Inhibition of Light Chain 6aJL2-R24G Amyloid Fiber Formation Associated with Light Chain Amyloidosis

Biochemistry

Volumn 54, Issue 32, 2015, Pages 4978-4986

  Pelaez Aguilar, Angel E ^a   Rivillas Acevedo, Lina ^a   French Pacheco, Leidys ^a   Valdes Garcia, Gilberto ^a   Maya Martinez, Roberto ^a   Pastor, Nina ^a   Amero, Carlos ^a  

^a UNIVERSIDAD AUTÓNOMA DEL ESTADO DE MORELOS   (Mexico)

Author keywords

[No Author keywords available]

Indexed keywords

CHAINS; DISEASES; GLYCOPROTEINS; HIGH RESOLUTION TRANSMISSION ELECTRON MICROSCOPY; LIGHT SCATTERING; MAGNETIC RESONANCE SPECTROSCOPY; MONOCLONAL ANTIBODIES; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; TRANSMISSION ELECTRON MICROSCOPY;

AMYLOID FIBERS; AMYLOID FIBRIL; AROMATIC RESIDUES; FIBRILLOGENESIS; IMMUNOGLOBULIN LIGHT CHAINS; ISOTHERMAL TITRATION CALORIMETRY; SMALL MOLECULES; THIOFLAVIN T;

PROTEINS;

AMYLOID; EPIGALLOCATECHIN GALLATE; MELATONIN; QUERCETIN; RIFAMPICIN; TETRACYCLINE; THIOFLAVINE; CATECHIN; IMMUNOGLOBULIN LIGHT CHAIN; PROTEIN BINDING; RECOMBINANT PROTEIN;

AMYLOIDOSIS; ARTICLE; FLUORESCENCE MICROSCOPY; ISOTHERMAL TITRATION CALORIMETRY; LIGHT SCATTERING; MOLECULAR DOCKING; NITROGEN NUCLEAR MAGNETIC RESONANCE; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN STABILITY; PROTON NUCLEAR MAGNETIC RESONANCE; SEQUENCE ALIGNMENT; STOICHIOMETRY; THERMOSTABILITY; TRANSMISSION ELECTRON MICROSCOPY; AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ANALOGS AND DERIVATIVES; ANTAGONISTS AND INHIBITORS; BIOSYNTHESIS; CHEMICAL STRUCTURE; DRUG EFFECTS; GENETICS; HUMAN; IN VITRO STUDY; METABOLISM; MISSENSE MUTATION; MOLECULAR GENETICS; NUCLEAR MAGNETIC RESONANCE; PROTEIN MULTIMERIZATION;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; AMYLOID; AMYLOIDOSIS; CATECHIN; HUMANS; IMMUNOGLOBULIN LIGHT CHAINS; IN VITRO TECHNIQUES; MELATONIN; MICROSCOPY, ELECTRON, TRANSMISSION; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTATION, MISSENSE; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN BINDING; PROTEIN MULTIMERIZATION; QUERCETIN; RECOMBINANT PROTEINS; RIFAMPIN; TETRACYCLINE;

EID: 84939603381     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/acs.biochem.5b00288     Document Type: Article

References (54)

