Concanavalin A aggregation and toxicity on cell cultures

Biochimica et Biophysica Acta - Proteins and Proteomics

Volumn 1804, Issue 1, 2010, Pages 173-183

  Vetri, Valeria ^a   Carrotta, Rita ^b   Picone, Pasquale ^a,c   Di Carlo, Marta ^c   Militello, Valeria ^a  

^a UNIVERSITY OF PALERMO   (Italy)

^b CNR   (Italy)

^c CNR Consiglio Nazionale delle Ricerche   (Italy)

Author keywords

Amyloid fibril; Concanavalin A; Light scattering; Oligomers cytotoxicity

Indexed keywords

AMYLOID; CASPASE 8; CONCANAVALIN A; OLIGOMER; THIOFLAVINE;

APOPTOSIS; ARTICLE; ATOMIC FORCE MICROSCOPY; CELL CULTURE; CELL MEMBRANE; CELL VIABILITY; CONFOCAL MICROSCOPY; CONFORMATIONAL TRANSITION; CYTOTOXICITY; EXPERIMENTAL STUDY; HUMAN; HUMAN CELL; INFRARED SPECTROSCOPY; LIGHT SCATTERING; NEUROBLASTOMA CELL; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN INTERACTION; PROTEIN STRUCTURE;

AMYLOID; APOPTOSIS; CELL LINE, TUMOR; CELL SURVIVAL; CONCANAVALIN A; HUMANS; MICROSCOPY, ATOMIC FORCE; NEURONS; PROTEIN STRUCTURE, QUATERNARY; SPECTROSCOPY, FOURIER TRANSFORM INFRARED;

EID: 71749097637     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2009.09.013     Document Type: Article

References (66)

