Study of the complement activation by amyloid aggregates of smooth muscle titin in vitro

References

• Chiti, F.; Dobson, C. M.; Misfolding, P.; Formation, A. Human Disease: A Summary of Progress over the Last Decade. Annu. Rev. Biochem. 2017, 86, 27–68. DOI: 10.1146/annurev-biochem-061516-045115.
   PubMed Web of Science ®Google Scholar
• Crouch, P. J.; Tew, D. J.; Du, T.; Nguyen, D. N.; Caragounis, A.; Filiz, G.; et al. Restored Degradation of the Alzheimer’s Amyloid-beta Peptide by Targeting Amyloid Formation. J. Neurochem. 2009, 108, 1198–1207. DOI: 10.1111/j.1471-4159.2009.05870.x.
   PubMed Web of Science ®Google Scholar
• Buxbaum, J. N.; Linke, R. P. A Molecular History of the Amyloidosis. J. Mol. Biol. 2012, 421, 142–159. DOI: 10.1016/j.jmb.2012.01.024.
   PubMed Web of Science ®Google Scholar
• Westermark, P.; Benson, M. D.; Buxbaum, J. N.; Cohen, A. S.; Frangione, B.; Ikeda, S.; Masters, C. L.; Merlini, G.; Saraiva, M. J.; Sipe, J. D.; et al. A Primer of Amyloid Nomenclature. Amyloid. 2007, 14(3), 179–183.
   PubMed Web of Science ®Google Scholar
• Liao, R.; Ward, J. E. Amyloid Cardiomyopathy – Disease on the Rise. Circ. Res. 2017, 120(12), 1865–1867.
   PubMed Web of Science ®Google Scholar
• Fikrlea, M.; Palecekab, T.; Kuchynka, P.; Nemecek, E.; Bauerovac, L.; Straub, J.; et al. Cardiac Amyloidosis: A Comprehensive Review. Corevasa. 2013, 55(1), e60–e75.
   Google Scholar
• Liewluck, T.; Milone, M. Characterization of Isolated Amyloid Myopathy. Eur. J. Neurol. 2017, 24(12), 1437–1445. DOI: 10.1111/ene.2017.24.issue-12.
   PubMed Web of Science ®Google Scholar
• Uversky, V. N.; Fink, A. L. Conformational Constraints for Amyloid Fibrillation: The Importance of Being Unfolded. Biochim. Biophys. Acta. 2004, 1698(2), 131–153. DOI: 10.1016/j.bbapap.2003.12.008.
   PubMed Web of Science ®Google Scholar
• Bosch-Morató, M.; Iriondo, C.; Guivernau, B.; Valls-Comamala, V.; Vidal, N.; Olivé, M.; Querfurth, H.; Muñoz, F. J.; et al. Increased Amyloid β-peptide Uptake in Skeletal Muscle Is Induced by Hyposialylation and May Account for Apoptosis in GNE Myopathy. Oncotarget. 2016, 7(12), 13354–13371.
   PubMedGoogle Scholar
• Yamada, M.; Tsukagoshi, H.; Hatakeyama, S. Skeletal Muscle Amyloid Deposition in AL- (Primary or myeloma-associated), AA- (Secondary), and Prealbumin-type Amyloidosis. J. Neurol. Sci. 1988, 85(2), 223–232. DOI: 10.1016/0022-510X(88)90158-X.
   PubMed Web of Science ®Google Scholar
• Janeway, C. A., Jr.; Travers, P.; Walport, M.; et al. Immunobiology: The Immune System in Health and Disease. 5th Edition. The Complement System and Innate Immunity; Garland Science: New York, 2001.
   Google Scholar
• Kuby, J. Immunology. 2; WH Freeman: New York, 1994; pp 402.
   Google Scholar
• Afagh, A.; Cummings, B. J.; Cribbs, D. H.; Cotman, C. W.; Tenner, A. J. Localization and Cell Association of C1q in Alzheimer’s Disease Brain. Exp. Neurol. 1996, 138, 22–32. DOI: 10.1006/exnr.1996.0043.
   PubMed Web of Science ®Google Scholar
• Chen, S.; Frederickson, R. C.; Brunden, K. R. Neuroglial-mediated Immunoinflammatory Responses in Alzheimer’s Disease: Complement Activation and Therapeutic Approaches. Neurobiol. Aging. 1996, 17, 781–787. DOI: 10.1016/0197-4580(96)00103-0.
   PubMed Web of Science ®Google Scholar
• Jiang, H.; Burdick, D.; Glabe, C. G.; Cotman, C. W.; Tenner, A. J. β-Amyloid Activates Complement by Binding to a Specific Region of the Collagen-like Domain of the C1q a Chain. J. Immunol. 1994, 152, 5050–5059.
