Probing the copper(II) binding features of angiogenin. Similarities and differences between a N-terminus peptide fragment and the recombinant human protein
Probing the copper(II) binding features of angiogenin. Similarities and differences between a N-terminus peptide fragment and the recombinant human protein(403 views) La Mendola D, Farkas D, Bellia F, Magri A, Travaglia A, Hansson O, Rizzarelli E
Keywords: Angiogenin, Copper, Pancreatic Ribonuclease, Peptide Fragment, Recombinant Protein, Amino Acid Sequence, Article, Chemistry, Circular Dichroism, Electron Spin Resonance, Human, Metabolism, Potentiometry, Protein Binding, Protein Conformation, Ultraviolet Spectrophotometry, Electron Spin Resonance Spectroscopy,
Affiliations: *** IBB - CNR ***
Istituto di Biostrutture e Bioimmagini-CNR-Catania, Viale A. Doria 6, 95125 Catania, Italy.
Department of Chemistry, University of Gothenburg, PO Box 462, SE-40530 Gothenburg, Sweden
Dipartimento di Scienze Chimiche, Università di Catania, Viale A. Doria 6, 95125 Catania, Italy
Kurachi, K., Davie, E.W., Strydom, D.J., Vallee, B.L., (1985) Biochemistry, 24, pp. 5494-5499
Soncin, F., Shapiro, R., Fett, J.W., (1994) J. Biol. Chem., 269, pp. 8999-9005
Kishimoto, K., Liu, S., Tsuji, T., Olson, A.K., Hu, G.F., (2005) Oncogene, 24, pp. 445-456
Folkman, J., D'Amore, P.A., (1996) Cell, 87, pp. 1153-1155
Tello-Montoliu, A., Patel, J.V., Lip, G.Y., (2006) J. Thromb. Haemost., 4, pp. 1864-1874
Vallee, B.L., Riordan, J.F., (1997) Cell. Mol. Life Sci., 53, pp. 803-815
Strydom, D.J., (1998) Cell. Mol. Life Sci., 54, pp. 811-824
Badet, J., Soncin, F., Guitton, J.D., Lamare, O., Cartwright, T., Barritault, D., (1989) Proc. Natl. Acad. Sci. U. S. A., 86, pp. 8427-8431
Kaplan, J.H., Lutsenko, S., (2009) J. Biol. Chem., 284, pp. 25461-25465
Lowndes, S.A., Harris, A.L., (2005) J. Mammary Gland Biol. Neoplasms, 10, pp. 299-310
Goodman, V.L., Brewer, G.J., Merajver, S.D., (2005) Curr. Cancer Drug Targets, 5, pp. 543-549
Finney, L., Mandava, S., Ursos, L., Zhang, W., Rodi, D., Vogt, S., Legnini, D., Glesne, D., (2007) Proc. Natl. Acad. Sci. U. S. A., 104, pp. 2247-2252
Hu, G.F., (1998) J. Cell. Biochem., 69, pp. 326-335
La Mendola, D., Magrì, A., Vagliasindi, L.I., Hansson, Ö., Bonomo, R.P., Rizzarelli, E., (2010) Dalton Trans., pp. 10678-10684
Acharya, K.R., Shapiro, R., Allen, S.C., Riordan, J.F., Vallee, B.L., (1994) Proc. Natl. Acad. Sci. U. S. A., 91, pp. 2915-2919
Papageorgiou, A.C., Shapiro, R., Acharya, K.R., (1997) EMBO J., 16, pp. 5162-5177
Lequin, O., Thuering, H., Robin, M., Lallemand, J.Y., (1997) Eur. J. Biochem., 250, pp. 712-726
La Mendola, D., Bonomo, R.P., Caminati, S., Di Natale, G., Emmi, S.S., Hansson, Ö., MacCarrone, G., Rizzarelli, E., (2009) J. Inorg. Biochem., 103, pp. 195-204
Holloway, D.E., Hares, M.C., Shapiro, R., Subramanian, V., Acharya, K.R., (2001) Protein Expr. Purif., 22, pp. 307-317
Shapiro, R., Weremowicz, S., Riordan, J.F., Vallee, B.L., (1987) Proc. Natl. Acad. Sci. U. S. A., 84, pp. 8783-8787
Bonomo, R.P., Bruno, V., Conte, E., De Guidi, G., La Mendola, D., MacCarrone, G., Nicoletti, F., Vecchio, G., (2003) Dalton Trans., pp. 4406-4415
Gans, P., Sabatini, A., Vacca, A., (1996) Talanta, 43, pp. 1739-1753
Alderighi, L., Gans, P., Ienco, A., Peters, D., Sabatini, A., Vacca, A., (1999) Coord. Chem. Rev., 184, pp. 311-318
