Abstract
Ligand affinity chromatography separation is based on unique interaction between the target analyte and a ligand, which is coupled covalently to a resin. It is a simple, rapid, selective, and efficient purification procedure of proteins providing tens of thousands fold purification in one step. The biological activity of the isolated proteins is retained in most cases thus function is revealed concomitantly with the isolation. Prior to the completion of the genome project this method facilitated rapid and reliable cloning of the corresponding gene. Upon completion of this project, a partial protein sequence is enough for retrieving its complete mRNA and hence its complete protein sequence. This method is indispensable for the isolation of both expected (e.g. receptors) but mainly unexpected, unpredicted and very much surprising binding proteins. No other approach would yield the latter. This chapter provides examples for both the expected target proteins, isolated from rich sources of human proteins, as well as the unexpected binding proteins, found by serendipity.
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References
Cuatrecasas, P., Wilchek, M., Anfinsen, C.B. (1968) Selective enzyme purification by affinity chromatography. Proc. Natl. Acad. Sci. USA 61: 636–643.
Uhlen, M. (2008) Affinity as a tool in life science. BioTechniques 44: 649–654.
Roque, A.C., Lowe, C.R. (2008) Affinity chromatography: history, perspectives, limitations and prospects. Methods Mol. Biol. 421: 1–21.
Tartaglia, L.A., Goeddel, D.V. (1992) Two TNF receptors. Immunol. Today 13: 151–153.
Chizzonite, R., Truitt, T., Kilian, P.L., Stern, A.S., Nunes, P., Parker, K.P., Kaffka, K.L., Chua, A.O., Lugg, D.K., Gubler, U. (1989) Two high-affinity interleukin 1 receptors represent separate gene products. Proc. Natl. Acad. Sci. USA 86: 8029–8033.
Novick, D., Cohen, B., Rubinstein, M. (1994) The human interferon alpha/beta receptor: characterization and molecular cloning. Cell 77: 391–400.
Domanski, P., Witte, M., Kellum, M., Rubinstein, M., Hackett, R., Pitha, P., Colamonici, O.R. (1995) Cloning and expression of a long form of the beta subunit of the interferon alpha beta receptor that is required for signaling. J. Biol. Chem. 270: 21606–21611.
Marcon, L., Fritz, M.E., Kurman, C.C., Jensen, J.C., Nelson, D.L. (1988) Soluble Tac peptide is present in the urine of normal individuals and at elevated levels in patients with adult T cell leukaemia (ATL). Clin. Exp. Immunol. 73: 29–33.
Levine, S.J. (2008) Molecular mechanisms of soluble cytokine receptor generation. J. Biol. Chem. 283: 14177–14181.
Novick, D., Engelmann, H., Wallach, D., Rubinstein, M. (1989) Soluble cytokine receptors are present in normal human urine. J. Exp. Med. 170: 1409–1414.
Engelmann, H., Novick, D., Wallach, D. (1990) Two tumor necrosis factor-binding proteins purified from human urine. Evidence for immunological cross-reactivity with cell surface tumor necrosis factor receptors. J. Biol. Chem. 265: 1531–1536.
Abeck, D., Korting, H.C., Zaba, R., Dangor, Y., Fehler, G., Ballard, R.C. (1990) Soluble interleukin-2 receptors in serum and urine of patients with chancroid and their response to therapy. Int. J. STD AIDS 1: 282–284.
Christie, G., Dacey, I., Weston, B.J. (1995) Identification of a soluble, high affinity human interleukin 4 binding protein in normal human urine. Cytokine 7: 305–310.
Fanslow, W.C., Clifford, K., VandenBos, T., Teel, A., Armitage, R.J., Beckmann, M.P. (1990) A soluble form of the interleukin 4 receptor in biological fluids. Cytokine 2: 398–401.
Zhang, J.G., Hilton, D.J., Willson, T.A., McFarlane, C., Roberts, B.A., Moritz, R.L., Simpson, R.J., Alexander, W.S., Metcalf, D., Nicola, N.A. (1997) Identification, purification, and characterization of a soluble interleukin (IL)-13-binding protein. Evidence that it is distinct from the cloned IL-13 receptor and IL-4 receptor alpha-chains. J. Biol. Chem. 272: 9474–9480.