   PubMed Web of Science ®Google Scholar
• Rogers, J.; Cooper, N. R.; Webster, S.; Schultz, J.; McGeer, P. L.; Styren, S. D.; Civin, W. H.; Brachova, L.; Bradt, B.; Ward, P.; et al. Complement Activation by Beta-amyloid in Alzheimer Disease. Proc. Natl. Acad. Sci. USA. 1992, 89, 10016–10020. DOI: 10.1073/pnas.89.21.10016.
   PubMed Web of Science ®Google Scholar
• Webster, S.; Bradt, B.; Rogers, J.; Cooper, N. Aggregation State-dependent Activation of the Classical Complement Pathway by the Amyloid Beta Peptide. J. Neurochem. 1997, 69, 388–398. DOI: 10.1046/j.1471-4159.1997.69010388.x.
   PubMed Web of Science ®Google Scholar
• Webster, S.; Lue, L. F.; Brachova, L.; Tenner, A.; McGeer, P. L.; Terai, K.; Walker, D. G.; Bradt, B.; Cooper, N. R.; Rogers, J.; et al. Molecular and Cellular Characterization of the Membrane Attack Complex, C5b-9, in Alzheimer’s Disease. Neurobiol. Aging. 1997, 18, 415–421. DOI: 10.1016/S0197-4580(97)00042-0.
   PubMed Web of Science ®Google Scholar
• Veerhuis, R.; Van Breemen, M. J.; Hoozemans, J. M.; Morbin, M.; Ouladhadj, J.; Tagliavini, F.; Eikelenboom, P.; et al. Amyloid Beta Plaque-associated Proteins C1q and SAP Enhance the Abeta1-42 Peptide-induced Cytokine Secretion by Adult Human Microglia in Vitro. Acta Neuropathol. 2003, 105(2), 135–144.
   PubMed Web of Science ®Google Scholar
• Tacnet-Delorme, P.; Chevallier, S.; Arlaud, G. J. Beta-amyloid Fibrils Activate the C1 Complex of Complement under Physiological Conditions: Evidence for A Binding Site for A Beta on the C1q Globular Regions. J. Immunol. 2001, 167(11), 6374–6381. DOI: 10.4049/jimmunol.167.11.6374.
   PubMed Web of Science ®Google Scholar
• Bradt, B. M.; Kolb, W. P.; Cooper, N. R. Complement-dependent Proinflammatory Properties of the Alzheimer’s Disease Beta-peptide. J. Exp. Med. 1998, 188, 431–438. DOI: 10.1084/jem.188.3.431.
   PubMed Web of Science ®Google Scholar
• Strohmeyer, R.; Shen, Y.; Rogers, J. Detection of Complement Alternative Pathway mRNA and Proteins in the Alzheimer’s Disease Brain. Mol. Brain Res. 2000, 81(1–2), 7–18. DOI: 10.1016/S0169-328X(00)00149-2.
   PubMedGoogle Scholar
• Watson, M. D.; Roher, A. E.; Kim, K. S.; Spiegel, K.; Emmerling, M. R. Complement Interactions with amyloid-β 1–42: A Nidus for Inflammation in AD Brains. Amyloid. 1997, 4, 147–156. DOI: 10.3109/13506129709014379.
   Web of Science ®Google Scholar
• Eikelenboom, P.; Stam, F. C. Immunoglobulins and Complement Factors in Senile Plaques. An Immunoperoxidase Study. Acta Neuropathol. 1982, 57, 239–242. DOI: 10.1007/BF00685397.
   PubMed Web of Science ®Google Scholar
• McGeer, P. L.; Akiyama, H.; Itagaki, S.; McGeer, E. G. Activation of the Classical Complement Pathway in Brain Tissue of Alzheimer Patients. Neurosci. Lett. 1989, 107, 341–346. DOI: 10.1016/0304-3940(89)90843-4.
   PubMed Web of Science ®Google Scholar
• Shen, Y.; Li, R.; McGeer, E. G.; McGeer, P. L. Neuronal Expression of mRNAs for Complement Proteins of the Classical Pathway in Alzheimer Brain. Brain Res. 1997, 769, 391–395. DOI: 10.1016/S0006-8993(97)00850-0.
   PubMed Web of Science ®Google Scholar
• Landlinger, C.; Oberleitner, L.; Gruber, P.; Noiges, B.; Yatsyk, K.; Santic, R.; Mandler, M.; Staffler, G.; et al. Active Immunization against Complement Factor C5a: A New Therapeutic Approach for Alzheimer’s Disease. J. Neuroinflammation. 2015, 12, 150. DOI: 10.1186/s12974-015-0369-6.