1. Dispenzieri, A., Gertz, M. a, and Buadi, F. (2012) What do I need to know about immunoglobulin light chain (AL) amyloidosis? Blood Rev. 26, 137-154 10.1016/j.blre.2012.03.001
2. Ramirez-Alvarado, M. (2013) Amyloid formation in light chain amyloidosis Curr. Top. Med. Chem. 12, 2523-2533
3. Comenzo, R. L., Wally, J., Kica, G., Murray, J., Ericsson, T., Skinner, M., and Zhang, Y. (1999) Clonal immunoglobulin light chain variable region germline gene use in AL amyloidosis: Association with dominant amyloid-related organ involvement and survival after stem cell transplantation Br. J. Haematol. 106, 744-751 10.1046/j.1365-2141.1999.01591.x
4. Wall, J. S., Gupta, V., Wilkerson, M., Schell, M., Loris, R., Adams, P., Solomon, A., Stevens, F., and Dealwis, C. (2004) Structural basis of light chain amyloidogenicity: comparison of the thermodynamic properties, fibrillogenic potential and tertiary structural features of four Vlambda6 proteins J. Mol. Recognit. 17, 323-331 10.1002/jmr.681
5. Blancas-Mejía, L. M. and Ramirez-Alvarado, M. (2013) Systemic amyloidoses Annu. Rev. Biochem. 82, 745-774 10.1146/annurev-biochem-072611-130030
6. Perfetti, V., Palladini, G., Casarini, S., Navazza, V., Rognoni, P., Obici, L., Invernizzi, R., Perlini, S., Klersy, C., Merlini, G., and Dc, W. (2012) The repertoire of λ light chains causing predominant amyloid heart involvement and identification of a preferentially involved germline gene, IGLV1-44 Blood 119, 144-150 10.1182/blood-2011-05-355784
7. Obici, L., Perfetti, V., Palladini, G., Moratti, R., and Merlini, G. (2005) Clinical aspects of systemic amyloid diseases Biochim. Biophys. Acta, Proteins Proteomics 1753, 11-22 10.1016/j.bbapap.2005.08.014
8. Maya-Martinez, R., Gil-Rodriguez, P., and Amero, C. (2015) Solution structure of 6aJL2 and 6aJL2-R24G amyloidogenics light chain proteins Biochem. Biophys. Res. Commun. 456, 695-699 10.1016/j.bbrc.2014.12.044
9. Del Pozo-Yauner, L., Ortiz, E., Sánchez, R., Sánchez-López, R., Güereca, L., Murphy, C. L., Allen, A., Wall, J. S., Fernández-Velasco, D. A., Solomon, A., Becerril-Luján, B., Del Pozo Yauner, L., Ortiz, E., Sánchez, R., Sánchez-López, R., Güereca, L., Murphy, C. L., Allen, A., Wall, J. S., Fernández-Velasco, D. A., Solomon, A., and Becerril, B. (2008) Influence of the germline sequence on the thermodynamic stability and fibrillogenicity of human lambda 6 light chains Proteins: Struct., Funct., Genet. 72, 684-692 10.1002/prot.21934
10. Kyle, R., Linos, A., and Beard, C. (1992) Incidence and natural history of primary systemic amyloidosis in Olmsted County, Minnesota, 1950 through 1989 Blood 79, 1817-1822
11. Reece, D. E., Hegenbart, U., Sanchorawala, V., Merlini, G., Palladini, G., Bladé, J., Fermand, J.-P. P., Hassoun, H., Heffner, L., Vescio, R. a., Liu, K., Enny, C., Esseltine, D.-L. L., Van De Velde, H., Cakana, A., and Comenzo, R. L. (2011) Efficacy and safety of once-weekly and twice-weekly bortezomib in patients with relapsed systemic AL amyloidosis: Results of a phase 1/2 study Blood 118, 865-873 10.1182/blood-2011-02-334227
12. Merlini, G. and Stone, M. J. (2006) Dangerous small B-cell clones Blood 108, 2520-2530 10.1182/blood-2006-03-001164
13. Leung, N., Nasr, S. H., and Sethi, S. (2012) How I treat amyloidosis: the importance of accurate diagnosis and amyloid typing Blood 120, 3206-3213 10.1182/blood-2012-03-413682