1. Rochet J.C., and Lansbury P.T.J. Amyloid fibrillogenesis: themes and variations. Curr. Opin. Struct. Biol. 10 (2000) 60-68
2. Ellis R.J., and Pinheiro T.J.T. Medicine: danger-misfolding proteins. Nature 416 (2002) 483-484
3. Bucciantini M., Giannoni E., Chiti F., Baroni F., Formigli L., Zurdo J., Taddei N., Ramponi G., Dobson C.M., and Stefani M. Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases. Nature 416 (2002) 507-511
4. Ross C.A., and Poirier M.A. Protein aggregation and neurodegenerative disease. Nat. Med. 10 (2004) 10-17
5. Walsh D.M., and Selkoe D.J. Oligomers on the brain: the emerging role of soluble protein aggregates in neurodegeneration. Protein Pept. Lett. 11/3 (2004) 213-228
6. Herczenik H., and Gebbink M.F.B.G. Molecular and cellular aspects of protein misfolding and disease. FASEB J. 22 (2008) 2115-2133
7. Walsh M.D., Klyubin I., Fadeeva J.V., Cullen W.K., Anwyl R., Wolfe M.S., Rowan M.J., and Selkoe D.J. Naturally secreted oligomers of amyloid beta protein potently inhibit hippocampal long-term potentiation in vivo. Nature 416 (2002) 535-539
8. Volles M.J., Lee S.J., Rochet J.C., Shtilerman M.D., Ding T.T., Kessler J.C., and Lansbury Jr. P.T. Vesicle permeabilization by protofibrillar alpha-synuclein: implications for the pathogenesis and treatment of Parkinson's disease. Biochemistry 40 (2001) 7812-7819
9. Kim H.J., Chae S.C., Lee D.K., Chromy B., Lee S.C., Park Y.C., Klein W.L., Krafft G.A., and Hong S.T. Selective neuronal degeneration induced by soluble oligomeric amyloid beta protein. FASEB J. 17 (2003) 118-120
10. Carrotta R., Di Carlo M., Manno M., Montana G., Picone P., Romancino D., and San Biagio P.L. Toxicity of recombinant beta-amyloid prefibrillar oligomers on the morphogenesis of the sea urchin Paracentrotus lividus. FASEB J. 20 /11 (2006) 1916-1917
11. Bitan G. Structural study of metastable amyloidogenic protein oligomers by photo-induced Cross-linking of unmodified proteins. Methods Enzymol. 413 (2006) 217-236
12. Zamotin V., Gharibyan A., Gibanova N.V., Lavrikova M.A., Dolgikh D.A., Kirpichnikov M.P., Kostanyan I.A., and Morozova-Roche L.A. Cytotoxicity of albebetin oligomers depends on cross-β-sheet formation. FEBS Lett. 580/10 (2006) 2451-245
13. Morozova-Roche L.A., Zamotin V., Malisauskas M., Ohman A., Chertkova R., Lavrikova M.A., Kostanyan I.A., Dolgikh D.A., and Kirpichnikov M.P. Fibrillation of carrier protein albebetin and its biologically active constructs. Multiple oligomeric intermediates and pathways. Biochemistry 43 (2004) 9610-9619
14. Cleary J.P., Walsh D.M., Hofmeister J.J., Shankar G.M., Kuskowski M.A., Selkoe D.J., and Ashe K.H. Natural oligomers of the amyloid-beta protein specifically disrupt cognitive function. Nat Neurosci. 8 (2005) 79-84
15. Andersson K., Olofsson A., Nielsen E.H., Svehag S., and Lundgren E. Only amyloidogenic intermediates of transthyretin induce apoptosis. Biochem. Biophys. Res. Commun. 294 (2002) 309-314
16. Novitskaya O., Bocharova V., Bronstein I., and Baskakov I.V. Amyloid fibrils of mammalian prion protein are highly toxic to cultured cells and primary neurons. J. Biol. Chem. 281/19 (2006) 13828-13836
17. Gharibyan A.L., Zamotin V., Yanamandra K., Moskaleva O.S., Margulis B.A., Kostanyan I.A., and Morozova-Roche L.A. Lysozyme amyloid oligomers and fibrils induce cellular death via different apoptotic/necrotic pathways. J. Mol. Biol. 365 (2007) 1337-1349
18. Sirangelo I., Malmo C., Iannuzzi C., Mezzogiorno A., Bianco M.R., Papa M., and Irace G. Fibrillogenesis and cytotoxic activity of the amyloid-forming apomyoglobin mutant W7FW14F. J. Biol. Chem. 279 (2004) 13183-13189
19. Sunde M., and Blake C. The structure of amyloid fibrils by electron microscopy and X-ray diffraction. Adv. Protein Chem. 50 (1997) 123-159
20. Pedersen J.S., Dikov D., Flink J.L., Hjuler H.A., Christiansen G., and Otzen D.E. The changing face of glucagon fibrillation: structural polymorphism and conformational imprinting. J. Mol. Biol. 355 (2006) 501-523
21. Anderson M., Bocharova O.V., Makarava N., Breydo L., Salnikov V.V., and Baskakov I.V. Polymorphism and ultrastructural organization of prion protein amyloid fibrils: an insight from high resolution atomic force microscopy. J. Mol. Biol. 358 (2006) 580-596
