potency of lectins on cellular activities deserves attention from a cell biological and a clinical point-of-view. In addition to serving as tools to delineate signaling processes that follow carbohydrate-dependent cell binding, plant lectins can apparently affect certain characteristics of the host immune system in vitro and in vivo with potential clinical benefit (1,2). With respect to defense mechanisms the generation of reactive oxygen compounds such as the superoxide anion radical (O 2 -) and H2O2 or the release of granule enzymes are supposed to play a notable role (3-6) Deliberate enhancement of these activities by lectins may increase the host’s capacity to control growth of infectious organisms or malignant cells. Therefore, rigorous testing of plants agglutinins and endogenous lectins that have been isolated from human tissues may enable one to devise a rational lectin-mediated treatment modality This chapter describes the protocols for the respective assay procedures used to determine the effects of lectins on production of reactive oxygen compounds and release of granule enzymes
This is a preview of subscription content, log in via an institution to check access.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
References
Gabius, H-J, Gabius, S, Joshi, S S, Koch, B, Schroeder, M, Manzke, W. M,and Westerhausen, M (1994) From Ill-defined extracts to the immunomoduiatorylectin: will there be a reason for oncological application of mtstletoe? Planta Med 60, 2–7
Gabius, H-J (1994) Lectinology meets mythology: oncological future for themistletoe lectin? Trends Glycosci Glycotechnol 6, 229–238.
Boxer, L A. and Smolen, J E. Neutrophtl granule constituents and then release inhealth and disease Hematol. Oncol Clm North Am 2, 101–134
Weiss, S. J. (1989) Tissue destruction by neutrophils N Engl J Med. 320, 365–380
Segal, A W and Abo, A (1993) The brochemical basts of the NADPH oxtdase of phagocytes. Trends Bzochem Sci 18, 43–47
Timoshenko, A V and Cherenkevtch, S. N (1994) Glycobiological aspects ofthe activation of phagocytes’ respiratory cham Blopollmery I Kletka 10, 58–66(in Russian).
Markert, M, Andrews, P. C., and Babior, B in (1984) Measurements of O2-productionby human neutrophils. The preparation and assay of NADPH oxtdase-containingparttcles from human neutrophtls Methods Enzymol 105, 358–365.
Corbett, J. T (1989) The scopoletin assay for hydrogen peroxide. A review and abetter method J Blochem Bzophys Methods 18, 297–308
Timoshenko, A. V and Gabius, H.-J. (1993) Efficient induction of superoxide release from human neutrophils by the galactoside-specific lectin from Viscumalbum Blol.Chem Hoppe Seyler 374, 237–243
Timoshenko, A V., Kayser, K, Drings, P, Kolb, G, Havemann, K, and Gabius, H-J. (1993) Modulation of lectin-triggered superoxide release from neutrophils of tumor patients with and without chemotherapy Anticancer Res 13,1789–1792
Timoshenko, A V and Gabius, H.-J (1995) Influence of the galactose-spectficlectin from Viscum album and Its subumts on cell aggregation and selected mtra-cellularparameters of rat thymocytes Planta Med 61, 130–133.
Bergmeyer, H U (1975) Methoden der enzymatzschen Analyse, vol 1, VerlagChemte, Wemhelm, Germany, pp. 607–623
Fittschen, C. and Henson, P. M. (1994) Linkage of azurophil granule secretion in neutrophils to chloride Ion transport and endosomal transcytosis J Clan Invest 93,247–255
Timoshenko, A V, Kayser, K, Drings, P., Andre, S, Dong, X, Kaltner, H, Schneller, M., and Gabius, H-J. (1995) Carbohydrate-binding protems (plam/humanlectins and autoanttbodres from human serum) as mediators of release of lyso-zyme, elastase, and myeloperoxtdase from human neutrophds Res Exp Med 195,153–162
Barrett, A J (1981) Leukocyte elastase Methods Enzymol 80,581–588
Nakajtma, K, Powers, J. C, Ashe, B. M., and Zimmerman, M. (1979) Mapping the extended substrate binding site of cathepsin G and human leukocyte elastase Studies with peptide substrates related to the a 1-protease inhibitor reactive site.J Biol Chem 254, 4027–4031
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1998 Humana Press Inc.
About this protocol
Cite this protocol
Timoshenko, A.V., Kayser, K., Gabius, HJ. (1998). Lectin-Triggered Superoxide/H2O2 and Granule Enzyme Release from Cells. In: Rhodes, J.M., Milton, J.D. (eds) Lectin Methods and Protocols. Methods in Molecular Medicine™, vol 9. Humana Press. https://doi.org/10.1385/0-89603-396-1:441
Download citation
DOI: https://doi.org/10.1385/0-89603-396-1:441
Publisher Name: Humana Press
Print ISBN: 978-0-89603-396-2
Online ISBN: 978-1-59259-593-8
eBook Packages: Springer Protocols