Abstract
Soluble forms of usually membrane bound molecules were identified in blood or other body fluids. Among these soluble forms of membrane proteins, which have been found to lack the transmembrane and the intracellular domain, the soluble cytokine receptors are of interest, because they have been found to be capable of binding the ligand and of influencing the biological activity of the cytokines1,2.
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Rose-John, St. and Heirich, P.C. (1994) Soluble receptors for cytokines and growth factors: generation and biological function. Biochem. J., 300, 281–290
Fernandez-Botran, R. (1991) Soluble cytokine receptors: their role in immunoregulation. FASEB J. 5, 2567–2574
Femadez-Botran, R and Viletta, E.S. (1990) Proc. Natl. Sci. U.S.A. 87, 4202–4206
Goodwin, R.G., Friend, D., Ziegler, S.F., Jerzy, R., Falk, B.A., Gimple, S., Cosman, D., Dower. S.K., March, C.J., Namen, A.E. and Park, L.S. (1990) Cell 60„ 941–951
Müllberg, J., Schooltink, H., Stojan, T., Gunter, M., Graeve, L., Buse. G., Mackiewicz, A., Heinrich P.C. and Rose-John, St. (1993) The soluble IL-6- receptor is generated by shedding. Eut J. Immunol. 23, 473–480
Bazil, V. and Strominger, J.L. (1991) Shedding is a mechanism of down modulation of CD 14 on stimulated human monocytes.. J. Immunol. 147 /5, 1567–1574
Arribas, J., Coodly, L., Vollmer, P., Kishimoto, T.K., Rose-John, St. and Massague. J. (1996) Diverse cell surface protein ectodomains are shed by a system sensitive to metalloproteinase inhibitors. J. Biol. Chem. 271 /19, 11376–11382
Ching-Hon Pui (1989)Serum interleukin-2-receptor: clinical and biological implications. Leukemia, 3/5, 323–327
Van Zee, K.J., Kohno, T., Fischer, E., Rock, C.S., Moldawer, L.L. and Lowry, S.F. (1992) Tumor necrosis factor soluble receptors circulate during experimental and clinical imflammation and can protect against excessive tumor necrosis factor in vitro and in vivo. Proc. Natl. Acad. Sci. U.S.A. 89, 4845–4849
Frieling, J.T.M., Sauerwein, R.W., Wijdenes, J., Hendriks, T., and van der Linden, G.J. (1994) Soluble Interleukin 6 receptor in biological fluids from human origin. Cytokine 6, 376–381
I I. Fritz, S., Striggow, F., Reinhold D., Schluter, T., Schonfeld, P.. Ansorge. S. Bohnensack. R. (1996) Phorbol ester-induced shedding of intercellular adhesion molecule-1 (ICAM-I) on erythroleukemic K 562 cells. Biochim-Biophys-Acta. 1312 /3, 255–261
Galve-de-Rochemonteix, B., Ntcod, L.P., Dayer J.M. (1996) Tumor necrosis factor soluble receptor 75: the principal receptor form released by human alveolar macrophages and monocytes in the presence of interferon(gamma). Am. J. Respir. Cell. Mol. Biol. 14 /3, 279–87
Porteu, F., Brockhaus, M., Wallach, D., Engelmann, H. and Nathan, C.F. (1991) Human neutrophil elastase releases a ligand-binding fragment from the 75-kDa Tumor Necrosis Factor (TNF) receptor. J. Biol. Chem. 266/28,18846/-18853
Kayagaki, N., Kawasaki, A., Ebate, T., Ohmoto, H., Ikeda, S., Inoue, S., Yoshino, K., Okomura. K. and Yagita, H. (1995) Metalloproteinase-mediated release of human Fas-ligand J. Exp. Med. 182 1777–1783
Crowe, P., Walter, B.N., Mohler, K.M., Otten-Evans, C., Black, R.A., Ware, C.F. (1995) A metalloproteinase inhibitor blocks shedding of 80kD TNF receptor and TNF processing in t-lymphocytes. J. Exp. Med. 181. 1205–1210
Müllberg, J., Durie, F.H., Otten-Evans, C. Alderson, M.R., Rose,-John, St., Cosman, D., Black. R.A. and Mohler, K., M. (1995) A metalloproteinase inhibitor blocks the shedding of then 1L-6 receptor and the TNF receptor. J. Immunol. 155, 5198–5205
Campbell, E.J., Cury, J.D., Shapiro, S.D., Goldberg, G.I. and Welgus, H.G. (1991) Neutral proteinases of human mononuclear phagocytes, J. Immunol. 146, 1286–1293
Trabandt, A., Gay, R.E., Fassbender, H.-G. and Gay, S. (1991) Cathepsin B in synovial cells at the site of joint destruction in rheumatoid arthritis. Arthritis and Rheumatism 34, 1444–1451
Nadel, J.A. (1991) Role of mast cell and neutrophil proteases in airway secretion. Am. Rev. Respir. Dis. 144, 48–51
Olssen, I. and Venge, S. 1974) Cationic proteins of human granulocytes. 11. Separation of the cationic proteins of granules of leukemic myeloid cells. Blood 44, 235–246 (1974)
Travis, J (1978) Neutral proteinases of human polymorhonuclear leukocytes, Biochemistry, physiology and clinical significance. Eds. Havemann, K., Janoff, A. Urban & Schwartzenberg Baltimore 118–1128
Johnson, D and Travis. J. (1978) The oxidative inactivation of human a,-protemase inhibitor. Further evidence for methionine at the reactive center. J. Biol. Chem. 254, 4022–4026
