Interleukin-1, Interleukin-1 Receptors and Interleukin-1 Receptor Antagonist

References

• Colottα F., Dower S. K., Sims J. E., Mantovani A. The type II “decoy” receptor: a novel regulatory pathway for interleukin-1. Immunol. Today 1994; 15: 562–566
   PubMedGoogle Scholar
• Greenfeder S. A., Nunes P., Kwee L., Labow M., Chizzonite R. A., Ju G. Molecular cloning and characterization of a second subunit of the interleukin-1 receptor complex. J. Biol. Chem. 1995; 270: 13757–13765
   PubMed Web of Science ®Google Scholar
• Polan M. L., Loukides J. A., Honig J. Interleukin-1 in human ovarian cells and in peripheral blood monocytes increases during the luteal phase: evidence of a midcycle surge in the human. Am. J. Obstet. Gynecol. 1994; 170: 1000–1006
   PubMedGoogle Scholar
• Stevenson F. T., Torrano F., Locksley R. M., Lovett D. H. Interleukin-1: the patterns of translation and intracellular distribution support alternative secretory mechanisms. J. Cell Physiol. 1992; 152: 223–231
   PubMed Web of Science ®Google Scholar
• Mosley B., Urdal D. L., Prickett K. S., Larsen A., Cosman D., Conlon P. J., Gillis S., Dower S. K. The interleukin-1 receptor binds the human interleukin-1α precursor but not the interleukin-1β precusor. J. Biol. Chem. 1987; 262: 2941–2944
   PubMed Web of Science ®Google Scholar
• Kobayashi Y., Oppenheim J. J., Matsushima K. Human pre-interleukin-1α and b: structural features revealed by limited proteolysis. Chem. Pharmaceut. Bull. 1991; 39: 1513–1517
   PubMedGoogle Scholar
• Kobayashi Y., Yamamoto K., Saido T., Kawasaki H., Oppenheim J. J., Matsushima K. Identification of calcium-activated neutral protease as a processing enzyme of human interleukin 1 alpha. Proc. Natl. Acad. Sci. USA 1990; 87: 5548–5552
   PubMed Web of Science ®Google Scholar
• Miller A. C., Schattenberg D. G., Malkinson A. M., Ross D. Decreased content of the IL-1α processing enzyme calpain in murine bone marrow-derived macrophages after treatment with the bezene metabolite hydroquinone. Tox. Lett. 1994; 74: 177–184
   PubMed Web of Science ®Google Scholar
• Watanabe N., Kobayashi Y. Selective release of a processed form of interleukin-1α. Cytokine 1994; 6: 597–601
   PubMed Web of Science ®Google Scholar
• Andersson J., Bjärk L., Dinarello C. A., Towbin H., Andersson U. Lipopolysaccharide induces human interleukin-1 receptor antagonist and interleukin-1 production in the same cell. Eur. J. Immunol. 1992; 22: 2617–2623
   PubMed Web of Science ®Google Scholar
• Cominelli F., Nast C. C., Clark B. D., Schindler R., Llerena R., Eysselein V. E., Thompson R. C., Dinarello C. A. Interleukin-1 gene expression, synthesis and effect of specific IL-1 receptor blockade in rabbit immune complex colitis. J. Clin. Invest. 1990; 86: 972–980
   PubMed Web of Science ®Google Scholar
• Wakabayashi G., Gelfand J. A., Jung W. K., Connolly R. J., Burke J. F., Dinarello C. A. Staphylococcus epidermidis induces complement activation, tumour necrosis factor and interleukin-1, a shock-like state and tissue injury in rabbits without endotoxemia. J. Clin. Invest. 1991; 87: 1925–1935
   PubMedGoogle Scholar
• Mizel S. B., Kilian P. L., Lewis J. C., Paganelli K. A., Chizzonite R. A. The interleukin 1 receptor. Dynamics of interleukin 1 binding and internalization in T cells and fibroblasts. J. Immunol. 1997; 138: 2906–2912
   Google Scholar
• Curtis B. M., Widmer M. B., deRoos P., Quarnstrom E. E. IL-1 and its receptor are translocated to the nucleus. J. Immunol. 1990; 144: 1295–1303
   PubMed Web of Science ®Google Scholar
• Heguy A., Baldari C., Bush K., Nagele R., Newton R. C., Robb R. J., Horuk R., Telford J. L., Melli M. Internalization and nuclear localization of interleukin 1 are not sufficient for function. Cell Growth Differ. 1991; 2: 311–315
   PubMedGoogle Scholar
• Weizmann M. N., Savage N. Nuclear internalization and DNA binding activities of interleukin-1, interleukin-1 receptor complexes. Biochem. Biophys. Res. Commun. 1992; 187: 1166–1171
   PubMedGoogle Scholar
• Hauser C., Saurat J. H., Schmitt A., Jaunin F., Dayer J.-M. Interleukin-1 is present in normal epidermis. J. Immunol. 1986; 136: 3317–3222
   PubMed Web of Science ®Google Scholar
• Hammerberg C., Arend W. P., Fisher G. J., Chan L. S., Berger A. E., Haskill J. S., Voorhees J. J., Cooper K. D. Interleukin-1 receptor antagonist in normal and psoriatic epidermis. J. Clin. Invest. 1992; 90: 571–583
   PubMedGoogle Scholar
• Kaplanski G., Farnarier C., Kaplanski S., Porat R., Shapiro L., Bongrand P., Dinarello C. A. Interleukin-1 induces interleukin-8 from endothelial cells by a juxacrine mechanism. Blood 1994; 84: 4242–4248
   PubMed Web of Science ®Google Scholar
• Beuscher H. U., Colten H. R. Structure and function of membrane IL-1. Mol. Immunol. 1988; 25: 1189–1195
   PubMed Web of Science ®Google Scholar
• Maier J. A.M., Statuto M., Ragnotti G. Endogenous interleukin-1 alpha must be transported to the nucleus to exert its activity in human endothelial cells. Mol. Cell Biol. 1994; 14: 1845–1851
   PubMed Web of Science ®Google Scholar
• Wessendorf J. H.M., Garfinkel S., Zhan X., Brown S., Maciag T. Identification of a nuclear localization sequence within the structure of the human interleukin-1α precursor. J. Biol. Chem. 1993; 268: 22100–22104
   PubMedGoogle Scholar
• Beuscher H. U., Nickells M. W., Colten H. R. The precursor of interleukin-1α is phosphorylated at residue serine 90. J. Biol. Chem. 1988; 263: 4023–4028
   PubMed Web of Science ®Google Scholar
• Stevenson F. T., Bursten S. L., Fanton C., Locksley R. M., Lovett D. H. The 31-kDa precursor of interleukin-1α is myristoylated on specific lysines within the 16-kDa N-terminal propiece. Proc. Natl. Acad. Sci. USA 1993; 90: 7245–7249
   PubMed Web of Science ®Google Scholar
• Maier J. A.M., Voulalas P., Roeder D., Maciag T. Extension of the life span of human endothelial cells by an interleukin-1α antisense oligomer. Science 1990; 249: 1570–1574
   PubMed Web of Science ®Google Scholar
• Falk W., Hofmeister R. Intracellular IL-1 replaces signaling by the membrane IL-1 type I receptor. Cytokine 1994; 6: 558
   Google Scholar
• Kurt-Jones E. A., Beller D. I., Mizel S. B., Unanue E. R. Identification of a membrane-associated interleukin-1 in macrophages. Proc. Natl. Acad. Sci. USA 1985; 82: 1204–1208
   PubMed Web of Science ®Google Scholar
• Brody D. T., Durum S. K. Membrane IL-1: IL-1α precursor binds to the plasma membrane via a lectin-like interaction. J. Immunol. 1989; 143: 1183
   PubMed Web of Science ®Google Scholar
