SELECTIVE AND DIFFERENTIAL BINDING OF INTERLEUKIN (IL)-1-ALPHA, IL-1-BETA, IL-2 AND IL-6 TO GLYCOSAMINOGLYCANS
SELECTIVE AND DIFFERENTIAL BINDING OF INTERLEUKIN (IL)-1-ALPHA, IL-1-BETA, IL-2 AND IL-6 TO GLYCOSAMINOGLYCANS
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DOI:
10.1002/eji.1830221139
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发表时间:
1992-11-01
影响因子:
5.4
通讯作者:
RIDER, CC
中科院分区:
文献类型:
--
作者:
RAMSDEN, L;RIDER, CC
The binding of interleukin (IL)-1alpha, IL-1beta, IL-2 and IL-6 to acidic polysaccharides was investigated by affinity chromatography of the recombinant, radioiodinated interleukins on columns of immobilized polysaccharide. Each interleukin showed selective binding retention. Overall heparin bound all four interleukins significantly, whereas chondroitin sulfate provided little retention. IL-1alpha and IL-1beta showed differential binding, with only the latter binding to hyaluronic acid. IL-2 was virtually completely retained on fucoidan. Noniodinated recombinant IL-2 bound similarly to fucoidan, and fucoidan was found to sequester IL-2 activity in a bioassay employing IL-2-dependent CTLL cells. In all other cases tested, interleukin retention was partial, implying that interleukin binding sites are sparsely distributed along the polysaccharide chains. These findings suggest that during the immune response, interleukins will tend to be retained at sites of secretion by interaction with glycosaminoglycans in the extracellular matrix and on cell surfaces.