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- W2162578049 endingPage "436" @default.
- W2162578049 startingPage "429" @default.
- W2162578049 abstract "Interleukin-2 (IL-2) is a potent activator of cellular immunity and has been utilized as an immunotherapeutic agent. We stably immobilized human IL-2 to collagen by covalently binding it to the N-terminus of human type III collagen (3A1) as IL2-3A1 chimeric protein using recombinant technology. The present study was aimed at liberating IL-2 from the immobilized chimeric protein by treating the chimera with bacterial collagenase. These IL2-3A1 chimeras were synthesized in insect cells which had been infected with baculovirus vectors carrying IL2-3A1 cDNA. The IL2-3A1 protein produced was shown to be in a pepsin-resistant triple helical structure and exhibited IL-2 activity to a similar extent as IL-2 itself. IL2-3A1 could be immobilized on the surface of plastic dishes by incubating it in the dishes. The IL-2 region of the immobilized IL2-3A1 was liberated to culture media by collagenase treatment and this freed IL-2 stimulated the growth of lined T cells. Thus, IL2-3A1 chimeric protein could be utilized as an IL-2 deliverer whose T cell mitogenic activity can be liberated by a collagenolytic environment." @default.
- W2162578049 created "2016-06-24" @default.
- W2162578049 creator A5051956583 @default.
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- W2162578049 date "2002-05-01" @default.
- W2162578049 modified "2023-09-23" @default.
- W2162578049 title "Interleukin-2-collagen chimeric protein which liberates interleukin-2 upon collagenolysis" @default.
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- W2162578049 doi "https://doi.org/10.1093/protein/15.5.429" @default.
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