• Minnich-Carruth L. L., Suttles J., Mizel S. B. Evidence against the existence of a membrane form of murine IL-1α. J. Immunol. 1989; 142: 526
   PubMedGoogle Scholar
• Bailly S., Ferrua B., Fay M., Gougerot-Pocidalo M.-A. Paraformaldehyde fixation of LPS-stimulated human monocytes: technical parameters permitting the study of membrane IL-1 activity. Eur. Cytokine Net 1990; 1: 47–51
   PubMedGoogle Scholar
• Fenton M. J., Vermeulen M. W., Clark B. D., Webb A. C., Auron P. E. Human pro-IL-1 beta gene expression in monocytic cells is regulated by two distinct pathways. J. Immunol. 1988; 140: 2267–2273
   PubMedGoogle Scholar
• Jarrous N., Kaempfer R. Induction of human interleukin-1 gene expression by retinoic acid and its regulation at processing of precursor transcripts. J. Biol. Chem. 1994; 269: 23141–23149
   PubMed Web of Science ®Google Scholar
• Serkkola E., Hurme M. Synergism between protein-kinase C and cAMP-dependent pathways in the expression of the interleukin-1β gene is mediated via the activator-protein-1 (AP-1) enhancer activity. Eur. J. Biochem. 1993; 213: 243–249
   PubMedGoogle Scholar
• Schindler R., Ghezzi P., Dinarello C. A. IL-1 induces IL-1. IV. IFN-γ suppresses IL-1 but not lipopolysaccharide-induced transcription of IL-1. J. Immunol. 1990; 144: 2216–2222
   PubMed Web of Science ®Google Scholar
• Vannier E., Dinarello C. A. Histamine enhances interleukin (IL)-1-induced IL-1 gene expression and protein synthesis via H2 receptors in peripheral blood mononuclear cells: comparison with IL-1 receptor antagonist. J. Clin. Invest. 1993; 92: 281–287
   PubMedGoogle Scholar
• Schindler R., Gelfand J. A., Dinarello C. A. Recombinant C5a stimulates transcription rather than translation of IL-1 and TNF; cytokine synthesis induced by LPS, IL-1 or PMA. Blood 1990; 76: 1631–1638
   PubMed Web of Science ®Google Scholar
• Ghezzi P., Dinarello C. A., Bianchi M., Rosandich M. E., Repine J. E., White C. W. Hypoxia increases production of interleukin-1 and tumor necrosis factor by human mononuclear cells. Cytokine 1991; 3: 189–194
   PubMed Web of Science ®Google Scholar
• Schindler R., Clark B. D., Dinarello C. A. Dissociation between interleukin-1β mRNA and protein synthesis in human peripheral blood mononuclear cells. J. Biol. Chem. 1990; 265: 10232–10237
   PubMed Web of Science ®Google Scholar
• Mileno M. D., Margolis N. H., Clark B. D., Dinarello C. A., Burke J. F., Gelfand J. A. Coagulation of whole blood stimulates interleukin-1β gene expression: absence of gene transcripts in anticoagulated blood. J. Inf. Dis. 1995; 172: 308–311
   PubMedGoogle Scholar
• Schindler R., Linnenweber S., Schulze M., Oppermann M., Dinarello C. A., Shaldon S., Koch K.-M. Gene expression of interleukin-1β during hemodialysis. Kidney Int. 1993; 43: 712–721
   PubMed Web of Science ®Google Scholar
• Kaspar R. L., Gehrke L. Peripheral blood mononuclear cells stimulated with C5a or lipopolysaccharide to synthesize equivalent levels of IL-1β mRNA show unequal IL-1β protein accumulation but similar polyribosome profiles. J. Immunol. 1994; 153: 277–286
   PubMed Web of Science ®Google Scholar
• Miller L. C., Isa S., Vannier E., Georgilis K., Steere A. C., Dinarello C. A. Live Borrelia burgdorferi preferentially activate IL-1β gene expression and protein synthesis over the interleukin-1 receptor antagonist. J. Clin. Invest. 1992; 90: 906–912
   PubMed Web of Science ®Google Scholar
• Stoeckle M. Y., Guan L. High-resolution analysis of gro-α mRNA poly (A) shortening: regulation by interleukin-1β. Nucl. Acid. Res. 1993; 21: 1613–1617
   PubMedGoogle Scholar
• Shapiro L., Panayotatos N., Meydani S. N., Wu D., Dinarello C. A. Ciliary neurotrophic factor combined with soluble receptor inhibits synthesis of proinflammatory cytokines and prostaglandin-E2 in vitro. Exp. Cell. Res. 1994; 215: 51–56
   PubMed Web of Science ®Google Scholar
• Jobling S. A., Auron P. E., Gurka G., Webb A. C., McDonald B., Rosenwasser L. J., Gehrke L. Biological activity and receptor binding of human prointerleukin-1β and subpeptides. J. Biol. Chem. 1988; 263: 16372
   PubMedGoogle Scholar
• Bakouche O., Brown D. C., Lachman L. B. Subcellular localization of human monocyte interleukin 1: evidence for an inactive precursor molecule and a possible mechanism for IL 1 release. J. Immunol. 1987; 138: 4249–4255
   PubMed Web of Science ®Google Scholar
• Rubartelli A., Cozzolino F., Talio M., Sitia R. A novel secretory pathway for interleukin-1 beta, a protein lacking a signal sequence. EM BO J. 1990; 9: 1503–1510
   PubMed Web of Science ®Google Scholar
• Auron P. E., Warner S. J., Webb A. C., Cannon J. G., Bernheim H. A., McAdam K. J., Rosenwasser L. J., LoPreste G., Mucci S. F., Dinarello C. A. Studies on the molecular nature of human interleukin 1. J. Immunol. 1987; 138: 1447–1456
   PubMed Web of Science ®Google Scholar
• Beuscher H. U., Guenther C., Roellinghoff M. IL-1β is secreted by activated murine macrophages as biologically inactive precursor. J. Immunol. 1990; 144: 2179–2183
   PubMedGoogle Scholar
• Black R. A., Kronheim S. R., Cantrell M., Deeley M. C., March C. J., Prickett K. S., Wignall J., Conlon P. J., Cosman D., Hopp T. P. Generation of biologically active interleukin-1 beta by proteolytic cleavage of the inactive precursor. J. Biol. Chem. 1988; 263: 9437–9442
   PubMed Web of Science ®Google Scholar
• Dinarello C. A., Cannon J. G., Mier J. W., Bernheim H. A., LoPreste G., Lynn D. L., Love R. N., Webb A. C., Auron P. E., Reuben R. C., Rich A., Wolff S. M., Putney S. D. Multiple biological activities of human recombinant interleukin 1. J. Clin. Invest. 1986; 77: 1734–1739
   PubMed Web of Science ®Google Scholar
• Mizutani H., Black R. A., Kupper T. S. Human keratinocytes produce but do not process pro-interleukin-1β. J. Clin, invest. 1991; 87: 1066–1071
   PubMed Web of Science ®Google Scholar
• Mizutani H., Schecter N., Zazarus G., Black R. A., Kupper T. S. Rapid and specific conversion of precursor interleukin-1β to an active IL-1 species by human mast cell chymase. J. Exp. Med. 1991; 174: 821–825
   PubMed Web of Science ®Google Scholar
• Hazuda D. J., Strickler J., Kueppers F., Simon P. L., Young P. R. Processing of precursor interleukin-1 beta and inflammatory disease. J. Biol. Chem. 1990; 265: 6318–6322
   PubMed Web of Science ®Google Scholar
• Hazuda D. J., Strickler J., Simon P., Young P. R. Structure-function mapping of interleukin 1 precursors. Cleavage leads to a conformational change in the mature protein. J. Biol. Chem. 1991; 266: 7081–7086
   PubMedGoogle Scholar