   PubMed Web of Science ®Google Scholar
• Klegeris, A.; McGeer, P. L. Complement Activation by Islet Amyloid Polypeptide (IAPP) and Alpha-synuclein 112. Biochem. Biophys. Res. Commun. 2007, 357(4), 1096–1099. DOI: 10.1016/j.bbrc.2007.04.055.
   PubMed Web of Science ®Google Scholar
• Dumestre-Pérard, C.; Osmundson, J.; Lemaire-Vieille, C.; Thielens, N.; Grives, A.; Favier, B.; Csopaki, F.; Jamin, M.; Gagnon, J.; Cesbron, J.-Y.; et al. Activation of Classical Pathway of Complement Cascade by Soluble Oligomers of Prion. Cell. Microbiol. 2007, 9(12), 2870–2879.
   PubMed Web of Science ®Google Scholar
• Romling, U.; Bian, Z.; Hammar, M.; Sierralta, W. D.; Normark, S. Curli Fibers are Highly Conserved between Salmonella Typhimurium and Escherichia Coli with respect to Operon Structure and Regulation. J. Bacteriol. 1998, 180, 722–731.
   PubMed Web of Science ®Google Scholar
• Claessen, D.; Rink, R.; de Jong, W.; Siebring, J.; de Vreugd, P.; Boersma, F. G.; et al. A Novel Class of Secreted Hydrophobic Proteins Is Involved in Aerial Hyphae Formation in Streptomyces Coelicolor by Forming Amyloid-like Fibrils. Genes Dev. 2003, 17, 1714–1726. DOI: 10.1101/gad.264303.
   PubMed Web of Science ®Google Scholar
• Otzen, D.; Nielsen, P. H. We Find Them Here, We Find Them There: Functional Bacterial Amyloid. Cell. Mol. Life Sci. 2008, 65(6), 910–927. DOI: 10.1007/s00018-007-7404-4.
   PubMed Web of Science ®Google Scholar
• Wöesten, H. A.; de Vocht, M. L. Hydrophobins, the Fungal Coat Unraveled. Biochim. Biophys. Acta. 2000, 1469, 79–86. DOI: 10.1016/S0304-4157(00)00002-2.
   PubMed Web of Science ®Google Scholar
• Iconomidou, V. A.; Chryssikos, G. D.; Gionis, V.; Galanis, A. S.; Cordopatis, P.; Hoenger, A.; Hamodrakas, S. J.; et al. Amyloid Fibril Formation Propensity Is Inherent into the Hexapeptidetandemly Repeating Sequence of the Central Domain of Silk Moth Chorion Proteins of the A-family. J. Struct. Biol. 2006, 156, 480–488. DOI: 10.1016/j.jsb.2006.08.011.
   PubMed Web of Science ®Google Scholar
• Slotta, U.; Hess, S.; Spiess, K.; Stromer, T.; Serpell, L.; Scheibel, T. Spider Silk and Amyloid Fibrils: A Structural Comparison. Macromol. Biosci. 2007, 7, 183–188. DOI: 10.1002/(ISSN)1616-5195.
   PubMed Web of Science ®Google Scholar
• Franchi, N.; Ballarin, L.; Peronato, A.; Cima, F.; Grimaldi, A.; Girardello, R.; de Eguileor, M.; et al. Functional Amyloidogenesis in Immunocytes from the Colonial Ascidian Botryllus Schlosseri: Evolutionary Perspective. Dev. Comp. Immunol. 2019, 90, 108–120. DOI: 10.1016/j.dci.2018.09.010.
   PubMed Web of Science ®Google Scholar
• Si, K.; Lindquist, S.; Kandel, E. R. A Neuronal Isoform of the Aplysia CPEB Has Prion-like Properties. Cell. 2003, 115, 879–891. DOI: 10.1016/S0092-8674(03)01020-1.
   PubMed Web of Science ®Google Scholar
• Hewetson, A.; Do, H. Q.; Myers, C.; Muthusubramanian, A.; Sutton, R. B.; Wylie, B. J.; Cornwall, G. A. Functional Amyloids in Reproduction. Biomolecules. 2017, 7(3), e46. DOI: 10.3390/biom7030046.
   PubMed Web of Science ®Google Scholar
• Fowler, D. M.; Koulov, A. V.; Alory-Jost, C.; Marks, M. S.; Balch, W. E.; Kelly, J. W.; Weissman, J. Functional Amyloid Formation within Mammalian Tissue. PLoS Biol. 2006, 4(1), e6. DOI: 10.1371/journal.pbio.0040006.
   PubMed Web of Science ®Google Scholar
• Pulze, L.; Bassani, B.; Gini, E.; D’Antona, P.; Grimaldi, A.; Luini, A.; Marino, F.; Noonan, D. M.; Tettamanti, G.; Valvassori, R.; et al. NET Amyloidogenic Backbone in Human Activated Neutrophils. Clin. Exp. Immunol. 2016, 183(3), 469–479.
