Involvement of hyposialylated immunoglobulins in the inactivation of alpha 1-proteinase inhibitor |
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Authors: | M Duc Dodon L Gazzolo |
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Affiliation: | 1. Physical Chemistry 2, Lund University, S-220 07 Lund, Sweden;2. National Institute for Medical Research, Mill Hill, London NW7 1AA, UK |
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Abstract: | The elastase inhibitory capacity of alpha 1-proteinase inhibitor (alpha 1-PI) was measured, using a direct and reproducible method, with phagocytic cells maintained in the tissue culture plate through the assay. The oxidative inactivation of alpha 1-PI is known to be mediated by the action of myeloperoxidase (MPO). The fact that hyposialylated IgG (hs IgG) induce the release of MPO prompted us to investigate the effects of such hs IgG on the inhibitory capacity of alpha 1-PI. The results show that 1-PI inactivation was observed only when phagocytic cells were activated by aggregated hs IgG, and not by unaggregated hs IgG. These observations indicate that hyposialylation should be completed by aggregation to perpetuate the oxidative reactions characteristic of inflammatory diseases. |
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Keywords: | CaM calmodulin ANS 8 anilinonaphthalene sulfonate BAPTA 1,2 bis (o-aminophenoxyl)ethane N,N,N′N′-tetra-acetic acid EDTA ethylene diamine N,N,N′N′-tetra-acetic acid EGTA ethylene glycol bis (β-aminoethyl ether)-N,N,N′,N′-tetra-acetic acid |
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