• Cerretti D. P., Kozlosky C. J., Mosley B., Nelson N., VanNess K., Greenstreet T. A., March C. J., Kronheim S. R., Druck T., Cannizzaro L. A., Huebner K., Black R. A. Molecular cloning of the IL-1β processing enzyme. Science 1992; 256: 97–100
   PubMed Web of Science ®Google Scholar
• Thornberry N. A., Bull H. G., Calaycay J. R., Chapman K. T., Howard A. D., Kostura M. J., Miller D. K., Molineaux S. M., Weidner J. R., Aunins J., Schmidt J. A., Tocci M. A novel heterodimeric cysteine protease is required for interleukin-1 beta processing in monocytes. Nature 1992; 356: 768–774
   PubMed Web of Science ®Google Scholar
• Wilson K. P., Black J. A., Thomson J. A., Kim E. E., Griffith J. P., Navia M. A., Murcko M. A., Chambers S. P., Aldape R. A., Raybuck S. A., Livingston D. J. Structure and mechanism of interleukin-1β converting enzyme. Nature 1994; 370: 270–275
   PubMed Web of Science ®Google Scholar
• Gu Y., Wu J., Faucheu C., Lalanne J. L., Diu A., Livingston D. L., Su M. S.-S. Interleukin-1β converting enzyme requires oligomerization for activity of processed forms in vivo. EMBO J. 1995; 14: 1923–1931
   PubMed Web of Science ®Google Scholar
• Alnermri E. S., Livingston D. J., Nicholson D. W., Salvesen G., Thonberry N. A., Wong W. W., Yuan J. Human ICE/CED-3 protease nomenclature. Cell 1996; 87: 171
   PubMedGoogle Scholar
• Walker N. P., Talanian R. V., Brady K. D., Dang L. C., Bump N. J., Ferenz C. R., Franklin S., Ghayur T., Hackett M. C., Hammill L. D. Crystal structure of the cysteine protease interleukin-1 beta-converting enzyme: a (p20/p10) 2 homodimer. Cell 1994; 78: 343–352
   PubMed Web of Science ®Google Scholar
• Irmler M., Hertig S., MacDonald H. R., Sadoul R., Becherer J. D., Proudfoot A., Solari R., Tschopp J. Granzyme A is an interleukin-1βconverting enzyme. J. Exp. Med. 1995; 181: 1917–1922
   PubMed Web of Science ®Google Scholar
• Higgins G. C., Foster J. L., Postlethwaite A. E. Interleukin-1 beta propeptide is detected intracellularly and extracellularly when human monocytes are stimulated with LPS in vitro. J. Exp. Med. 1994; 180: 607–614
   PubMedGoogle Scholar
• Higgins G. C., Foster J. L., Postlethwaite A. E. Synthesis and biological activity of human interleukin-1β propiece in vitro. Arthrit. Rheumat. 1993; 39: S153.
   Google Scholar
• Rubartelli A., Bajetto A., Allavena G., Wollman E., Sitia R. Secretion of thioredoxin by normal and neoplastic cells through a leaderless secretory pathway. J. Biol. Chem. 1992; 267: 24161–24164
   PubMed Web of Science ®Google Scholar
• Mignatti P., Rifkin D. B. Release of basic fibroblast growth factor, an angiogenic factor devoid of secretory signal sequence: a trivial phenomenon or a novel secretion mechanism?. J. Cell Biochem. 1991; 47: 201–217
   PubMed Web of Science ®Google Scholar
• Singer I. I., Scott S., Chin J., Kostura M. J., Miller D. K., Chapman K., Bayne E. K. Interleukin-1β converting enzyme is localized on the external cell-surface membranes and in the cytoplasmic ground substance of activated human monocytes by immuno-electronmicroscopy. Lymphokine Cytokine Res. 1993; 12: 340, abs
   Google Scholar
• Li P., Allen H., Banerjee S., Franklin S., Herzog L., Johnston C., McDowell J., Paskind M., Rodman L., Salfeld J., Towne E., Tracey D., Wardwell S., Wei F. Y., Wong W., Kamen R., Seshadri T. Mice deficient in interleukin-1 converting enzyme (ICE) are defective in production of mature interleukin-1β and resistant to endotoxic shock. Cell 1995; 80: 401–411
   PubMed Web of Science ®Google Scholar
• Kuida K., Lippke J. A., Ku G., Harding M. W., Livingston D. J., Su M. S.-S., Flavell R. A. Altered cytokine export and apoptosis in mice deficient in interleukin-1β converting enzyme. Science 1995; 267: 2000–2003
   PubMed Web of Science ®Google Scholar
• Dinarello C. A., Ikejima T., Warner S. J., Orencole S. F., Lonnemann G., Cannon J. G., Libby P. Interleukin 1 induces interleukin 1. I. Induction of circulating interleukin 1 in rabbits in vivo and in human mononuclear cells in vitro. J. Immunol. 1987; 139: 1902–1910
   PubMed Web of Science ®Google Scholar
• Nakamura K., Okamura H., Wada M., Nagata K., Tamura T. Endotoxin-induced serum factor that stimulates gamma inteferon production. Inf. Immun. 1989; 57: 590–595
   PubMed Web of Science ®Google Scholar
• Nakamura K., Okamura H., Nagata K., Komatsu T., Tamura T. Purification of a factor which provides a costimulatory signal for gamma interferon production. Inf. Immun. 1993; 61: 64–70
   PubMed Web of Science ®Google Scholar
• Okamura H., Nagata K., Komatsu T., Tanimoto T., Nukata Y., Tanabe F., Akita K., Torigoe K., Okura T., Fukuda S., Kurimoto M. A novel costimulatory factor for gamma interferon induction found in the livers of mice causes endotoxic shock. Infect. Immun. 1995; 63: 3966–3972
   PubMed Web of Science ®Google Scholar
• Okamura H., Tsutsui H., Komatsu T., Yutsudo M., Hakura A., Tanimoto T., Torigoe K., Okura T., Nukada Y., Hattori K., Akita K., Namba M., Tanabe F., Konishi K., Fukuda S., Kurimoto M. Cloning of a new cytokine that induces interferon-γ. Nature 1995; 378: 88–91
   PubMed Web of Science ®Google Scholar
• Heremans H., vanDamme J., Dillen C., Dikman R., Billiau A. Interferon-γ, a mediator of lethal lipopolysaccharide-induced Shwartzman-like shick in mice. J. Exp. Med. 1990; 171: 1853–1861
   PubMed Web of Science ®Google Scholar
• Car B. D., Eng V. M., Schnyder B., Ozmen L., Huang S., Gallay P., Heumann D., Aguet M., Ryffel B. Interferon γ receptor deficient mice are resistant to endotoxic shock. J. Exp. Med. 1994; 179: 1437–1444
   PubMed Web of Science ®Google Scholar
• Ushio S., Namba M., Okura T., Hattori K., Nukada Y., Akita K., Tanabe F., Konishi K., McAllef M., Fujii M., Torigoe K., Tanimoto T., Fukuda S., Ikeda M., Okamura H., Kurimoto M. Cloning of the cDNA for human IFN-γ-inducing factor, expression in Escherichia coli, and studies on the biologic activities of the protein. J. Immunol. 1996; 156: 4274–4279
   PubMed Web of Science ®Google Scholar
• Kohno K., Kataoka J., Ohtsuki T., Suemoto Y., Okamoto I., Usui M., Ikeda M., Kurimoto M. IFN-γ-inducing factor (IGIF) is a co-stimulatory factor on the activation of Th1 but not Th2 cells and exerts its effect independently of IL-12. J. Immunol. 1997; 158: 1541–1550
   PubMed Web of Science ®Google Scholar
• Tsutsui H., Nakanishi K., Matsui K., Higashino K., Okamura H., Miyazawa Y., Kaneda K. IFN-γ-inducing factor up-regulates Fas ligand-mediated cytotoxic activity of murine natural killer cell clones. J. Immunol. 1996; 157: 3967–3973
   PubMed Web of Science ®Google Scholar
• Bazan J. F., Timans J. C., Kaselein R. A. A newly defined interleukin-1?. Nature 1996; 379: 591