14. Merlini, G., Wechalekar, A. D., and Palladini, G. (2013) Systemic light chain amyloidosis: An update for treating physicians Blood 121, 5124-5130 10.1182/blood-2013-01-453001
15. Kyle, R., Gertz, M., and Greipp, P. (1999) Long-term survival (10 years or more) in 30 patients with primary amyloidosis Blood 93, 1062-1066
16. Comenzo, R. L. and Gertz, M. a. (2002) Autologous stem cell transplantation for primary systemic amyloidosis Blood 99, 4276-4282 10.1182/blood.V99.12.4276
17. Palladini, G., Perfetti, V., Perlini, S., Obici, L., Lavatelli, F., Caccialanza, R., Invernizzi, R., Comotti, B., and Merlini, G. (2005) The combination of thalidomide and intermediate-dose dexamethasone is an effective but toxic treatment for patients with primary amyloidosis (AL) Blood 105, 2949-2951 10.1182/blood-2004-08-3231
18. Kastritis, E., Anagnostopoulos, A., Roussou, M., Toumanidis, S., Pamboukas, C., Migkou, M., Tassidou, A., Xilouri, I., Delibasi, S., Psimenou, E., Mellou, S., Terpos, E., Nanas, J., and Dimopoulos, M. A. (2007) Treatment of light chain (AL) amyloidosis with the combination of bortezomib and dexamethasone Haematologica 92, 1351-1358 10.3324/haematol.11325
19. Reece, D. E., Sanchorawala, V., Hegenbart, U., Merlini, G., Palladini, G., Fermand, J., Vescio, R. A., Liu, X., Elsayed, Y. a, Cakana, A., and Comenzo, R. L. (2009) Weekly and twice-weekly bortezomib in patients with systemic AL amyloidosis: results of a phase 1 dose-escalation study Blood 114, 1489-1497 10.1182/blood-2009-02-203398
20. Ward, J. E., Ren, R., Toraldo, G., SooHoo, P., Guan, J., O'Hara, C., Jasuja, R., Trinkaus-randall, V., Liao, R., Connors, L. H., Seldin, D. C., and Hara, C. O. (2011) Doxycycline reduces fibril formation in a transgenic mouse model of AL amyloidosis Blood 118, 6610-6617 10.1182/blood-2011-04-351643
21. Cohen, A. D. and Comenzo, R. L. (2010) Systemic light-chain amyloidosis: advances in diagnosis, prognosis, and therapy Hematology Am. Soc. Hematol. Educ. Program 2010, 287-294 10.1182/asheducation-2010.1.287
22. Gunasingh, M. J., Philip, J. E., Ashok, B. S., Kirubagaran, R., Jebaraj, W. C. E., Davis, G. D. J., Vignesh, S., Dhandayuthapani, S., and Jayakumar, R. (2008) Melatonin prevents amyloid protofibrillar induced oxidative imbalance and biogenic amine catabolism Life Sci. 83, 96-102 10.1016/j.lfs.2008.05.011
23. Pappolla, M., Bozner, P., Soto, C., Shao, H., Robakis, N. K., Zagorski, M., Frangione, B., and Ghiso, J. (1998) Inhibition of Alzheimer β-fibrillogenesis by melatonin J. Biol. Chem. 273, 7185-7188 10.1074/jbc.273.13.7185
24. Wang, J.-B., Wang, Y.-M., and Zeng, C.-M. (2011) Quercetin inhibits amyloid fibrillation of bovine insulin and destabilizes preformed fibrils Biochem. Biophys. Res. Commun. 415, 675-679 10.1016/j.bbrc.2011.10.135
25. Stoilova, T., Colombo, L., Forloni, G., Tagliavini, F., and Salmona, M. (2013) A new face for old antibiotics: tetracyclines in treatment of amyloidoses J. Med. Chem. 56, 5987-6006 10.1021/jm400161p
26. Giorgetti, S., Raimondi, S., Pagano, K., Relini, A., Bucciantini, M., Corazza, A., Fogolari, F., Codutti, L., Salmona, M., Mangione, P., Colombo, L., De Luigi, A., Porcari, R., Gliozzi, A., Stefani, M., Esposito, G., Bellotti, V., and Stoppini, M. (2011) Effect of tetracyclines on the dynamics of formation and destructuration of β2-microglobulin amyloid fibrils J. Biol. Chem. 286, 2121-2131 10.1074/jbc.M110.178376