Chidwick, K., Winyard. P.G., Zhang, Z., Farrell. A.D., Blake, D.R. (1991) Inactivation of the elastase inhibitory activity of ai-antìtrypsin in fresh samples of synovial fluid from patients with rheumatoid arthritis. Ann. Rheumat. Dis. 50, 915–916
Michaelis, J., Vissers, M.C.M. and Winterbourn, C.C. (1990) Human neutrophil collagenase cleaves a,-antitrypsin. Biochem. J. 270, 809–814
Janusz, M.J., Doherty, N.S.: Degradation of cartilage matrix proteoglycan by human neutrophils involves both elastase and cathepsin G. J. Immunol. 146, 3922–3928 (1991)
Eckle, I., Seitz, R., Egbring, R., Kolb, G. and Havemann, K. (1991) Protein C degradation in vitro by neutrophil elastase. Biol. Chem. Hoppe-Seyler 372, 1007–1013
Turkington, S.T. (1991) Degradation of human factor X by human polymorphonuclear leucocyte cathepsin G and elastase. Hämostasis 21, 111–116
Padrines, M. Wolf, M., Walz, A. and Baggiolini, M. (1994) Interleukin-8 processing by neutrophil diastase, cathepsin G and proteinase-3. FEBS Letters 352, 23I - 235
Hannah, S. and Ryle, A.S. (1991) Proteolysis of lung elasttn by human neutrophil elastase. Biochemical Society Transactions 19, 294
Eckle, I., Kolb. G. and Havemann. K. (1991) inhibition of neutrophil chernotaxis by elastase-generated IgG fragments. Scand. J. Immunol 34. 359–364
Kanayama, N., Terao, ‘F.. Inactivation of human tumor cell pro-urokinase by granulocyte elastase. Jpn. J. Cancer Res. 81. 994–1002 (1990)
Janotf, A (1985) Elastase to tissue injury. Ann. Rev. Med. 36, 207–216
Brown, D.M., Brown, G.M., Macnee, W. and Donaldson, K. (1992) Activated human peripheral blood neutrophils produce epithelial injury and fibronectin breakdown in vitro. Inflammation 16. 21–30
Jochum. M., Gippner-Steppert. C., Machleidt, W. and Fritz, H. (1994) The role of phagocyte protemases and proteinase inhibitors in multiple organ failure. Am. J. Cru. Care Med. 150. 5123–130
Johnstone, R.M. (1996) Cleavage of the transferrin receptor by human granulocytes: differential proteolysis of the exosome-bound TFR. J. Cell. Physiol. 168 /2, 333–345
Bjornberg, F., Lantz, M., Gullberg, U. (1995) Metalloproteases and serineproteases are involved in the cleavage of the two tumour necrosis factor (TNF) receptors to soluble forms in the myeloid cell Imes 0937 and THP-1. Scand-J-Immunol. 42 /4. 418–24
Nakajima, K., Power, J.C., Ashe. B.M. and Zimmermann, M. (1979) Mapping the extended substrate binding site of cathepsin G and human leukocyte elastase. J. Biol.Chem. 254. 4027–4032
Leonhard, W.J., Deppner. J.M., Crabtree, G.R., Rudikoff, S., Pumphrey, J.. Robb. R.J., Kronke. M.. Svetlik, P.B.. Pfeffer, N.J., Waldmann, T.A. (1994) Molecular cloning and expression of cDNA for the human interleukin-2 receptor. Nature 311, 626–631
Cosman, D. Cerreti, D.P., Larsen, A., Park, L., March, C., Dower, S., Gillis, S. and Urdal, D. (1984) Cloning, sequence and expression of the human interleukin-2 receptor. Nature 312, 768–771
Nikaido. T., Shimizu, A., Ishida, N., Sabe, H., Teshigwara, K., Maeda, M.. Uchiyama.. Yodoi, J., Honlo. (1984) Molecular cloning of cDNA encoding human interelukin-2 receptor. Nature 311, 631–135
Yamasaki, K., Taga, T., Hirata, Y, Yamata, H., Kawanishi, Y., Seed, B., Taniguchi, T., Hirano, T., Kishimoto, T. (1988) Cloning and expression of the human interleukin-6 (BSF-2/IFN-l32) receptor Science 241 825–828
Döring, G., Frank, F., Boucher, C., Herbert, Silvia, Fleischer, B. and Bellon, G. (1995) Cleavage of the lymphocyte surface antigens CD2, CD4, and CD8 by polymorphonuclear leukocyte elastase and cathepsin G in Patients with cystic fibrosis. J. Immunol. 154, 4842–4850
Ugnotz, R.A., Kelly, B., Davis, R.J. and Massague, J. (1986) Biologically active prccursorfor transforming growzh factor type alpha released by retroviral transformed cells. Proc. Natl. Acad. Sci. 83 /17 6307–6311
Hibi, M., Murakami, M., Saito, M., Hirano, T., Taga, T. and Kishimoto, T. (1990) Molecular cloning and expression of an IL-6 signal transducer, gp 130. Cell 63, 1149–1157
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Bank, U., Reinhold, D., Kunz, D., Ansorge, S. (1997). Selective Proteolytical Cleavage of the Ligand-Binding Chains of the IL-2-Receptor and IL-6-Receptor by Neutrophil-Derived Proteases. In: Ansorge, S., Langner, J. (eds) Cellular Peptidases in Immune Functions and Diseases. Advances in Experimental Medicine and Biology, vol 421. Springer, Boston, MA. https://doi.org/10.1007/978-1-4757-9613-1_30
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DOI: https://doi.org/10.1007/978-1-4757-9613-1_30
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