   PubMed Web of Science ®Google Scholar
• Gu Y., Kuida K., Tsutsui H., Ku G., Hsiao K., Fleming M. A., Hayashi N., Higashino K., Okamura H., Nakanishi K., Kurimoto M., Tanimoto T., Flavell R. A., Sato V., Harding M. W., Livingston D. L., Su M. S.-S. Activation of interferon-γ inducing factor mediated by interleukin-1/3 converting enzyme. Science 1997; 275: 206–209
   PubMed Web of Science ®Google Scholar
• Yuan J., Shaam S., Ledoux S., Ellis H. M., Horvitz H. R. The C. elegans cell death gene ced-3 encodes a protein similar to mammalian interleukin-1β-converting enzyme. Cell 1993; 75: 641–652
   PubMed Web of Science ®Google Scholar
• Kumar S., Kinoshita M., Noda M., Copeland N. G., Jenkins N. A. Induction of apoptosis by the mouse Nedd 2 gene, which encodes a protein similar to the product of the Caenorhabditis elegans cell death gene ced-3 and mammalian IL-1β converting enzyme. Genes Dev. 1994; 8: 1613–1626
   PubMed Web of Science ®Google Scholar
• Fernandes-Alnemri T., Litwack G., Alnemri E. S. CPP32, a novel human apoptotic protein with homology to Caenorhabditis elegans cell death protein Ced-3 and mammalian interleukin-1β converting enzyme. J. Biol. Chem. 1994; 269: 30761–30764
   PubMed Web of Science ®Google Scholar
• Miura M., Zhu H., Rotello R., Hartwieg E. A., Yuan J. Induction of apoptosis in fibroblasts by IL-1β converting enzyme, a mammalian homolog of the C. elegans cell death gene ced-3. Cell 1993; 75: 653–660
   PubMed Web of Science ®Google Scholar
• Faucheu C., Diu A., Chan A. W.E., Blanchet A. M., Miossec C., Hervé F., Collard-Dutilleul V., Gu Y., Aldape R. A., Lippke J. A., Rocher C., Su M. S.-S., Livingston D. L., Hercend T., Lalanne J.-L. A novel human protease similar to the interleukin-1β converting enzyme induces apoptosis in transfected cells. EMBO J. 1995; 14: 1914–1922
   PubMed Web of Science ®Google Scholar
• Ray C. A., Black R. A., Kronheim S. R., Greenstreet T. A., Sleath P. R., Salvesen G. S., Pickup D. J. Viral inhibition of inflammation: cowpox virus encodes an inhibitor of the interleukin-1β converting enzyme. Cell 1992; 69: 597–604
   PubMed Web of Science ®Google Scholar
• Gagliardini V., Fernandez P. A., Lee R. K.K., Drexler H. C.A., Rotello R. J., Fishman M. C., Yuan J. Prevention of vertibrate death by the crmA gene. Science 1994; 263: 826–828
   PubMed Web of Science ®Google Scholar
• Enari M., Hug H., Nagata S. Involvement of an ICE-like protease in Fasmediated apoptosis. Nature 1995; 375: 78–81
   PubMed Web of Science ®Google Scholar
• Smith D. J., McGuire M. J., Tocci M. J., Thiele D. L. IL-1β convertase (ICE) does not play a requisite role in apoptosis induced in T lymphoblasts by Fas-dependent or Fas-independent CTL effector mechanisms. J. Immunol. 1997; 158: 163–170
   PubMedGoogle Scholar
• Gu Y., Sarnecki C., Aldape R. A., Livingston D. L., Su M. S. Cleavage of poly (ADP-ribose) polymerase by interleukin-1 beta converting enzyme and its homologs TX and Nedd-2. J. Biol. Chem. 1995; 270: 18715–18718
   PubMed Web of Science ®Google Scholar
• Margolis N. H., Dinarello C. A. Incorporation of 3-H-thymidine by peripheral blood mononuclear cells from normal subjects and acute myelogenous leukemia patients is independent of interleukin-1β converting enzyme. Cytokine 1994; 6: 566, abs
   Google Scholar
• Estrov Z., Black R. A., Kurzrock R., Wetzler M., Sleath P. R., Estey E. H., Harris D., Van Q., Talpaz M. IL-1β converting enzyme (ICE) inhibitor suppresses AML blast proliferation. Blood 1994; 84: 380A.
   PubMedGoogle Scholar
• Stosic-Grujicic S., Basara N., Milenkovic P., Dinarello C. A. Modulation of acute myeloblasts leukemia (AML) cell proliferation and blast colony formation by antisense oligomer of IL-1 beta converting enzyme (ICE) and IL-1 receptor antagonist (IL-1ra). J. Chemother. 1995; 7: 67–70
   PubMed Web of Science ®Google Scholar
• Cozzolino F., Rubartelli A., Aldinucci D., Sitia R., Torcia M., Shaw A., DiGuglielmo R. Interleukin 1 as an autocrine growth factor for acute myeloid leukemia cells. Proc. Natl. Acad. Sci. USA 1989; 86: 2369–2373
   PubMed Web of Science ®Google Scholar
• Arend W. P. Interleukin-1 receptor antagonist. Adv. Immunol. 1993; 54: 167–227
   PubMed Web of Science ®Google Scholar
• Haskill S., Martin M., VanLe L., Morris J., Peace A., Bigler C. F., Jaffe G. J., Sporn S. A., Fong S., Arend W. P., Ralph P. cDNA cloning of a novel form of the interleukin-1 receptor antagonist associated with epithelium. Proc. Natl. Acad. Sci. USA 1991; 88: 3681–3685
   PubMed Web of Science ®Google Scholar
• Vigers G. P., Caffes P., Evans R. J., Thompson R. C., Eisenberg S. P., Brandhuber B. J. X-ray structure of interleukin-1 receptor antagonist at 2.0-Å resolution. J. Biol. Chem. 1994; 269: 12874–12879
   PubMedGoogle Scholar
• Preistle J. P., Schar H. P., Grutter M. G. Crystallography refinement of interleukin 1 beta at 2.0 Å resolution. Proc. Natl. Acad. Sci. USA 1989; 86: 9667–9671
   PubMedGoogle Scholar
• Graves B. J., Hatada M. H., Hendrickson W. A., Miller J. K., Madison V. S., Satow Y. Structure of interleukin-1α at 2.7 Å resolution. Biochem. 1990; 29: 2679–2684
   PubMed Web of Science ®Google Scholar
• Murzin A. G., Lesk A. M., Chothia C. β-trefoil fold. Patterns of structure and sequence in the Kunitz inhibitors interleukins-1β and 1α and fibroblast growth factors. J. Mol. Biol. 1992; 223: 531–543
   PubMed Web of Science ®Google Scholar
• Schreuder H. Crystal structure of the interleukin-1 receptor antagonist complex. Cytokine 1995; 7: 599, abs
   Google Scholar
• Gruetter M. G., vanOostrum J., Priestle J. P., Edelmann E., Joss U., Feige U., Vosbeck K., Schmitz A. A mutational analysis of receptor binding sites of interleukin-1β: differences in binding of human interleukin-1β muteins to human and mouse receptors. Protein Eng. 1994; 7: 663–671
   PubMedGoogle Scholar
• Lambriola-Tomkins E., Chandran C., Varnell T. A., Madison V. S., Ju G. Structure-function analysis of human IL-1α: identification of residues required for binding to the human type I IL-1 receptor. Protein Eng. 1993; 6: 535–539
   PubMedGoogle Scholar
• Evans R. J., Bray J., Childs J. D., Vigers G. P.A., Brandhuber B. J., Skalicky J. J., Thompson R. C., Eisenberg S. P. Mapping receptor binding sites in the IL-1 receptor antagonist and IL-1β by site-directed mutagenesis: identification of a single site in IL-1ra and two sites in IL-1β. J. Biol. Chem. 1994; 270: 11477–11483
   Google Scholar
• Dripps D. J., Brandhuber B. J., Thompson R. C., Eisenberg S. P. Effect of IL-1ra on IL-1 signal transduction. J. Biol. Chem. 1991; 266: 10331–10336