Veenbergen, S., Smeets, R.L., Bennink, M.B., Arntz, O.J., Joosten, L.A., van den Berg, W.B., van de Loo, F.A. (2010) The natural soluble form of IL-18 receptor {beta} exacerbates collagen-induced arthritis via modulation of T cell immune responses. Ann. Rheum. Dis. 69: 276–283.
Xu, W., Presnell, S.R., Parrish-Novak, J., Kindsvogel, W., Jaspers, S., Chen, Z., Dillon, S.R., Gao, Z., Gilbert, T., Madden, K., Schlutsmeyer, S., Yao, L., Whitmore, T.E., Chandrasekher, Y., Grant, F.J., Maurer, M., Jelinek, L., Storey, H., Brender, T., Hammond, A., Topouzis, S., Clegg, C.H., Foster, D.C. (2001) A soluble class II cytokine receptor, IL-22RA2, is a naturally occurring IL-22 antagonist, Proc. Natl. Acad. Sci. U. S. A. 98: 9511–9516.
Hayakawa, H., Hayakawa, M., Kume, A., Tominaga, S. (2007) Soluble ST2 blocks interleukin-33 signaling in allergic airway inflammation. J. Biol. Chem. 282: 26369–26380.
Meissner, U., Blum, H., Schnare, M., Rollinghoff, M., Gessner, A. (2001) A soluble form of the murine common gamma chain is present at high concentrations in vivo and suppresses cytokine signaling. Blood 97: 183–191.
Yasuda, H., Shima, N., Nakagawa, N., Mochizuki, S.I., Yano, K., Fujise, N., Sato, Y., Goto, M., Yamaguchi, K., Kuriyama, M., Kanno, T., Murakami, A., Tsuda, E., Morinaga, T., Higashio, K. (1998) Identity of osteoclastogenesis inhibitory factor (OCIF) and osteoprotegerin (OPG): a mechanism by which OPG/OCIF inhibits osteoclastogenesis in vitro. Endocrinology 139: 1329–1337.
Elson, G.C., Graber, P., Losberger, C., Herren, S., Gretener, D., Menoud, L.N., Wells, T.N., Kosco-Vilbois, M.H., Gauchat, J.F. (1998) Cytokine-like factor-1, a novel soluble protein, shares homology with members of the cytokine type I receptor family. J. Immunol. 161: 1371–1379.
Novick, D., Kim, S.H., Fantuzzi, G., Reznikov, L.L., Dinarello, C.A., Rubinstein, M. (1999) Interleukin-18 binding protein: a novel modulator of the Th1 cytokine response. Immunity 10: 127–136.
Novick, D., Rubinstein, M., Azam, T., Rabinkov, A., Dinarello, C.A., Kim, S.H. (2006) Proteinase 3 is an IL-32 binding protein. Proc. Natl. Acad. Sci. USA 103: 3316–3321.
Kim, S.H., Han, S.Y., Azam, T., Yoon, D.Y., Dinarello, C.A. (2005) Interleukin-32: a cytokine and inducer of TNFalpha. Immunity 22: 131–142.
Frosch, M., Foell, D. (2004) Wegener granulomatosis in childhood and adolescence. Eur. J. Pediatr. 163: 425–434.
Fischer, D.G., Tal, N., Novick, D., Barak, S., Rubinstein, M. (1993) An antiviral soluble form of the LDL receptor induced by interferon. Science 262: 250–253.
Engelmann, H., Aderka, D., Rubinstein, M., Rotman, D., Wallach, D. (1989) A tumor necrosis factor-binding protein purified to homogeneity from human urine protects cells from tumor necrosis factor toxicity. J. Biol. Chem. 264: 11974–11980.
Hock, R.A., Hollenberg, M.D. (1980) Characterization of the receptor for epidermal growth factor-urogastrone in human placenta membranes. J. Biol. Chem. 255: 10731–10736.
Rubinstein, M. (1979) Preparative high perofmance liquid chromatography of proteins. Anal. Biochem. 97: 1–7.