22. Petkova A.T., Leapman R.D., Guo Z., Yau W.M., Mattson M.P., and Tycko R. Self-propagating, molecular-level polymorphism in Alzheimer's beta-amyloid fibrils. Science 307 (2005) 262-265
23. San Biagio P.L., Bulone D., Emanuele A., and Palma M.U. Self-assembly of biopolymeric structures below the threshold of random cross-link percolation. Biophys. J 70 (1996) 494-499
24. Manno M., Emanuele A., Martorana V., Bulone D., San Biagio P.L., Palma-Vittorelli M.B., and Palma M.U. Multiple interactions between molecular and supramolecular ordering. Phys. Rev. E 159 (1999) 2222-2230
25. Modler J., Gast K., Lutsch G., and Damaschun G. Assembly of amyloid protofibrils via critical oligomers-a novel pathway of amyloid formation. J. Mol. Biol. 325 (2003) 135-148
26. Vaiana S.M., Palma-Vittorelli M.B., and Palma I M.U. Time scale of protein aggregation dictated by liquid-liquid demixing. Proteins 51 (2003) 147-153
27. Militello V., Vetri V., and Leone M. Conformational changes involved in thermal aggregation processes of bovine serum albumin. Biophys. Chem. 105 (2003) 133-141
28. Khurana R., Gillespie J.R., Talapatra A., Minert L.J., Ionescu-Zanetti C., Millett I., and Fink A.L. Partially folded intermediates as critical precursors of light chain amyloid fibrils and amorphous aggregates. Biochemistry 40 (2001) 3525-3535
29. Uversky V.N., and Fink A.L. Conformational constraints for amyloid fibrillation: the importance of being unfolded. Biochim. Biophys. Acta 1698 (2004) 131-153
30. Hamada D., Segawa S., and Goto Y. Non-native alpha-helical intermediate in the refolding of beta-lactoglobulin, a predominantly beta-sheet protein. Nat. Struct. Biol. 3 (1996) 868-873
31. Militello V., Casarino C., Emanuele A., Giostra A., Pullara F., and Leone M. Aggregation kinetics of bovine serum albumin studied by FTIR spectroscopy and light scattering. Biophys. Chem. 107 (2004) 175-187
32. Jahn T., and Radford S.E. Folding versus aggregation: polypeptide conformations on competing pathways Arch. Biochem. Biophys. 469 (2008) 100-117
33. Svanborg C., Agerstam H., Aronson A., Bjerkvig R., Duringer C., Fischer W., Gustafsson L., Hallgren O., Leijonhuvud I., Linse S., Mossberg A.K., Nilsson H., Pettersson J., and Svensson M. HAMLET kills tumor cells by an apoptosis-like mechanism-cellular, molecular, and therapeutic aspects. Adv. Cancer Res. 88 (2003) 1-29
34. Zhang Y.H., Leliveld S.R., Kooistra K., Molenaar C., Rohn J.L., Tanke H.J., Abrahams J.P., and Noteborn M.H.M. Recombinant apoptin multimers kill tumor cells but are non-toxic and epitope-shielded in a normal-cell-specific fashion. Exp. Cell Res. 289 (2003) 36-46
35. S. Ceru, E. Zerovnik, Similar toxicity of the oligomeric molten globule state and the prefibrillar oligomers, FEBS Lett., 582/2 (2008), 23:203-209
36. Vetri V., Canale C., Relini A., Librizzi F., Militello V., Gliozzi A., and Leone M. Amyloid fibrils formation and amorphous aggregation in concanavalin A. Biophys. Chem. 125 (2006) 184-1954
37. Vetri V., Librizzi F., Militello V., and Leone M. Effect of succinylation on thermal induced amyloid formation in concanavalin A. Eur. Biophys J. 36 (2007) 733-741
38. Janssen O., Scheffler A., and Kabelitz D. In vitro effects of mistletoe extracts and mistletoe lectins cytotoxicity towards tumor cells due to the induction of programmed cell death (apoptosis). Arzneim.-Forsch. 133 (1993) 12221-12227
39. Kim M., Rao M.V., Tweardy D.J., Prakash M., Gralili U., and Gorelik E. Lectin-induced apoptosis of tumour cells. Glycobiology 3 (1993) 447-453
40. Ruhul Amin A.R.M., Paul R.K., Thakur V.S., and Agarwal M.L. Novel role for p73 in the regulation of Akt-Foxo1a-Bim signaling and apoptosis induced by the plant lectin, concanavalin A. Cancer Res. 67 (2007) 5617-5620
41. Liu B., Li C.-Y., Bian H.-j., Min M.-w., Chen L.-f., and Bao J.-k. Antiproliferative activity and apoptosis-inducing mechanism of concanavalin A on human melanoma A375 cells. Arch. Biochem. Biophys. 482 (2009) 1-6
42. Tiegs G., Hentschel J., and Wendel A. A T cell-dependent experimental liver injury in mice inducible by concanavalin A. J. Clin. Invest. 90 (1992) 196-203
43. Senear D.F., and Teller D.C. Effects of saccharide and salt binding on dimer-tetramer equilibrium of concanavalin A. Biochemistry 26 (1981) 3083-3091