   PubMed Web of Science ®Google Scholar
• Bird T. A., Saklatvala J. IL-1 and TNF transmodulate epidermal growth factor receptors by a protein kinase C-independent mechanism. J. Immunol. 1989; 142: 126–133
   PubMedGoogle Scholar
• Crown J., Jakubowski A., Kemeny N., Gordon M., Gasparetto C., Wong G., Toner G., Meisenberg B., Botet J., Applewhite J., Sinha S., Moore M., Kelsen D., Buhles W., Gabrilove J. A phase I trial of recombinant human interleukin-1β alone and in combination with myelosuppressive doses of 5-fluoruracil in patients with gastrointestinal cancer. Blood 1991; 78: 1420–1427
   PubMed Web of Science ®Google Scholar
• Smith J. W., Urba W. J., Curti B. D., Elwood L. J., Steis R. G., Janik J. E., Sharfman W. H., Miller L. L., Fenton R. G., Conlon K. C., Rossio J., Kopp W., Shimuzut M., Oppenheim J. J., Longo D. Phase II trial of interleukin-1 alpha in combination with indomethacin in melanoma patients. Proc. Am. Soc. Clin. Oncol. 1991; 10: 293, abs
   Google Scholar
• Granowitz E. V., Porat R., Mier J. W., Pribble J. P., Stiles D. M., Bloedow D C, Catalano M. A., Wolff S. M., Dinarello C. A. Pharmacokinetics, saftey, and immunomodulatory effects of human recombinant interleukin-1 receptor antagonist in healthy humans. Cytokine 1992; 4: 353–360
   PubMed Web of Science ®Google Scholar
• Greenfeder S. A., Varnell T., Powers G., Lombard-Gillooly K., Shuster D., McLntyre K. W., Ryan D. E., Leven W., Madison V., Ju G. Insertion of a structural domain of interleukin-1β confers agonist activity to the IL-1 receptor antagonist. J. Biol. Chem. 1995; 270: 22460–22465
   PubMedGoogle Scholar
• Gehrke L., Jobling S. A., Paik L. S., McDonald B., Rosenwasser L. J., Auron P. E. A point mutation uncouples human interleukin-1β biological activity and receptor binding. J. Biol. Chem. 1990; 265: 5922–5925
   PubMed Web of Science ®Google Scholar
• Simoncsits A., Bristulf J., Tjornhammar M. L., Cserzo M., Pongor S., Rybakina E., Gatti S., Bartfai T. Deletion mutants of human IL-1β with significantly reduced agonist properties: search for the agonist/antgonist switch in ligands to the interleukin-1 receptors. Cytokine 1994; 6: 206–214
   PubMedGoogle Scholar
• Tewari A., Buhles W. C., Jr., Starnes H. F. Jr. Preliminary report: effects of interleukin-1 on platelet counts. Lancet 1990; 336: 712–714
   PubMed Web of Science ®Google Scholar
• Sims J. E., March C. J., Cosman D., Widmer M. B., MacDonald H. R., McMahan C. J., Grubin C. E., Wignall J. M., Jackson J. L., Call S. M., et al. cDNA expression cloning of the IL-1 receptor, a member of the immunoglobulin superfamily. Science 1988; 241: 585–589
   PubMed Web of Science ®Google Scholar
• McMahon C. J., Slack J. L., Mosley B., Cosman D., Lupton S. D., Brunton L. L., Grubin C. E., Wignall J. M., Jenkins N. A., Brannan C. I., Copeland N. G., Huebner K., Croce C. M., Cannizzaro L. A., Benjamin D., Dower S., Spriggs M. K., Sims J. E. A novel IL-1 receptor cloned form B cells by mammalian expression is exprressed in many cell types. EMBO J. 1991; 10: 2821–2832
   PubMedGoogle Scholar
• Kroggel R., Martin M., Pingoud V., Dayer J.-M., Resch K. Two-chain structure of the interleukin-1 receptor. FEBS Lett. 1988; 229: 59–62
   PubMedGoogle Scholar
• Bird T. A., Gearing A. J., Saklatvala J. Murine interleukin-1 receptor: differences in binding properties between fibroblastic and thymoma cells and evidence for a two-chain receptor model. FEBS Lett. 1987; 225: 21–26
   PubMedGoogle Scholar
• Savage N., Puren A. J., Orencole S. F., Ikejima T., Clark B. D., Dinarello C. A. Studies on IL-1 receptors on D10S T-helper cells: demonstration of two molecularly and antigenically distinct IL-1 binding proteins. Cytokine 1989; 1: 23–25
   PubMedGoogle Scholar
• Sims J. E., Painter S. L., Gow I. R. Genomic organization of the type I and type II IL-1 receptors. Cytokine 1995; 7: 483–490
   PubMedGoogle Scholar
• Bergers G., Reikerstorfer A., Braselmann S., Graninger P., Busslinger M. Alternative promoter usage of the Fos-responsive gene Fit-1 generates mRNA isoforms coding for either secreted or membrane-bound proteins related to the IL-1 receptor. EMBO J. 1994; 13: 1176–1188
   PubMed Web of Science ®Google Scholar
• Reikerstorfer A., Holtz H., Stuynnenberg H. G., Busslinger M. Low affinity binding of interleukin-1 beta and intracellular signaling via NFKB identify Fit-1 as a distant member of the interleukin-1 receptor family. J. Biol. Chem. 1995; 270: 17645–17648
   PubMedGoogle Scholar
• Hopp T. P. Evidence from sequence information that the interleukin-1 receptor is a transmembrane GTPase. Protein Sci. 1995; 4: 1851–1859
   PubMedGoogle Scholar
• Mancilla J., Ikejima I., Dinarello C. A. Glycosylation of the interleukin-1 receptor type I is required for optimal binding of interleukin-1. Lymphokine Cytokine Res. 1992; 11: 197–205
   PubMedGoogle Scholar
• Rosoff P. M., Savage N., Dinarello C. A. Interleukin-1 stimulates diacylglycerol production in T lymphocytes by a novel mechanism. Cell 1988; 54: 73–81
   PubMed Web of Science ®Google Scholar
• Shirakawa F., Tanaka Y., Ota T., Suzuki H., Eto S., Yamashita U. Expression of interleukin-1 receptors on human peripheral T-cells. J. Immunol. 1987; 138: 4243–4248
   PubMedGoogle Scholar
• Stylianou E., O'Neill L. A.J., Rawlinson L., Edbrooke M. R., Woo P., Saklatvala J. Interleukin-1 induces NFkB through its type I but not type II receptor in lymphocytes. J. Biol. Chem. 1992; 267: 15836–15841
   PubMedGoogle Scholar
• Dower S. K., Fanslow W., Jacobs C., Waugh S., Sims J. E., Widmer M. B. Interleukin-1 antagonists. Therapeutic Immunol. 1994; 1: 113–122
   PubMedGoogle Scholar
• Sims J. E., Gayle M. A., Slack J. L., Alderson M. R., Bird T. A., Giri J. G., Colotta F., Re F., Mantovani A., Shanebeck K., Grabstein K. H., Dower S. K. Interleukin-1 signaling occurs exclusively via the type I receptor. Proc. Natl. Acad. Sci. USA 1993; 90: 6155–6159
   PubMed Web of Science ®Google Scholar
• Sims J. E., Giri J. G., Dower S. K. The two interleukin-1 receptors play different roles in IL-1 activities. Clin. Immunol. Immunopathol. 1994; 72: 9–14
   PubMedGoogle Scholar
• Burch R. M., Mahan L. C. Oligonucleotides antisense to the interleukin-1 receptor mRNA block the effects of interleukin-1 in cultured murine and human fibroblasts and in mice. J. Clin. Invest. 1991; 88: 1190–1196
   PubMedGoogle Scholar
• Gallis B., Prickett K. S., Jackson J., Slack J., Schooley K., Sims J. E., Dower S. K. IL-1 induces rapid phosphorylation of the IL-1 receptor. J. Immunol. 1989; 143: 3235–3240
