Binding of interleukin 2 to gangliosides |
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| Authors: | J Parker G Caldini C Krishnamurti P B Ahrens H Ankel |
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| Affiliation: | 1. Department of Biochemistry, Medical College of Wisconsin, Milwaukee, WI 53226 USA;2. Department of Biology, Marquette University, Milwaukee, WI 53223, USA |
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| Abstract: | Exogenous gangliosides inhibit interleukin 2 (IL2)-dependent growth of a T cell line, AKIL -1.E8. IL2 activity is retained by columns of ganglioside covalently linked to poly(L-lysine)-agarose and is not eluted with ethylene glycol but is completely recovered by elution with 1% SDS. The ability of gangliosides to inhibit IL2 activity is directly related to the complexity of their carbohydrate portion, and related ceramide derivatives at similar concentrations do not inhibit IL2 activity. We conclude that IL2 bound to exogenous gangliosides is inactive and that the carbohydrate portion of the ganglioside is crucial to its interaction with IL2. |
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| Keywords: | Interleukin 2 T cell growth factor Lymphokine T cell IL2, interleukin 2 PBS, phosphate buffer EG, ethylene glycol BSA, bovine serum albumin globoside, GalNAcβ1-3Galα1-4Galβ1-4Glc-Cer GD1a, NeuNAcα2-3Galβ1-3GalNAcβ1-4[NeuNAcα2-3]Galβ1-4Glc-Cer GD1b, Galβ1-3GalNAcβ1-4[NeuNAcα2-8 NeuNAcα2-3]Galβ1-4Glc-Cer GT1b, NeuNAcα2-3Galβ1-3[NeuNAcα2-8 NeuNAcα2-3]GalNAcβ1-4Galβ1-4Glc-Cer |
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