Human interleukin

DPI Ohlendorf. Accuracy of refined protein structures. II. Comparison of four independently refined models of human interleukin 1(1. Acta Cryst 050 808-812, 1994. 

Human interleukin 2, a 133-residue protein, has been separated into multiple molecular forms by selective immunoaffinity chromatography and chromatofocusing. Most of the heterogeneity has been attributed to variations in glycosylation of the threonine residue in position 3 of the polypep-... 

H2O2 The chemical symbol for hydrogen peroxide Hag Haemagglutinin Hag-1, Hag-2 Cleaved haemagglutinin subunits-1, -2 H E Haematoxylin and eosin hIL Human interleukin Hb Haemoglobin... 

Holmes WE, Lee J, Kuang WJ, Rice GC, Wood WI. Structure and functional expression of a human interleukin-8 receptor. Science 1991 253 1278-1280. 

Clubb RT, Omichinski JG, Clore GM, Gronenbom AM. Mapping the binding surface of interleukin-8 complexes with an N-terminal fragment of the type 1 human interleukin-8 receptor. FEBS Lett 1994 338 93-7. 

Kuschert GS, Hoogewerf AJ, Proudfoot AE, et al. Identification of a glycosami-noglycan binding surface on human interleukin-8. Biochemistry 1998 37 11193-201. 

Damaj BB, McColl SR, Neote K, et al. Identification of G-protein binding sites of the human interleukin-8 receptors by functional mapping of the intracellular loops. FASEB J 1996 10(12) 1426-1434. 

Dunstan C-AN, Salafranca MN, Adhikari S, Xia Y, Feng L, Harrison JK. Identification of two rat genes orthologous to the human interleukin-8 receptors. J Biol Chem 1996 271 32770-32776. 

Lee J, Horuk R, Rice GC, Bennett GL, Camerato T, Wood WI. Characterization of two high affinity human interleukin-8 receptors. J Biol Chem 1992 267(23) 16283-16287. 

Morohashi H, Miyawaki T, Nomura H, et al. Expression of both types of human interleukin-8 receptors on mature neutrophils, monocytes, and natural killer cells. J Leukoc Biol 1995 57(1) 180-187. 

Johnson BJ et al. Differential gene expression in response to adjunctive recombinant human interleukin-2 immunotherapy in multidrug-resistant tuberculosis patients. Infect Immunity 1998 66 2426-2433. 

Kratje, R. B., and Wagner, R., Evaluation of Production of Recombinant Human Interleukin-2 in Fluidized Bed Bioreactor, Biotechnol. Bioeng., 39 233... 

Interleukin-12, human Suspension Nicotiana tabacum (tobacco) A. tumefaciens transformation of leaf explant, regenerated plants sexually crossed CaMV 35 S Native human interleukin-12 subunit bOngL-1 (i) 175 pg L-1 (e) 700 ng L 1 (e) with gelatin 60... 

Calcium oxalate monohydrate responsible for the formation of most kidney stones significantly increased mitochondrial superoxide production in renal epithelial cells [42], Recombinant human interleukin IL-(3 induced oxygen radical generation in alveolar epithelial cells, which was suppressed by mitochondrial inhibitors 4 -hydroxy-3 -methoxyacetophe-none and diphenylene iodonium [43]. Espositio et al. [44] found that mitochondrial oxygen radical formation depended on the expression of adenine nucleotide translocator Anti. Correspondingly, mitochondria from skeletal muscle, heart, and brain from the Antl-deficient mice sharply increased the production of hydrogen peroxide. 

Figure 2.8 Three-dimensional structure of (a) human interleukin-4, as determined by NMR, and (b) human follicle-stimulating hormone, as determined by X-ray diffraction. Reproduced from protein data bank (www. rcsb.org/pdb, molecule ID numbers 1ITM and 1 FL7 respectively)...

Kitamura H, Kawata H, Takahashi F, Higuchi Y, Furuichi T, Ohkawa H (1995) Bone marrowneutrophilia and suppressed bone turnover in human interleukin-6 transgenic mice. A cellular relationship among hematopoietic cells, osteoblasts, and osteoclasts mediated by stromal cells in bone marrow. Am J Pathol 147 1682-1692... 

Hora et al. [3.19] described the complexity of protein stabilization by the example of recombinant, human Interleukin-2 (rhIL-2). Formulations with amino acids and mannitol/ sucrose are sensitive to mechanical stress e. g. by pumping. Hydroxypropyl-beta-cyclodextrin (HPcD) provides stability, but increases the sensitivity to oxygen. Polysor-bate 80 forms a mechanically stable product, but results in oxidation. In both cases contamination in the HPcD or traces of H202 in the Polysorbate may have been the starter for the oxidation. Brewster [3.20] reports, that HPcD stabilizes interleukin without forming aggregations and this results in 100 % biopotency. 

Sarmiento, U.M. et al., Biologic effects of recombinant human interleukin-12 in squirrel monkeys (Sciureau saimiri), Lab. Invest., 71, 862, 1994. 

Talmadge, J.E. et al., Systematic preclinical study on the therapeutic properties of recombinant human interleukin 2 for the treatment of metastatic disease, Cancer Res, 47, 5725, 1987. 

Mingari, M.C. et al., Human interleukin-2 promotes proliferation of activated B cells via surface receptors similar to those of activated T cells, Nature, 312, 641, 1984. 

A protein whose degradation pattern is even more difficult to explain is recombinant human interleukin 2 (rhIL-2), a lymphokine produced by T-cells and being developed as an immunomodulator. This protein, which consists... 

R. A. Kenley, N. W. Warne, Acid-Catalyzed Peptide Bond Hydrolysis of Recombinant Human Interleukin 11 , Pharm. Res. 1994, 11, 72-76. 

K. Sasaoki, T. Hiroshima, S. Kusumoto, K. Nishi, Deamidation at Asparagine-88 in Recombinant Human Interleukin 2 , Chem. Pharm. Bull. 1992, 40, 976-980. 

Feng Y., Klein B.K., and McWherter C.A. (1996), Three-dimensional solution structure and backbone dynamics of a variant of human interleukin-3,./. Mol. Biol. 259, 524-541. 

Morton, T.A., D.B. Bennett, E.R. Appelbaum, D.M. Cusimano, K.O. Johanson, R.E. Matico, RR. Young, M. Doyle, and I.M. Chaiken. 1994. Analysis of the interaction between human interleukin-5 and the soluble domain of its receptor using a surface plasmon resonance biosensor. J Mol Recognit 7 47-55. 

Bullock, J. (1993). Capillary zone electrophoresis and packed capillary column liquid-chromatographic analysis of recombinant human interleukin-4. /. Chromatogr. 633, 235—244. 

USP received a medication error report involving the products Neumega (oprel-vekin) and Proleukin (aldesleukin). Oprelvekin, a recombinant human interleukin-11 product used to stimulate platelet production in selected patients undergoing chemotherapy, is sometimes abbreviated as IL-11. Aldesleukin, a recombinant human interleukin-2 derivative indicated in designated patient populations for the treatment of metastatic renal-cell carcinoma, is sometimes abbreviated as IL-2. 

Pharmacology Anakinra is a recombinant, nonglycosylated form of the human interleukin-1 receptor antagonist (IL-1 Ra). Anakinra differs from native human IL-IRa in that it has a single methionine residue at its amino terminus. It is produced by recombinant DNA technology using an Escherichia coli bacterial expression system. 

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