   PubMed Web of Science ®Google Scholar
• Gay N. J., Keith F. J. Drosophila Toll and IL-1 receptor. Nature 1991; 351: 355–356
   PubMed Web of Science ®Google Scholar
• Guida S., Heguy A., Melli M. The chicken IL-1 receptor: differential evolution of the cytoplasmic and extracellular domains. Gene 1992; 111: 239–243
   PubMed Web of Science ®Google Scholar
• Heguy A., Baldari Macchia C. T.-G., Telford J. L., Melli M. Amino acids conserved in interleukin-1 receptors and the Drosophila Toll protein are essential for IL-1R signal transduction. J. Biol. Chem. 1992; 267: 2605–2609
   PubMedGoogle Scholar
• Slack J., McMahan C. J., Waugh S., Schooley K., Spriggs M. K., Sims J. E., Dower S. K. Independent binding of interleukin-1 alpha and interleukin-1 beta to type I and type II interleukin-1 receptors. J. Biol. Chem. 1993; 268: 2513–2524
   PubMedGoogle Scholar
• Colotta F., Re F., Muzio M., Bertini R., Polentarutti N., Sironi M., Giri J., Dower S. K., Sims J. E., Mantovani A. Interleukin-1 type II receptor: a decoy target for IL-1 that is regulated by IL-4. Science 1993; 261: 472–475
   PubMed Web of Science ®Google Scholar
• Heguy A., Baldari C. T., Censini S., Ghiara P., Telford J. L. A chimeric type II/I interleukin-1 receptor can mediate interleukin-1 induction of gene expression in T cells. J. Biol. Chem. 1993; 268: 10490–10494
   PubMedGoogle Scholar
• Giri J., Newton R. C., Horuk R. Identification of soluble interleukin-1 binding protein in cell-free supernatants. J. Biol. Chem. 1990; 265: 17416–17419
   PubMedGoogle Scholar
• Arend W. P., Malyak M., Smith M. F., Whisenand T. D., Slack J. L., Sims J. E., Giri J. G., Dower S. K. Binding of IL-1α, IL-1β, and IL-1 receptor antagonist by soluble IL-1 receptors and levels of soluble IL-1 receptors in synovial fluids. J. Immunol. 1994; 153: 4766–4774
   PubMed Web of Science ®Google Scholar
• Orencole S. F., Vannier E., Dinarello C. A. Detection of soluble IL-1 receptor type II (IL-1sRII) in sera and plasma from healthy volunteers. Cytokine 1994; 6: 554, abs
   Google Scholar
• Symons J. A., Young P. A., Duff G. W. The soluble interleukin-1 receptor: ligand binding properties and mechanisms of release. Lymphokine Cytokine Res. 1993; 12: 381
   Google Scholar
• Symons J. A., Eastgate J. A., Duff G. W. Purification and characterization of a novel soluble receptor for interleukin-1. J. Exp. Med. 1991; 174: 1251–1254
   PubMed Web of Science ®Google Scholar
• Giri J. G., Wells J., Dower S. K., McCall C. E., Guzman R. N., Slack J., Bird T. A., Shanebeck K., Grabstein K. H., Sims J. E., Alderson M. R. Elevated levels of shed type II IL-1 receptor in sepsis. J. Immunol. 1994; 153: 5802–5813
   PubMed Web of Science ®Google Scholar
• Orencole S. F., Fantuzzi G., Vannier E., Dinarello C. A. Circulating levels of IL-1 soluble receptors in health and after endotoxin or IL-2. Cytokine 1995; 7: 642
   Google Scholar
• Leitman D. C., Andersen J. W., Kuno T., Kamisaki Y., Chang J., Murad F. Identification of multiple binding sites for atrial natriuretic factor by affinity cross-linking in cultured endothelial cells. J. Biol. Chem. 1986; 261: 11650–11656
   PubMedGoogle Scholar
• Alcami A., Smith G. L. A soluble receptor for interleukin-1β encoded by vaccinia virus: a novel mechanism of virus modulation of the host response to infection. Cell 1992; 71: 153–167
   PubMed Web of Science ®Google Scholar
• Spriggs M. K., Hruby D. E., Maliszewski C. R., Pickup D. J., Sims J. E., Buller R. M., VanSlyke J. Vaccinia and cowpox viruses encode a novel secreted interleukin-1 binding protein. Cell 1992; 71: 145–152
   PubMed Web of Science ®Google Scholar
• Laughlin M. J., Kirkpatrick G., Sabiston N., Peters W., Kurtzberg J. Hematopoietic recovery following high-dose combined alkylating-agent chemotherapy and autologous bone marrow support in patients in phase I clinical trials of colony stimulating factors: G-CSF, GM-CSF, IL-1, IL-2 and M-CSF. Ann. Hematol. 1993; 67: 267–276
   PubMedGoogle Scholar
• Kitamura T., Takaku F. A preclinical and Phase I clinical trial of IL-1. Exp. Med. 1989; 7: 170–177
   Google Scholar
• Nemunaitis J., Appelbaum F. R., Lilleby K., Buhles W. C., Rosenfeld C., Zeigler Z. R., Shadduck R. K., Singer J. W., Meyer W., Buckner C. D. Phase I study of recombinant interleukin-1β in patients undergoing autologous bone marrow transplantation for acute myelogenous leukemia. Blood 1994; 83: 3473–3479
   PubMed Web of Science ®Google Scholar
• Smith J. W., Urba W. J., Curti B. D., Elwood L. J., Steis R. G., Janik J. E., Sharfman W. H., Miller L. L., Fenton R. G., Conlon K. C., Rossio J., Kopp W., Shimuzut M., Oppenheim J. J., Longo D. The toxic and hematologic effects of interleukin-1 alpha administered in a phase I trial to patients with advanced malignancies. J. Clin. Oncol. 1992; 10: 1141–1152
   PubMed Web of Science ®Google Scholar
• Iizumi T., Sato S., Iiyama T., Hata R., Amemiya H., Tomomasa H., Yazaki T., Umeda T. Recombinant human interleukin-1 beta analogue as a regulator of hematopoiesis in patients receiving chemotherapy for urogenital cancers. Cancer 1991; 68: 1520–1523
   PubMed Web of Science ®Google Scholar
• Smith J. W., Longo D., Alford W. G., Janik J. E., Sharfman W. H., Gause B. L., Curti B. D., Creekmore S. P., Holmlund J. T., Fenton R. G., Sznol M., Miller L. L., Shimzu M., Oppenheim J. J., Fiem S. J., Hursey J. C., Powers G. C., Urba W. J. The effects of treatment with interleukin-1α on platelet recovery after high-dose carboplatin. N. Engl. J. Med. 1993; 328: 756–761
   PubMed Web of Science ®Google Scholar
• Starnes H. F. Biological effects and possible clinical applications of interleukin-1. Semin. Hematol. 1991; 28: 43–41
   PubMedGoogle Scholar
• van der Poll T., Bueller H. R., tenCate H., Wortel C. H., Bauer K. A., vanDeventer S. J.H., Hack C. E., Sauerwein H. P., Rosenberg R. D., Cateten J. W. Activation of coagulation after administration of tumor necrosis factor to normal subjects. N. Engl. J. Med. 1990; 322: 1622–1627
   PubMed Web of Science ®Google Scholar
• Tilg H., Trehu E., Atkins M. B., Dinarello C. A., Mier J. W. Interieukin-6 (IL-6) as an anti-inflammatory cytokine: Induction of circulating IL-1 receptor antagonist and soluble tumor necrosis factor receptor p55. Blood 1994; 83: 113–118
   PubMed Web of Science ®Google Scholar
• Tilg H., Trehu E., Shapiro L., Pape D., Atkins M. B., Dinarello C. A., Mier J. W. Induction of circulating soluble tumour necrosis factor receptor and interleukin 1 receptor antagonist following interleukin-1α infusion in humans. Cytokine 1994; 6: 215–219