Stoll, S., Schweiger, A., (2006) J. Magn. Reson., 178, pp. 42-55
Kallay, C., Varnagy, K., Micera, G., Sanna, D., Sovago, I., (2005) J. Inorg. Biochem., 99, pp. 1514-1525
Kowalik- Jankowska, T., Jankowska, E., Kasrzykowski, F., (2010) Inorg. Chem., 49, pp. 2182-2192
Kulon, K., Valensin, D., Kamysz, W., Valensin, G., Nadolski, P., Porciatti, E., Gaggelli, E., Kozlowski, H., (2008) J. Inorg. Biochem., 102, pp. 960-972
Sanna, D., Micera, G., Kallay, C., Rigo, V., Sovago, I., (2004) Dalton Trans., pp. 2702-2707
Di Natale, G., Grasso, G., Impellizzeri, G., La Mendola, D., Micera, G., Mihala, N., Nagy, Z., Sovago, I., (2005) Inorg. Chem., 44, pp. 7214-7225
Pietropaolo, A., Muccioli, L., Zannoni, C., La Mendola, D., MacCarrone, G., Pappalardo, G., Rizzarelli, E., (2008) J. Phys. Chem. B, 112, pp. 5182-5188
Perczel, A., Hollosi, M., (1996) Circular Dichroism and the Conformational Analysis of Biomolecules, pp. 285-380. , Fasman, G. D. Plenum Press: New York
Krittinai, C., Johnson, W.C., (1997) Anal. Biochem., 253, pp. 57-64
Chakrabartty, A., Kortemme, T., Padmanabhan, S., Baldwin, R.L., (1993) Biochemistry, 32, pp. 5560-5565
Orfei, M., Alcaro, M.C., Chelli, G.M.M., Gianneschi, M., Kozlowki, H., Brasun, J., Messori, L., (2003) J. Inorg. Biochem., 97, pp. 299-307
Boka, B., Myari, A., Sovago, I., Hadjliadis, N., (2004) J. Inorg. Biochem., 98, pp. 113-122
Karavelas, T., Malandrinos, G., Hadjiliadis, N., Mlynarz, P., Kozlowski, H., Barsan, M., Butler, I., (2008) Dalton Trans., pp. 1215-1223
Kowalik-Jankowska, T., Ruta-Dolejsz, M., Wisniewska, K., Lankiewicz, L., Kozlowski, H., (2000) J. Chem. Soc., Dalton Trans., pp. 4511-4519
Zoroddu, M.A., Kowalik-Jankowska, T., Medici, S., Peana, M., Kozlowski, H., (2008) Dalton Trans., pp. 6127-6134
Varnagy, K., Boka, B., Sovago, I., Sanna, D., Marras, P., Micera, G., (1998) Inorg. Chim. Acta, 275-276, pp. 440-446
Rivillas-Acevedo, L., Grande-Aztatzi, R., Lomelì, I., Garcia, J.E., Barrios, E., Teloxa, S., Vela, A., Quintanar, L., (2011) Inorg. Chem., 50, pp. 1956-1972
Mylonas, M., Plakatouras, J.C., Hadjiliadis, N., Krezel, A., Bal, W., (2002) Inorg. Chim. Acta, 339, pp. 60-70
Travaglia, A., Arena, G., Fattorusso, R., Isernia, C., La Mendola, D., Malgieri, G., Nicoletti, V.G., Rizzarelli, E., (2011) Chem.-Eur. J., 17, pp. 3726-3738
Casolaro, M., Chelli, M., Ginanneschi, M., Laschi, F., Messori, L., Muniz-Mirand, M., Papini, A.M., Kozlowski, H., (2002) J. Inorg. Biochem., 89, pp. 181-190
Jancso, A., Paksi, Z., Jakab, N., Gyurcsik, B., Rockenbauer, A., Gajda, T., (2005) Dalton Trans., pp. 3187-3194
Sokolowska, M., Bal, W., (2005) J. Inorg. Biochem., 99, pp. 1653-1660
Millhauser, G.L., (2007) Annu. Rev. Phys. Chem., 58, pp. 299-320
Fett, J. W., Strydom, D. J., Lobb, R. R., Alderman, E. M., Bethune, J. L., Riordan, J. F., Vallee, B. L., (1985) Biochemistry, 24, pp. 5480-548
Strydom, D. J., Fett, J. W., Lobb, R. R., Alderman, E. M., Bethune, J. L., Riordan, J. F., Vallee, B. L., (1985) Biochemistry, 24, pp. 5486-5494
Vallee, B. L., Riordan, J. F., (1997) Cell. Mol. Life Sci., 53, pp. 803-815
Strydom, D. J., (1998) Cell. Mol. Life Sci., 54, pp. 811-824
Kaplan, J. H., Lutsenko, S., (2009) J. Biol. Chem., 284, pp. 25461-25465
Lowndes, S. A., Harris, A. L., (2005) J. Mammary Gland Biol. Neoplasms, 10, pp. 299-310
Goodman, V. L., Brewer, G. J., Merajver, S. D., (2005) Curr. Cancer Drug Targets, 5, pp. 543-549