44. Kulkarni G.V., and McCulloch C.A.G. Concanavalin A induced apoptosis in fibroblasts: the role of cell surface carbohydrates in lectin mediated cytotoxicity. J. Cell. Physiol. 165 (1995) 119-133
45. Suen Y.K., Fung K.P., Choy Y.M., Lee C.Y., Chan C.W., and Kong S.K. Concanavalin A induced apoptosis in murine macrophage PU5-1.8 cells through clustering of mitochondria and release of cytochrome c. Apoptosis 5 (2004) 369-377
46. Cribbs D.H., Kreng V.M., Anderson J., and Cotman C.W. Cross-linking of concanavalin A receptors on cortical neurons induces programmed cell death. Neuroscience 75 (1996) 173-185
47. Anderson A.J., Pike C.J., and Cotman C.W. Differential induction of immediate early gene proteins in cultured neurons by beta-amyloid (Aβ): association of c-Jun with Aβ-induced apoptosis. J. Neurochem. 65 (1995) 1487-1498
48. Picone P., Carrotta R., Montana G., Nobile M.R., San Biagio P.L., and Di Carlo M. Abeta oligomers and fibrillar aggregates induce different apoptotic pathways in LAN 5 neuroblastoma cell cultures. Biophys. J. 96 (2009) 1-12
49. Carrotta R., Manno M., Bulone D., Martorana V., and San Biagio P.L. Protofibril formation of amyloid beta-protein at low pH via a non-cooperative elongation mechanism. J. Biol. Chem. 280 (2005) 30001-30008
50. Berne B.J., and Pecora R. Dynamic Light Scattering (1976), Wiley Interscience, New York, NY
51. Schmitz K.S. An Introduction to Dynamic Light Scattering by Macromolecules (1990), Academic Press, Inc
52. Foderà V., Groenning M., Vetri V., Librizzi F., Spagnolo S., Cornett C., Olsen L., van de Weert M., and Leone M. Thioflavin T hydroxylation at basic pH and its effect on amyloid fibril detection. J. Phys. Chem. B 112 (2008) 15174-15181
53. LeVine III H. Quantification of beta-sheet amyloid fibril structures with thioflavin T. Methods Enzymol. 309 (1999) 274-284
54. Chimon S., and Ishii Y. Capturing intermediate structures of Alzheimer's b-amyloid, Ab(1-40), by solid-state NMR spectroscopy. J. Am. Chem. Soc. 127 (2005) 13472-13473
55. Levine III H. Stopped-flow kinetics reveal multiple phases of thioflavin T binding to Alzheimer beta (1-40) amyloid fibrils. Arch. Biochem. Biophys. 342 (1997) 306-316
56. Foderà V., Librizzi F., Groenning M., van de Weert M., and Leone M. Secondary nucleation and accessible surface in insulin amyloid fibril formation. Phys. Chem. B 112 (2008) 3853-3858
57. Y.B. Yan, Z. Jun, He, Hua-Wei, Zhou, Hai-Meng v Oligomerization and Aggregation of Bovine Pancreatic Ribonuclease A: Characteristic Events Observed by FTIR Spectroscopy Biophys. J. 90 (2006) 2525-2533.
58. Carrotta R., Waninge R.B.R., and Rischel C. Conformational characterization of oligomeric intermediates and aggregates in β-lactoglobulin heat aggregation. Protein Sci. 101 (2001) 312-318
59. Stefani M., and Dobson C.M. Protein aggregation and aggregate toxicity: new insights into protein folding, misfolding diseases and biological evolution. J. Mol. Med. 81 (2003) 678-699
60. Zhu M., Souillac P.O., Ionescu-Zanetti C., Carter S.A., and Fink A.L. Surface-catalyzed Amyloid Fibril Formation. J. Biol. Chem. 277 (2002) 50914-50922
61. Zhao H., Tuominen E.K.J., and Kinnunen P.K.J. Formation of amyloid fibers triggered by phosphatidylserine-containing membranes. Biochemistry 43 (2004) 10302-10307
62. Meng X., Fink A.L., and Uversky V.N. The effect of membranes on the in vitro Fibrillation of an amyloidogenic light-chain variable-domain SMA. J. Mol. Biol. 381 (2008) 989-999
63. Bateman D.A., McLaurin J., and Chakrabartty A. Requirement of aggregation propensity of Alzheimer amyloid peptides for neuronal cell surface binding. Neuroscience 8 (2007) 29
64. Engel M.F.M., Khemtemourian L., Kleijer C.C., Meeldijk H.J.D., Jacobs J., Verkleij A.J., de Kruijff B., Killian J.A., and Hoppener W.J.M. Membrane damage by human islet amyloid polypeptide through fibril growth at the membrane. PNAS 105 (2008) 6033-6038
65. Stefani M. Generic cell dysfunction in neurodegenerative disorders: role of surfaces in early protein misfolding, aggregation, and aggregate cytotoxicity. Neuroscience 13 (2007) 519-531
66. Pellistri F., Bucciantini M., Relini A., Nosi D., Gliozzi A., Robello M., and Stefani M. Nonspecific interaction of prefibrillar amyloid aggregates with glutamatergic receptors results in Ca2+ increase in primary neuronal cells. J. Biol. Chem. 283 (2008) 29950-29960