   PubMedGoogle Scholar
• Bargetzi M. J., Lantz M., Smith C. G., Torti F. M., Olsson I., Eisenberg S. P., Starnes H. F. Interleukin-1 beta induces interleukin-1 receptor antagonist and tumor necrosis factor binding proteins. Cancer Res. 1993; 53: 4010–4013
   PubMed Web of Science ®Google Scholar
• Shapiro L., Clark B. D., Orencole S. F., Poutsiaka D. D., Granowitz E. V., Dinarello C. A. Detection of tumor necrosis factor soluble receptor p55 in blood samples from healthy and endotoxemic humans. J. Infect. Dis. 1993; 167: 1344–1350
   PubMedGoogle Scholar
• Granowitz E. V., Santos A., Poutsiaka D. D., Cannon J. G., Wilmore D. A., Wolff S. M., Dinarello C. A. Circulating interleukin-1 receptor antagonist levels during experimental endotoxemia in humans. Lancet 1991; 338: 1423–1424
   PubMed Web of Science ®Google Scholar
• Wolff S. M. Biological effects of bacterial endotoxins in man. J. Infect. Dis. 1973; 128(suppl)733–758
   Google Scholar
• Porat R., Poutsiaka D. D., Miller L. C., Granowitz E. V., Dinarello C. A. Interleukin-1 (IL-1) receptor blockade reduces endotoxin and Borrelia burgdorferi-stimulated IL-8 synthesis in human mononuclear cells. FASEB J. 1992; 6: 2482–2486
   PubMed Web of Science ®Google Scholar
• Norman J. G., Franz M. G., Messina J., Riker A., Fabri P. J., Rosemurgy A. S., Gower W. R. Interleukin-1 receptor antagonist decreases severity of experimental acute pancreatitis. Surgery 1995; 117: 648–655
   PubMed Web of Science ®Google Scholar
• Norman J. G., Franz M. G., Fink G. S., Messina J., Fabri P. J., Gower W. R., Carey L. C. Decreased mortality of severe acute pancreatitis after proximal cytokine blockade. Ann. Surg. 1995; 221: 625–634
   PubMed Web of Science ®Google Scholar
• Vidal-Vanaclocha F., Amézaga C., Asumendi A., Kaplanski G., Dinarello C. A. Interleukm-1 receptor blockade reduces the number and size of murine B16 melanoma hepatic metastases. Cancer Res. 1994; 54: 2667–2672
   PubMed Web of Science ®Google Scholar
• Kaplanski G., Porat R., Aiura K., Erban J. K., Gelfand J. A., Dinarello C. A. Activated platelets induce endothelial secretion of interleukin-8 in vitro via an interleukin-1-mediated event. Blood 1993; 81: 2492–2495
   PubMedGoogle Scholar
• Aiura K., Gelfand J. A., Wakabayashi G., Burke J. F., Thompson R. C., Dinarello C. A. Interleukin-1 (IL-1) receptor antagonist prevents Staphylococcus epidermidis-induced hypotension and reduces circulating levels of tumor necrosis factor and IL-1β in rabbits. Infect. Immun. 1993; 61: 3342–3350
   PubMed Web of Science ®Google Scholar
• Arend W. P., Welgus H. G., Thompson R. C., Eisenberg S. P. Biological properties of recombinant human monocyte-derived interleukin-1 receptor antagonist. J. Clin. Invest. 1990; 85: 1694–1697
   PubMed Web of Science ®Google Scholar
• Granowitz E. V., Clark B. D., Vannier E., Callahan M. V., Dinarello C. A. Effect of interleukin-1 (IL-1) blockade on cytokine synthesis: I. IL-1 receptor antagonist inhibits IL-1-induced cytokine synthesis and blocks the binding of IL-1 to its type II receptor on human monocytes. Blood 1992; 79: 2356–2363
   PubMed Web of Science ®Google Scholar
• Estrov Z., Kurzrock R., Wetzler M., Kantarjian H., Blake M., Harris D., Gutterman J. U., Talpaz M. Suppression of chronic myelogenous leukemia colony growth by IL-1 receptor antagonist and soluble IL-1 receptors: a novel application for inhibitors of IL-1 activity. Blood 1991; 78: 1476–1484
   PubMed Web of Science ®Google Scholar
• Schirò R., Longoni D., Rossi V., Maglia O., Doni A., Arsura M., Carrara G., Masera G., Vannier E., Dinarello C. A., Rambaldi A., Biondi A. Supression of juvenile chronic myelogenous leukemia colony growth by interleukin-1 receptor antagonist. Blood 1993; 83: 460–465
   Google Scholar
• Rambaldi A., Torcia M., Bettoni S., Barbui T., Vannier E., Dinarello C. A., Cozzolino F. Modulation of cell proliferation and cytokine production in acute myeloblastic leukemia by interleukin-1 receptor antagonist and lack of its expression by leukemic cells. Blood 1991; 78: 3248–3253
   PubMed Web of Science ®Google Scholar
• Wetzler M., Kurrzock R., Estrov Z., Kantarjian H., Gisslinger H., Underbrink M. P., Talpaz M. Altered levels of interleukin-1β and interleukin-1 receptor antagonist in chronic myelogenous leukemia: clinical and prognostic correlates. Blood 1994; 84: 3142–3147
   PubMed Web of Science ®Google Scholar
• Holmberg L. A., Seidel K., Leisenring W., Torok-Storb B. Aplastic anemia analysis of stromal cell-function in long-term marrow cultures. Blood 1994; 84: 3685–3690
   PubMed Web of Science ®Google Scholar
• Barak V., Nisman B., Dann E. J., Kalickman I., Ruchlemer R., Bennett M. A., Pollack A. Serum interleukin-1β levels as a marker in hairy cell leukemia: correlation with disease status and sIL-2R levels. Leuk. Lymphom. 1994; 14: 33–39
   PubMed Web of Science ®Google Scholar
• Miller L. C., Lynch E. A., Isa S., Logan J. W., Dinarello C. A., Steere A. C. Balance of synovial fluid IL-1β and IL-1 receptor antagonist and recovery from Lyme arthritis. Lancet 1993; 341: 146–148
   PubMed Web of Science ®Google Scholar
• Firestein G. S., Boyle D. L., Yu C., Paine M. M., Whisenand T. D., Zvaifler N. J., Arend W. P. Synovial IL-1 receptor antagonist and interleukin-1 balance in rheumatoid arthritis. Arthrit. Rheumat. 1994; 37: 644–652
   PubMed Web of Science ®Google Scholar
• Roux-Lombard P., Modoux C., Vischer T., Grassi J., Dayer J.-M. Inhibitors of interleukin 1 activity in synovial fluids and in cultured synovial fluid mononuclear cells. J. Rheumatol. 1992; 19: 517–523
   PubMedGoogle Scholar
• Firestein G. S., Berger A. E., Tracey D. E., Chosay J. G., Chapman D. L., Paine M. M., Yu C., Zvaifler N. J. IL-1 receptor antagonist protein production and gene expression in rheumatoid arthritis and osteoarthritis synovium. J. Immunol. 1992; 149: 1054–1062
   PubMed Web of Science ®Google Scholar
• Kristensen M., Deleuran B., Eedy D. J., Feldmann M., Breathnach S. M., Brennan F. M. Distribution of interleukin-1 receptor antagonist protein (IRAP), interleukin-1 receptor, and interleukin-1 alpha in normal and psoriatic skin. Brit. J. Dermatol. 1992; 127: 305–311
   PubMedGoogle Scholar
• Corradi A., Franzi A. T., Rubartelli A. Interleukin-1α and interleukin-1 receptor antagonist in cultured keratinocytes: intra and extracellular localization, changes in IL-1ra/IL-1α ratio during differentiation. J. Invest. Derm. 1994, in press
   Google Scholar