27. Li, J., Zhu, M., Rajamani, S., Uversky, V. N., and Fink, A. L. (2004) Rifampicin inhibits alpha-synuclein fibrillation and disaggregates fibrils Chem. Biol. 11, 1513-1521 10.1016/j.chembiol.2004.08.025
28. Rezai-Zadeh, K., Arendash, G. W., Hou, H., Fernandez, F., Jensen, M., Runfeldt, M., Shytle, R. D., and Tan, J. (2008) Green tea epigallocatechin-3-gallate (EGCG) reduces β-amyloid mediated cognitive impairment and modulates tau pathology in Alzheimer transgenic mice Brain Res. 1214, 177-187 10.1016/j.brainres.2008.02.107
29. Bieschke, J., Russ, J., Friedrich, R. P., Ehrnhoefer, D. E., Wobst, H., Neugebauer, K., and Wanker, E. E. (2010) EGCG remodels mature alpha-synuclein and amyloid-beta fibrils and reduces cellular toxicity Proc. Natl. Acad. Sci. U. S. A. 107, 7710-7715 10.1073/pnas.0910723107
30. Roberts, B. E., Duennwald, M. L., Wang, H., Chung, C., Nicholas, P., Sweeny, E. A., Knight, M. N., and Shorter, J. (2009) A synergistic small molecule combination directly eradicates diverse prion strain structures Nat. Chem. Biol. 5, 936-946 10.1038/nchembio.246
31. Meng, F., Abedini, A., Plesner, A., Verchere, C. B., and Raleigh, D. P. (2010) The flavanol (-)-epigallocatechin 3-gallate inhibits amyloid formation by islet amyloid polypeptide, disaggregates amyloid fibrils, and protects cultured cells against IAPP-induced toxicity Biochemistry 49, 8127-8133 10.1021/bi100939a
32. Hunstein, W. (2007) Epigallocathechin-3-gallate in AL amyloidosis: a new therapeutic option? Blood 110, 2216 10.1182/blood-2007-05-089243
33. Mereles, D., Buss, S. J., Hardt, S. E., Hunstein, W., and Katus, H. A. (2010) Effects of the main green tea polyphenol epigallocatechin-3-gallate on cardiac involvement in patients with AL amyloidosis Clin. Res. Cardiol. 99, 483-490 10.1007/s00392-010-0142-x
34. Mereles, D., Wanker, E. E., and Katus, H. A. (2008) Therapy effects of green tea in a patient with systemic light-chain amyloidosis Clin. Res. Cardiol. 97, 341-344 10.1007/s00392-008-0649-6
35. Wilkins, M. R., Gasteiger, E., Bairoch, A., Sanchez, J. C., Williams, K. L., Appel, R. D., and Hochstrasser, D. F. (1999) Protein identification and analysis tools in the ExPASy server Methods Mol. Biol. 112, 531-552 10.1385/1-59259-584-7:531
36. Delaglio, F., Grzesiek, S., Vuister, G. W., Zhu, G., Pfeifer, J., and Bax, A. (1995) NMRPipe: a multidimensional spectral processing system based on UNIX pipes J. Biomol. NMR 6, 277-293 10.1007/BF00197809
37. Keller, R. L. J. (2004) The Computer Aided Resonance Assignment Tutorial, CANTINA Verlag.
38. Rooney, L. M., Sachchidanand, and Werner, J. M. (2004) Characterizing domain interfaces by NMR Methods Mol. Biol. 278, 123-138 10.1385/1-59259-809-9:123
39. Foster, M. P., Wuttke, D. S., Clemens, K. R., Jahnke, W., Radhakrishnan, I., Tennant, L., Reymond, M., Chung, J., and Wright, P. E. (1998) Chemical shift as a probe of molecular interfaces: NMR studies of DNA binding by the three amino-terminal zinc finger domains from transcription factor IIIA J. Biomol. NMR 12, 51-71 10.1023/A:1008290631575
40. Trott, O. and Olson, A. J. (2010) AutoDock Vina: improving the speed and accuracy of docking with a new scoring function, efficient optimization, and multithreading J. Comput. Chem. 31, 455-461 10.1002/jcc.21334