   PubMed Web of Science ®Google Scholar
• Biesecker, S. G.; Nicastro, L. K.; Wilson, R. P.; Tükel, Ç. The Functional Amyloid Curli Protects Escherichia Coli against Complement-Mediated Bactericidal Activity. Biomolecules. 2018, 8(1), e5. DOI: 10.3390/biom8010005.
   PubMed Web of Science ®Google Scholar
• Dorta-Estremera, S. M.; Li, J.; Cao, W. Rapid Generation of Amyloid from Native Proteins in Vitro. J. Vis. Exp. 2013, 82, 50869.
   Google Scholar
• Goldschmidt, L.; Teng, P. K.; Riek, R.; Eisenberg, D. Identifying the Amylome, Proteins Capable of Forming Amyloid-like Fibrils. Proc. Nat. Acad. Sci. USA. 2010, 107(8), 3487–3492. DOI: 10.1073/pnas.0915166107.
   PubMed Web of Science ®Google Scholar
• Bobylev, A. G.; Galzitskaya, O. V.; Fadeev, R. S.; Bobyleva, L. G.; Yurshenas, D. A.; Molochkov, N. V.; Dovidchenko, N.; Selivanova, O.; Penkov, N.; Podlubnaya, Z.; et al. Smooth Muscle Titin Forms in Vitro Amyloid Aggregates. Biosci. Rep. 2016, 36(3), e00334.
   PubMedGoogle Scholar
• Yakupova, E. I.; Vikhlyantsev, I. M.; Bobyleva, L. G.; Penkov, N. V.; Timchenko, A. A.; Timchenko, M. A.; Enin, G. A.; Khutzian, S. S.; Selivanova, O. M.; Bobylev, A. G.; et al. Different Amyloid Aggregation of Smooth Muscles Titin in Vitro. J. Biomol. Struct. Dyn. 2018, 36(9), 2237–2248.
   PubMed Web of Science ®Google Scholar
• Labeit, S.; Lahmers, S.; Burkart, C.; Fong, C.; McNabb, M.; Witt, S.; Witt, C.; Labeit, D.; Granzier, H.; et al. Expression of Distinct Classes of Titin Isoforms in Striated and Smooth Muscles by Alternative Splicing, and Their Conserved Interaction with Filamins. J. Mol. Biol. 2006, 362(4), 664–681.
   PubMed Web of Science ®Google Scholar
• Yakupova, E. I.; Vikhlyantsev, I. M.; Lobanov, M. Y.; Galzitskaya, O. V.; Bobylev, A. G. Amyloid Properties of Titin. Biochemistry (Mosc). 2017, 82(13), 1675–1685. DOI: 10.1134/S0006297917130077.
   PubMed Web of Science ®Google Scholar
• Fritz, J. D.; Swartz, D. R.; Greaser, M. L. Factors Affecting Polyacryamide Gel Electrophoresis and Electroblotting of High Molecular Weight Myofibrillar Proteins. Anal. Biochem. 1989, 180, 205–210. DOI: 10.1016/0003-2697(89)90116-4.
   PubMed Web of Science ®Google Scholar
• Shen, Y.; Lue, L.; Yang, L.; Roher, A.; Kuo, Y.; Strohmeyer, R.; Goux, W. J.; Lee, V.; Johnson, G. V. W.; Webster, S. D.; et al. Complement Activation by Neurofibrillary Tangles in Alzheimer’s Disease. Neurosci. Lett. 2001, 305(3), 165–168.
   PubMed Web of Science ®Google Scholar
• Saad, S.; Cereghetti, G.; Feng, Y.; Picotti, P.; Peter, M.; Dechant, R. Reversible Protein Aggregation Is a Protective Mechanism to Ensure Cell Cycle Restart after Stress. Nat. Cell Biol. 2017, 19, 1202–1213. DOI: 10.1038/ncb3600.
   PubMed Web of Science ®Google Scholar
• Alberti, S.; Mateju, D.; Mediani, L.; Carra, S. Granulostasis: Protein Quality Control of RNP Granules. Front Mol. Neurosci. 2017, 10, 84. DOI: 10.3389/fnmol.2017.00084.
   PubMed Web of Science ®Google Scholar
• Rivas-Pardo, J. A.; Eckels, E. C.; Popa, I.; Kosuri, P.; Linke, W. A.; Fernández, J. M. Work Done by Titin Protein Folding Assists Muscle Contraction. Cell Rep. 2016, 14(6), 1339–1347. DOI: 10.1016/j.celrep.2016.01.025.
   PubMed Web of Science ®Google Scholar