Structural and functional studies of the human selenium binding protein-1 and its involvement in hepatocellular carcinoma

Biochimica et Biophysica Acta - Proteins and Proteomics

Volumn 1814, Issue 4, 2011, Pages 513-522

  Raucci, Raffaele ^a   Colonna, Giovanni ^b   Guerriero, Eliana ^a   Capone, Francesca ^a   Accardo, Marina ^b   Castello, Giuseppe ^a   Costantini, Susan ^a  

^a NATIONAL CANCER INSTITUTE   (Italy)

^b SECOND UNIVERSITY OF NAPLES   (Italy)

Author keywords

Hepatocarcinoma; Hepatocarcinoma prognosis; Molecular dynamics; Selenium binding protein; Structural model

Indexed keywords

5,5' DITHIOBIS(2 NITROBENZOIC ACID); ANTINEOPLASTIC AGENT; CYSTEINE; SELENIUM; SELENIUM BINDING PROTEIN; SELENIUM BINDING PROTEIN 1; UNCLASSIFIED DRUG;

AGED; ARTICLE; CLINICAL ARTICLE; CONTROLLED STUDY; FEMALE; HUMAN; HUMAN TISSUE; IMMUNOHISTOCHEMISTRY; LIVER CELL CARCINOMA; MALE; MOLECULAR DYNAMICS; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN INTERACTION; PROTEIN PURIFICATION; PROTEIN STABILITY; PROTEIN STRUCTURE; STRUCTURE ACTIVITY RELATION;

AGED; AMINO ACID SEQUENCE; CARCINOMA, HEPATOCELLULAR; CIRCULAR DICHROISM; FEMALE; HUMANS; IMMUNOHISTOCHEMISTRY; LIVER NEOPLASMS; MALE; MIDDLE AGED; MOLECULAR DYNAMICS SIMULATION; MOLECULAR SEQUENCE DATA; SELENIUM-BINDING PROTEINS; SEQUENCE ALIGNMENT; SULFIDES; TITRIMETRY;

EID: 79952488092     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2011.02.006     Document Type: Article

References (51)