41. Irwin, J. J., Sterling, T., Mysinger, M. M., Bolstad, E. S., and Coleman, R. G. (2012) ZINC: a free tool to discover chemistry for biology J. Chem. Inf. Model. 52, 1757-1768 10.1021/ci3001277
42. Laskowski, R. a. and Swindells, M. B. (2011) LigPlot+: Multiple ligand-protein interaction diagrams for drug discovery J. Chem. Inf. Model. 51, 2778-2786 10.1021/ci200227u
43. Larkin, M. A., Blackshields, G., Brown, N. P., Chenna, R., Mcgettigan, P. A., McWilliam, H., Valentin, F., Wallace, I. M., Wilm, A., Lopez, R., Thompson, J. D., Gibson, T. J., and Higgins, D. G. (2007) Bioinformatics 23, 2947-2948 10.1093/bioinformatics/btm404
44. Benson, D. A., Karsch-Mizrachi, I., Lipman, D. J., Ostell, J., and Wheeler, D. L. (2004) GenBank Nucleic Acids Res. 33, D34-D38 10.1093/nar/gki063
45. Retter, I., Althaus, H. H., Münch, R., and Müller, W. (2004) VBASE2, an integrative V gene database Nucleic Acids Res. 33, D671-D674 10.1093/nar/gki088
46. Bodi, K., Prokaeva, T., Spencer, B., Eberhard, M., Connors, L. H., and Seldin, D. C. (2009) AL-Base: a visual platform analysis tool for the study of amyloidogenic immunoglobulin light chain sequences Amyloid 16, 1-8 10.1080/13506120802676781
47. Sussman, J. L., Lin, D., Jiang, J., Manning, N. O., Prilusky, J., Ritter, O., and Abola, E. E. (1998) Protein Data Bank (PDB): Database of three-dimensional structural information of biological macromolecules Acta Crystallogr., Sect. D: Biol. Crystallogr. 54, 1078-1084 10.1107/S0907444998009378
48. Lee, J., Jeong, K., and Kim, Y. (2011) Epigallocatechin 3-gallate Binds to Human Salivary α-Amylase with Complex Hydrogen Bonding Interactions Bull. Korean Chem. Soc. 32, 2222-2226 10.5012/bkcs.2011.32.7.2222
49. Nguyen, T. T. H., Jung, S.-H. H., Lee, S., Ryu, H.-J. J., Kang, H.-K. K., Moon, Y.-H. H., Kim, Y.-M. M., Kimura, A., and Kim, D. (2012) Inhibitory effects of epigallocatechin gallate and its glucoside on the human intestinal maltase inhibition Biotechnol. Bioprocess Eng. 17, 966-971 10.1007/s12257-012-0242-8
50. Hyung, S., DeToma, A. S., Brender, J. R., Lee, S., Vivekanandan, S., Kochi, A., Choi, J.-S., Ramamoorthy, A., Ruotolo, B. T., and Lim, M. H. (2013) Insights into antiamyloidogenic properties of the green tea extract (-)-epigallocatechin-3-gallate toward metal-associated amyloid-β species Proc. Natl. Acad. Sci. U. S. A. 110, 3743-3748 10.1073/pnas.1220326110
51. Abraham, R. S., Geyer, S. M., Price-Troska, T. L., Allmer, C., Kyle, R. a., Gertz, M. a., and Fonseca, R. (2003) Immunoglobulin light chain variable (V) region genes influence clinical presentation and outcome in light chain-associated amyloidosis (AL) Blood 101, 3801-3807 10.1182/blood-2002-09-2707
52. Comenzo, R. L. (2001) The tropism of organ involvement in primary systemic amyloidosis: contributions of Ig VL germ line gene use and clonal plasma cell burden Blood 98, 714-720 10.1182/blood.V98.3.714
53. Gil-Rodríguez, P. and Amero, C. (2015) (1)H, (15)N and (13)C resonance assignments for 3rC and 3rCWP: amyloidogenic variants of imunoglobulin λ 3 light-chain Biomol. NMR Assignments 9, 139-142 10.1007/s12104-014-9560-4
54. Qin, Z., Hu, D., Zhu, M., and Fink, A. L. (2007) Structural characterization of the partially folded intermediates of an immunoglobulin light chain leading to amyloid fibrillation and amorphous aggregation Biochemistry 46, 3521-3531 10.1021/bi061716v