Aldesleukin, a lymphokine, is produced by way of recombinant DNA technology the use of a genetically engineered E. coli stress containing an analog of the human interleukin-2 gene. Genetic engineering techniques had been used to modify the human IL-2 gene, and the ensuing expression clone encodes a modified human interleukin-2. This recombinant shape differs from native interleukin-2 inside the following approaches: a) Aldesleukin isn't always glycosylated due to the fact it is derived from E. coli; b) the molecule has no N-terminal alanine; the codon for this amino acid changed into deleted for the duration of the genetic engineering process; c) the molecule has serine substituted for cysteine at amino acid function a hundred twenty five.
Used to treat renal cell carcinoma, Aldesleukin induces the enhancement of lymphocyte mitogenesis and stimulation of long-term growth of human interleukin-2 dependent cell lines, the enhancement of lymphocyte cytotoxicity, the induction of killer cell (lymphokine-activated (LAK) and natural (NK)) activity; and the induction of interferon-gamma production. IL-2 is normally produced by the body, secreted by T cells, and stimulates growth and differentiation of T cell response. It can be used in immunotherapy to treat cancer. It enhances the ability of the immune system to kill tumor cells and may interfere with blood flow to the tumor.
For treatment of adults with metastatic renal cell carcinoma.
Aldesleukin binds to the IL-2 receptor which leads to heterodimerization of the cytoplasmic domains of the IL-2R beta and gamma(c) chains, activation of the tyrosine kinase Jak3, and phosphorylation of tyrosine residues on the IL-2R beta chain. These events led to the creation of an activated receptor complex, to which various cytoplasmic signaling molecules are recruited and become substrates for regulatory enzymes (especially tyrosine kinases) that are associated with the receptor. These events stimulate growth and differentiation of T cells.