1. P.W. Chang, S.K. Tsui, C. Liew, C.C. Lee, M.M. Waye, K.P. Fung, Isolation, characterization, and chromosomal mapping of a novel cDNA clone encoding human selenium binding protein, J. Cell. Biochem. 64 (1997) 217-224. (Pubitemid 27065436)
2. M.P. Bansal, T. Mukhopadhyay, J. Scott, R.G. Cook, R. Mukhopadhyay, D. Medina, DNA sequencing of a mouse liver protein that binds selenium: implications for selenium's mechanism of action in cancer prevention, Carcinogenesis 11 (1990) 2071-2073. (Pubitemid 20375959)
3. M.J. Berry, G.W. Martin III, S.C. Low, RNA and protein requirements for eukaryotic selenoprotein synthesis, Biomed. Environ. Sci. 10 (1997) 182-189.
4. W. Self, R. Pierce, T. Stadtman, Cloning and heterologous expression of a Methanococcus vannielii gene encoding a selenium-binding protein, IUBMB Life 56 (2004) 501-507. (Pubitemid 39576899)
5. M. Haratake, K. Fujimoto, M. Ono, M. Nakayama, Selenium binding to human hemoglobin via selenotrisulfide, BBA 1723 (2005) 215-220. (Pubitemid 40744689)
6. M. Suzuki, D.-Y. Lee, N. Inyamah, T.C. Stadtman, N. Tjandra, Solution NMR structure of selenium-binding protein from Methanococcus vannielii, J. Biol. Chem. 283 (2008) 25936-25943.
7. G.M. Lacourciere, R.L. Levine, T.C. Stadtman, Direct detection of potential selenium delivery proteins by using an Escherichia coli strain unable to incorporate selenium from selenite into proteins, PNAS 99 (2002) 9150-9153. (Pubitemid 34764582)
8. Y. Ogasawara, G. Lacourciere, T.C. Stadtman, Formation of a selenium-substituted rhodanese by reaction with selenite and glutathione: possible role of a protein perselenide in a selenium delivery system, PNAS 98 (2001) 9494-9498. (Pubitemid 32769331)
9. J.Y. Jeong, Y. Wang, A.J. Sytkowski, Human selenium binding protein-1 (hSP56) interacts with VDU1 in a selenium-dependent manner, BBRC 379 (2009) 583-588.
10. F. Capone, S. Costantini, E. Guerriero, R. Calemma, M. Napolitano, S. Scala, F. Izzo, G. Castello, Serum cytokine levels in patients with hepatocellular carcinoma, Eur. Cytokine Netw. 21 (2010) 99-104.
11. G. Castello, S. Scala, G. Palmieri, S.A. Curley, F. Izzo, HCV-related hepatocellular carcinoma: from chronic inflammation to cancer, Clin. Immunol. 134 (2010) 237-250.
12. M. Fusco, E. Girardi, P. Piselli, R. Palombino, J. Polesel, C. Maione, P. Scognamiglio, F.A. Pisanti, M. Solmone, P. Di Cicco, G. Ippolito, S. Franceschi, D. Serraino, Epidemiology of viral hepatitis infections in an area of southern Italy with high incidence rates of liver cancer, Eur. J. Cancer 44 (2008) 847-853.
13. G. Chen, H. Wang, C.T. Miller, D.G. Thomas, T.G. Gharib, D.E. Misek, T.J. Giordano, M.B. Orringer, S.M. Hanash, D.G. Beer, Reduced selenium-binding protein 1 expression is associated with poor outcome in lung adenocarcinomas, J. Pathol. 202 (2004) 321-329. (Pubitemid 38325241)
14. M.E. Schaner, D.T. Ross, G. Ciaravino, T. Sorlie, O. Troyanskaya, M. Diehn, Y.C. Wang, G.E. Duran, T.L. Sikic, S. Caldeira, H. Skomedal, I.P. Tu, T. Hernandez- Boussard, S.W. Johnson, P.J. O'Dwyer, M.J. Fero, G.B. Kristensen, A.L. Borresen-Dale, T. Hastie, R. Tibshirani, M. van de Rijn, N.N. Teng, T.A. Longacre, D. Botstein, P.O. Brown, B.I. Sikic, Gene expression patterns in ovarian carcinomas, Mol. Biol. Cell 14 (2003) 4376-4386.
15. L.M. Brown, S.M. Helmke, S.W. Hunsucker, R.T. Netea-Maier, S.A. Chiang, D.E. Heinz, K.R. Shroyer, M.W. Duncan, B.R. Haugen, Quantitative and qualitative differences in protein expression between papillary thyroid carcinoma and normal thyroid tissue, Mol. Carcinog. 45 (2006) 613-626.
16. H. Kim, H.J. Kang, K.T. You, S.H. Kim, K.Y. Lee, T.I. Kim, C. Kim, S.Y. Song, H.J. Kim, C. Lee, Suppression of human selenium-binding protein 1 is a late event in colorectal carcinogenesis and is associated with poor survival, Proteomics 6 (2006) 3466-3476. (Pubitemid 43886162)
17. A.L. Silvers, L. Lin, A.J. Bass, G. Chen, Z. Wang, D.G. Thomas, J. Lin, T.J. Giordano, M.B. Orringer, D.G. Beer, A.C. Chang, Decreased selenium-binding protein 1 in esophageal adenocarcinoma results from posttranscriptional and epigenetic regulation and affects chemosensitivity, Clin. Cancer Res. 16 (7) (2010) 2009-2021.
18. P. Zhang, C. Zhang, X. Wang, F. Liu, C.J. Sung, M.R. Quddus, W.D. Lawrence, The expression of selenium-binding protein 1 is decreased in uterine leiomyoma, Diagn. Pathol. 5 (1) (2010) 80.
19. G. Corona, E. De Lorenzo, C. Elia, M.P. Simula, C. Avellini, U. Baccarani, F. Lupo, C. Tiribelli, A. Colombatti, G. Toffoli, Differential proteomic analysis of hepatocellular carcinoma, Int. J. Oncol. 36 (2010) 93-99.
20. L. Whitmore, B.A. Wallace, Protein secondary structure analyses from circular dichroism spectroscopy: methods and reference databases, Biopolymers 89 (2008) 392-400.
21. D.B. Wetlaufer, Ultraviolet spectra of proteins and amino acids, Adv. Protein Chem. 17 (1962) 303-390.