• Janson R. W., King J. T.E., Hance K. R., Arend W. P. Enhanced production of IL-1 receptor antagonist by alveolar macrophages from patients with interstitial lung disease. Am. Rev. Resp. Dis. 1993; 148: 495–503
   PubMedGoogle Scholar
• Santos A. A., Scheltinga M. R., Lynch E., Brown E. F., Lawton P., Chambers E., Browning J., Dinarello C. A., Wolff S. M., Wilmore D. W. Elaboration of interleukin-1 receptor antagonist is not attenuated by glucocorticoids after endotoxemia. Arch. Surg. 1993; 128: 138–144
   PubMedGoogle Scholar
• Pereira B. J.G., Poutsiaka D. D., King A. J., Strom J. A., Narayan G., Levey A. S., Dinarello C. A. In vitro production of interleukin-1 receptor antagonist in chronic renal failure, continuous peritoneal disalysis and hemodialysis. Kidney Int. 1992; 42: 1419–1424
   PubMed Web of Science ®Google Scholar
• Chomarat P., Vannier E., Dechanet J., Rissoan M. C., Banchereau J., Dinarello C. A., Miossec P. The balance of IL-1 receptor antagonist/ IL-1β in rheumatoid synovium and its regulation by IL-4 and IL-10. J. Immunol. 1995; 154: 1432–1439
   PubMed Web of Science ®Google Scholar
• Thea D. M., Porat R., Nagimbi K., Baangi M. St., Louis M. E., Kaplan G., Dinarello C. A., Keusch G. T. Relationship of cytokine and cytokine antagonist plasma levels to disease progression in African women infected with HIV-1. Ann. Int. Med. 1996; 94–3738, in press revised MS#
   Google Scholar
• Chensue S. W., Bienkowski M., Eessalu T. E., Warmington K. S., Hershey S. D., Lukas N. W., Kunkel S. L. Endogenous IL-1 receptor antagonist protein (IRAP) regulates schistosome egg granuloma formation and the regional lymphoid response. J. Immunol. 1993; 151: 3654–3662
   PubMed Web of Science ®Google Scholar
• Ferretti M., Casini-Raggi V., Pizarro T. T., Eisenberg S. P., Nast C. C., Cominelli F. Neutralization of endogenous IL-1 receptor antagonist exacerbates and prolongs inflammation in rabbit immune colitis. J. Clin. Invest. 1994; 94: 449–453
   PubMed Web of Science ®Google Scholar
• LeMay L. G., Otterness I. G., Vander A. J., Kluger M. J. In vivo evidence that the rise in plasma IL-6 following injection of a fever-inducing dose of LPS is mediated by IL-1 beta. Cytokine 1990; 2: 199–204
   PubMedGoogle Scholar
• Dinarello C. A., Zhang X. X., Wen H. D., Wolff S. M., Ikejima T. The effect of interleukin-1 receptor antagonist on IL-1, LPS, Staphylococcus epidermidis and tumor necrosis factor fever. The effect of interleukin-1 receptor antagonist on IL-1, LPS, Staphylococcus epidermidis and tumor necrosis factor fever, T. Bartfai, D. Ottoson. Pergamon Press, Book Oxford 1992; 11–18
   Google Scholar
• Granowitz E. V., Porat R., Mier J. W., Orencole S. F., Callahan M. V., Cannon J. G., Lynch E. A., Ye K., Poutsiaka D. D., Vannier E., Shapiro L., Pribble J. P., Stiles D. M., Catalano M. A., Wolff S. M., Dinarello C. A. Hematological and immunomodulatory effects of an interleukin-1 receptor antagonist coinfusion during low-dose endotoxemia in healthy humans. Blood 1993; 82: 2985–2990
   PubMed Web of Science ®Google Scholar
• Markewitz A., Faist E., Lang S., Endres S., Fuchs B., Reichart B. Successful restoration of cell-mediated immune response after cardiopulmonary bypass by immunomodulation. J. Thoras. Card. Surg. 1993; 105: 15–24
   PubMed Web of Science ®Google Scholar
• Fisher C. J.J., Slotman G. J., Opal S. M., Pribble J., Bone R. C., Emmanuel G., Ng D., Bloedow D. C., Catalano M. A. Initial evaluation of human recombinant interleukin-1 receptor antagonist in the treatment of sepsis syndrome: a randomized, open-label, placebo-controlled multicenter trial. Crit. Care Med. 1994; 22: 12–21
   PubMed Web of Science ®Google Scholar
• Fischer E., Marano M. A., Barber A. E., Hudson A. A., Lee K., Rock C. S., Hawes A. S., Thompson R. C., Hayes T. V., Anderson T. D., Benjamin W. R., Lowry S. F., Moldawer L. L. A comparison between the effects of interleukin-1α administration and sublethal endotoxemia in primates. Am. J. Physiol. 1991; 261: R442–R449
   PubMed Web of Science ®Google Scholar
• Gershenwald J. E., Fong Y. M., Fahey T. J., Calvano S. E., Chizzonite R., Kilian P. L., Lowry S. F., Moldawer L. L. Interleukin 1 receptor blockade attenuates the host inflammatory response. Proc. Natl. Acad. Sci. USA 1990; 87: 4966–4970
   PubMed Web of Science ®Google Scholar
• Casey L. C., Balk R. A., Bone R. C. Plasma cytokines and endotoxin levels correlate with survival in patients with the sepsis syndrome. Ann. Intern. Med. 1993; 119: 771–778
   PubMed Web of Science ®Google Scholar
• Fisher C. J.J., Dhainaut J. F., Opal S. M., Pribble J. P., Balk R. A., Slotman G. J., Iberti T. J., Rackow E. C., Shapiro M. J., Greenman R. L. Recombinant human interleukin-1 receptor antagonist in the treatment of patients with sepsis syndrome. Results from a randomized, double blind, placebo-controlled trial. JAMA 1994; 271: 1836–1843
   PubMed Web of Science ®Google Scholar
• Knaus W. A., Harrell F. E., Fisher C. J., Wagner D. P., Opal S. M., Sadoff J. C., Draper E. A., Walawander C. A., Conboy K., Grasela T. H. The clinical evaluation of new drugs for sepsis. JAMA 1993; 270: 1233–1241
   PubMedGoogle Scholar
• Lebsack M. E., Paul C. C., Bloedow D. C., Burch F. X., Sack M. A., Chase W., Catalano M. A. Subcutaneous IL-1 receptor antagonist in patients with rheumatoid arthritis. Arthr. Rheumatol. 1991; 34(suppl)S67
   Google Scholar
• Lebsack M. E., Paul C. C., Martindale J. J., Catalano M. A. A dose- and regimen-ranging study of IL-1 receptor antagonist in patients with rheumatoid arthritis. Arthr. Rheumat. 1993; 36: S39.
   PubMed Web of Science ®Google Scholar
• Bresnihan B., Lookabaugh J., Witt K., Musikic P. Treatment with recombinant human interleukin-1 receptor antagonist in rheumatoid arthritis: results of a randomized, double-blind, placebo-controlled multicenter trial. Arthrit. Rheumat. 1996; 39: S73, abs
   PubMedGoogle Scholar
• Watt I., Cobby M. Recombinant human interleukin-1 receptor antagonist reduces the rate of joint erosion in rheumatoid arthritis. Arthrit. Rheumat. 1996; 39: S123.
   Google Scholar
• Antin J. H., Weinstein H. J., Guinan E. C., McCarthy P., Bierer B. E., Gilliland D. G., Parsons S. K., Ballen K. K., Rimm I. J., Falzarano G., Ferrara J. L. Recombinant human interleukin-1 receptor antagonist in the treatment of steroid-resistant graft-versus-host disease. Blood 1994; 84: 1342–1348
   PubMedGoogle Scholar
• McCarthy P. L., Abhyankar S., Neben S., Sieff C., Thompson R. C., Burakoff S., Ferrara J. L.M. Inhibition of interleukin-1 by interleukin-1 receptor antagonist prevents graft versus host disease. Blood 1991; 78: 1915–1918
   PubMed Web of Science ®Google Scholar