Hu, G. F., (1998) J. Cell. Biochem., 69, pp. 326-335
Acharya, K. R., Shapiro, R., Allen, S. C., Riordan, J. F., Vallee, B. L., (1994) Proc. Natl. Acad. Sci. U. S. A., 91, pp. 2915-2919
Papageorgiou, A. C., Shapiro, R., Acharya, K. R., (1997) EMBO J., 16, pp. 5162-5177
Holloway, D. E., Hares, M. C., Shapiro, R., Subramanian, V., Acharya, K. R., (2001) Protein Expr. Purif., 22, pp. 307-317
Jang, S. H., Kang, D. K., Chang, S. I., Scheraga, H. A., Shin, H. C., (2004) Biotechnol. Lett., 26, pp. 1501-1504
Bonomo, R. P., Bruno, V., Conte, E., De Guidi, G., La Mendola, D., MacCarrone, G., Nicoletti, F., Vecchio, G., (2003) Dalton Trans., pp. 4406-4415
Zoroddu, M. A., Kowalik-Jankowska, T., Medici, S., Peana, M., Kozlowski, H., (2008) Dalton Trans., pp. 6127-6134
Lee, F. S., Vallee, B. L., (1989) Biochem. Biophys. Res. Commun., 161, pp. 121-126
Millhauser, G. L., (2007) Annu. Rev. Phys. Chem., 58, pp. 299-320
Probing the copper(II) binding features of angiogenin. Similarities and differences between a N-terminus peptide fragment and the recombinant human protein
The angiogenin protein (hAng) is a potent angiogenic factor and its cellular activities may be affected by copper ions even if it is yet unknown how this metal ion is able to produce this effect. Among the different regions of hAng potentially able to bind copper ions, the N-terminal domain appears to be an ideal candidate. Copper(II) complexes of the peptide fragments encompassing the amino acid residues 4-17 of hAng protein were characterized by potentiometric, UV-vis, CD, and EPR spectroscopic methods. The results show that these fragments have an unusual copper(II) binding ability. At physiological pH, the prevailing complex species formed by the peptide encompassing the protein sequence 4-17 is [CuHL], in which the metal ion is bound to two imidazole and two deprotonated amide nitrogen atoms disposed in a planar equatorial arrangement. Preliminary spectroscopic (UV-vis, CD, and EPR) data obtained on the copper(II) complexes formed by the whole recombinant hAng protein, show a great similarity with those obtained for the N-terminal peptide fragments. These findings indicate that within the N-terminal domain there is one of the preferred copper(II) ions anchoring site of the whole recombinant hAng protein.
Probing the copper(II) binding features of angiogenin. Similarities and differences between a N-terminus peptide fragment and the recombinant human protein
Probing the copper(II) binding features of angiogenin. Similarities and differences between a N-terminus peptide fragment and the recombinant human protein
Kállay C, Dávid A, Timári S, Nagy EM, Sanna D, Garribba E, Micera G, De Bona P, Pappalardo G, Rizzarelli E, Sóvágó I * Copper(II) complexes of rat amylin fragments(357 views) Dalton T (ISSN: 1477-9234, 1477-9226, 1477-9234electronic), 2011 Oct 14; 40(38): 9711-9721. Impact Factor:3.838 ViewExport to BibTeXExport to EndNote
Aloj L, Aurilio M, Rinaldi V, D'Ambrosio L, Tesauro D, Peitl PK, Maina T, Mansi R, Von Guggenberg E, Joosten L, Sosabowski JK, Breeman WA, De Blois E, Koelewijn S, Melis M, Waser B, Beetschen K, Reubi JC, De Jong M * The EEE project(449 views) Proc Int Cosm Ray Conf Icrc Universidad Nacional Autonoma De Mexico, 2007; 5(HEPART2): 977-980. Impact Factor:0 ViewExport to BibTeXExport to EndNote