22. S.C. Gill, P.H. Von Hippel, Calculation of protein extinction coefficients from amino acid sequence data, Anal. Biochem. 182 (1989) 319-326.
23. M.M. Bradford, A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding, Anal. Biochem. 72 (1976) 248-254.
24. G.L. Ellman, Tissue sulfhydryl groups, Arch. Biochem. Biophys. 82 (1959) 70-77.
25. E. Gasteiger, C. Hoogland, A. Gattiker, S. Duvaud, M.R. Wilkins, R.D. Appel, A. Bairoch, Protein Identification and Analysis Tools on the ExPASy Server, in: John M. Walker (Ed.), The Proteomics Protocols Handbook, Humana Press, 2005, pp. 571-607.
26. J.A. Cuff, G.J. Barton, Application of enhanced multiple sequence alignment profiles to improve protein secondary structure prediction, Proteins 40 (2000) 502-511. (Pubitemid 30624459)
27. Z.R. Yang, R. Thomson, P. McMeil, R.M. Esnouf, RONN: the bio-basis function neural network technique applied to the dectection of natively disordered regions in proteins, Bioinformatics 21 (2005) 3369-3376. (Pubitemid 41222441)
28. S.F. Altschul, W. Gish, W. Miller, E. Myers, D.J. Lipman, Best local alignment search tool, J. Mol. Biol. 215 (1990) 403-410.
29. S. Costantini, F. Buonocore, A.M. Facchiano, Molecular modelling of co-receptor CD8αα Sparus aurata, Fish Shellfish Immunol. 25 (2008) 782-790.
30. A. Paladino, S. Costantini, G. Colonna, A.M. Facchiano, Molecular modelling of miraculin: structural analyses and functional hypotheses, BBRC 367 (2008) 26-32.
31. I. Autiero, S. Costantini, G. Colonna, Human sirt-1: molecular modeling and structure-function relationships of an unordered protein, PLoS ONE 4 (2009) e7350.
32. J.D. Thompson, D.G. Higgins, T. Gibson, CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice, Nucleic Acids Res. 22 (1994) 4673-4680.
33. A. Sali, T.L. Blundell, Comparative protein modelling by satisfaction of spatial restraints, J. Mol. Biol. 234 (1993) 779-815.
34. M.J. Sippl, Recognition of errors in three-dimensional structures of proteins, Proteins 17 (1993) 355-362. (Pubitemid 23358545)
35. R.A. Laskowski, M.W. MacArthur, D.S. Moss, J.M. Thornton, PROCHECK: a program to check the stereochemical quality of protein structures, J. Appl. Cryst. 26 (1993) 283-291.
36. Z. Xiang, C.S. Soto, B. Honig, Evaluating conformational free energies: the colony energy and its application to the problem of loop prediction, PNAS 99 (2002) 7432-7437. (Pubitemid 34568708)
37. W. Kabsch, C. Sander, Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features, Biopolymers 2 (1983) 2577-2637.
38. S. Ahmad, M.M. Gromiha, H. Fawareh, A. Sarai, ASAView: solvent accessibility graphics for proteins, BMC Bioinform. 5 (2004) 51.
39. D. Van Der Spoel, E. Lindahl, B. Hess, G. Groenhof, A.E. Mark, H.J. Berendsen, GROMACS: fast, flexible, and free, J. Comput. Chem. 26 (2005) 1701-1718.
40. A. Paladino, G. Colonna, A.M. Facchiano, S. Costantini, Functional hypothesis on miraculin' sweetness by a molecular dynamics approach, BBRC 396 (2010) 726-730.
41. A. Amadei, A.B. Linssen, H.J. Berendsen, Essential dynamics of proteins, Proteins 17 (4) (1993) 412-425. (Pubitemid 23358549)
42. A.K. Dunker, C.J. Brown, J.D. Lawson, L.M. Iakoucheva, Z. Obradovic, Intrinsic disorder and protein function, Biochemistry 41 (2002) 6573-6582. (Pubitemid 34547347)
43. S. Costantini, M. Costantini, G. Colonna, Frequencies of specific peptides in intrinsic disordered protein domains, Protein and Peptide Letters 2010 Jun 3.
44. S.M. Choi, C.Y. Ma, Structural characterization of globulin from common buckwheat (Fagopyrum esculentum Moench) using circular dichroism and Raman spectroscopy, Food Chem. 102 (2007) 150-160.
45. R.W. Woody, Contributions of tryptophan side chains to the far-ultraviolet circular dichroism of proteins, Eur. Biophys. J. 23 (1994) 253-262.
46. I.B. Grishina, R.W. Woody, Contributions of tryptophan side chains to the circular dichroism of globular proteins: exciton couplets and coupled oscillators, Faraday Discuss. (1994) 245-262.
47. P. Neumann, K. Markau, H. Sund, Studies of glutamate dehydrogenase. Regulation of glutamate dehydrogenase from Candida utilis by a pH and temperature-dependent conformational transition, Eur. J. Biochem. 65 (1976) 465-472.
48. A.L. Rucker, T.P. Creamer, Polyproline II helical structure in protein unfolded states: lysine peptides revisited, Protein Sci. 11 (2002) 980-985. (Pubitemid 34241306)
49. W.C. Johnson, I. Tinoco, Circular dichroism of polypeptide solutions in the vacuum ultraviolet, J. Am. Chem. Soc. 94 (1972) 4389-4397.
50. D. Behne, A. Kyriakopoulos, Mammalian selenium-containing proteins, Annu. Rev. Nutr. 21 (2001) 453-473. (Pubitemid 32695280)
51. Y. Ogasawara, G.M. Lacourciere, K. Ishii, T.C. Stadtman, Characterization of potential selenium-binding proteins in the selenophosphate synthetase system, Proc. Natl Acad. Sci. USA 102 (2005) 1012-1016. (Pubitemid 40170717)