Functional comparison of recombinant interleukin 2 (IL-2) with IL-2-containing preparations derived from cultured cells.
Due to its purity and potential availability in large amounts, human recombinant interleukin 2 (IL-2) expressed in Escherichia coli is an important source of IL-2 for experimentation and possible therapy. To date, very few comparisons between the activity of recombinant IL-2 and conventional cell-derived preparations of IL-2 have been made. This is particularly important since the use of recombinant IL-2 may have some specific limitations. For example, recombinant IL-2 is not post-translationally modified as are cell-derived preparations. Lack of modifications such as glycosylation of threonine 3 may alter efficacy or stability. Comparative studies are necessary to demonstrate the efficacy, species specificity, and stability of recombinant IL-2. By comparing IL-2 activity of recombinant IL-2 to that of cell-derived IL-2, we have demonstrated that each of the preparations are equally active in several murine and human IL-2 proliferation assays and that IL-2 is the active moiety in these assays. In contrast to previous reports, we also show that recombinant IL-2 is sufficient to establish and maintain long-term cell lines. Additionally, by using "synthetic" recombinant IL-2 of defined protein sequence, we have demonstrated that this amino acid-defined structure is indeed responsible for the functions attributed to IL-2.
D000818:Animals; D002455:Cell Division; D002460:Cell Line; D003001:Cloning, Molecular; D004274:DNA, Recombinant; D006801:Humans; D007376:Interleukin-2 / Q000096:biosynthesis / Q000502:physiology; D051379:Mice; D008934:Mitogens; D013329:Structure-Activity Relationship; D013601:T-Lymphocytes / Q000166:cytology; D013997:Time Factors
D004274:DNA, Recombinant; D007376:Interleukin-2; D008934:Mitogens