Marshall, T., Williams, K.M. (1984) Artifacts associated with 2-mercaptoethanol upon high resolution two-dimensional electrophoresis. Anal. Biochem. 139: 502–505.
Oakley, B.R., Kirsch, D.R., Morris, N.R. (1980) A simplified ultrasensitive silver stain for detecting proteins in polyacrylamide gels. Anal. Biochem. 105: 361–363.
Hunter, W. M. (1978) Radioimmunoassay. The Hanbook of Experimental Immunology (D. M. Weir, Ed.), Blackwell Press, Oxford, 14.11-14.30.
Bolton, A.E., Hunter, W.M. (1973) The labelling of proteins to high specific radioactivities by conjugation to a 125I-containing acylating agent. Biochem. J. 133: 529–539.
Novick, D., Cohen, B., Rubinstein, M. (1992) Soluble interferon-alpha receptor molecules are present in body fluids. FEBS Lett. 314: 445–448.
Mosley, B., Beckmann, M.P., March, C.J., Idzerda, R.L., Gimpel, S.D., VandenBos, T., Friend, D., Alpert, A., Anderson, D., Jackson, J., Wignall, J.M., Smith, C., Gallis, B., Sims, J.E., Urdal, D., Widmer, M.B., Cosman, D., Park, L.S. (1989) The murine interleukin-4 receptor: molecular cloning and characterization of secreted and membrane bound forms. Cell 59: 335–348.
Aderka, D., Engelmann, H., Maor, Y., Brakebusch, C., Wallach, D. (1992) Stabilization of the bioactivity of tumor necrosis factor by its soluble receptors. J. Exp. Med. 175: 323–329.
Narazaki, M., Yasukawa, K., Saito, T., Ohsugi, Y., Fukui, H., Koishihara, Y., Yancopoulos, G.D., Taga, T., Kishimoto, T. (1993) Soluble forms of the interleukin-6 signal-transducing receptor component gp130 in human serum possessing a potential to inhibit signals through membrane-anchored gp130. Blood 82: 1120–1126.
Kim, S.H., Eisenstein, M., Reznikov, L., Fantuzzi, G., Novick, D., Rubinstein, M., Dinarello, C.A. (2000) Structural requirements of six naturally occurring isoforms of the IL-18 binding protein to inhibit IL-18. Proc. Natl. Acad. Sci. USA 97: 1190–1195.
Xiang, Y., Moss, B. (1999) Identification of human and mouse homologs of the MC51L-53L-54L family of secreted glycoproteins encoded by the Molluscum contagiosum poxvirus. Virology 257: 297–302.
Alcami, A. (2003) Viral mimicry of cytokines, chemokines and their receptors. Nat. Rev. Immunol. 3: 36–50.
Cohen, B., Novick, D., Barak, S., Rubinstein, M. (1995) Ligand-induced association of the type I interferon receptor components. Mol. Cell. Biol. 15: 4208–4214.
Novick, D., Rubinstein, M. (2007) The tale of soluble receptors and binding proteins: from bench to bedside. Cytokine Growth Factor Rev. 18: 525–533.
Chen, C.H. (2008) Review of a current role of mass spectrometry for proteome research. Anal. Chim. Acta 624: 16–36.
Sparbier, K., Wenzel, T., Dihazi, H., Blaschke, S., Müller, G.A., Deelder, A., Flad, T., Kostrzewa, M. (2009) Immuno-MALDI-TOF MS: New perspectives for clinical applications of mass spectrometry. Proteomics 9: 1442–1450.
Conrotto P, Souchelnytskyi S. (2008) Proteomic approaches in biological and medical sciences: principles and applications. Exp. Oncol. 30: 171–80.
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Novick, D., Rubinstein, M. (2012). Ligand Affinity Chromatography, an Indispensable Method for the Purification of Soluble Cytokine Receptors and Binding Proteins. In: De Ley, M. (eds) Cytokine Protocols. Methods in Molecular Biology, vol 820. Humana Press, Totowa, NJ. https://doi.org/10.1007/978-1-61779-439-1_12
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DOI: https://doi.org/10.1007/978-1-61779-439-1_12
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