Cytokine with antiviral, antiproliferative, and immunomodulatory activity. Produced by leukocytes stimulated by virus, bacteria, or protozoa as part of the immune response; artificially induced by double-stranded RNA. Inhibits protein synthesis and viral replication; enhances cytotoxic activity. Multiple subtypes have been identified which contain ≈166 amino acids and are variably glycosylated; mol wt 16-27.5 kDa. Identification of interferon produced by human leukocytes exposed to virus: I. Gresser, Proc. Soc. Exp. Biol. Med. 108, 799 (1961). Purification and characterization: M. Rubinstein et al., Proc. Natl. Acad. Sci. USA 76, 640 (1979). Prepn by recombinant DNA technology: S. Nagata et al., Nature 284, 316 (1980); D. V. Goeddel et al., ibid. 287, 411 (1980). Comparison of structures and activities of HuIFN-α subtypes: M. Streuli et al., Science 209, 1343 (1980); D. V. Goeddel et al., Nature 290, 20 (1981). Review: A. Meager in Cytokines, A. R. Mire-Sluis, R. Thorpe, Eds. (Academic Press, San Diego, 1998) pp 361-389. Review of pharmacology and clinical efficacy in malignant and viral disease: R. T. Dorr, Drugs 45, 177-211 (1993); of use in metastatic renal cell carcinoma: A. Ravaud, M.-S. Dilhuydy, Expert Opin. Biol. Ther. 5, 749-762 (2005); in chronic hepatitis C: M. Moriyama, Y. Arakawa, Expert Opin. Pharmacother. 7, 1163-1179 (2006).
Recombinant HuIFN-α produced in E. coli. Contains 165 amino acids; mol wt ≈19 kDa. Symposium on clinical antineoplastic activity: Semin. Oncol. 12, Suppl. 5, 1-34 (1985). Review of clinical efficacy in hepatitis C: C. M. Perry, M. I. Wilde, BioDrugs 10, 65-89 (1998).
Recombinant HuIFN-α produced in E. coli. Mol wt ≈19 kDa. Symposium on clinical antineoplastic activity: Invest. New Drugs 5, Suppl, S1-S77 (1987). Clinical trial in hepatitis C: S. Schenker et al., J. Interferon Cytokine Res. 17, 665 (1997).
Clinical trial in chronic myelogenous leukemia: J. Thaler et al., Leuk. Res. 21, 75 (1997); in lung cancer: C. Prior et al., Eur. Respir. J. 10, 392 (1997).
Synthetic, recombinant interferon derived by assigning the most commonly observed amino acid in each position of several alpha IFN subtypes to create a consensus sequence. Contains 166 amino acids; mol wt 19.5 kDa. Molecular characterization and bioactivity: L. M. Blatt et al., J. Interferon Cytokine Res. 16, 489 (1996). Clinical trial in hepatitis C: M. J. Tong et al., Hepatology 26, 747 (1997).
Mixture of natural human α-interferons derived from lymphoblastoid cells exposed to Sendai virus. Review of clinical trials in hepatitis C: G. C. Farrell, Hepatology 26, Suppl. 1, 96S-100S (1997); of pharmacology and clinical efficacy: C. M. Perry, A. J. Wagstaff, BioDrugs 9, 125-154 (1998).
Mixture of natural, human α-interferons produced by human leukocytes exposed to Sendai virus. mol wt 16-27 kDa. Clinical trial in hepatitis C: D. M. Simon et al., Hepatology 25, 445 (1997).
Antiviral; antineoplastic.
Antineoplastic; Immunomodulators; Antiviral