Diversity of amyloid beta peptide actions

References

Alves da Costa, C., Sunyach, C., Pardossi-Piquard, R., Sévalle, J., Vincent, B., Boyer, N., Kawarai, T., Girardot, N., George-Hyslop, P.St., and Checler, F. (2006). Presenilin-dependent gamma-secretase mediated control of p53-associated cell death in Alzheimer’s disease. J. Neurosci. 26: 6377–6385, https://doi.org/10.1523/jneurosci.0651-06.2006.Suche in Google Scholar PubMed PubMed Central

Antonyan, A.A., Sharoyan, S.G., Harutyunyan, H.A., and Mardanyan, S.S. (2009). Influence of aluminum toxicosis on the activity of adenosine deaminase and dipeptidyl peptidases II and IV. Neurochem. J. 3: 118–121, https://doi.org/10.1134/s181971240902007x.Suche in Google Scholar

Antonyan, A., Sharoyan, S., Harutyunyan, H., Barboni, L., Lupidi, G., and Mardanyan, S. (2016). Protection of hippocampal and islet β cells in vitro by emodin from leaves of Rumex confertus. Int. J. Pharmacogn. 3: 437–444.Suche in Google Scholar

Antonyan, A., Schlenzig, D., Schilling, S., Naumann, M., Sharoyan, S., Mardanyan, S., and Demuth, H.-U. (2018). Concerted action of dipeptidyl peptidase IV and glutaminylcyclase results in formation of pyroglutamate-modified amyloid peptides in vitro. Neurochem. Int. 113: 112–119, https://doi.org/10.1016/j.neuint.2017.12.001.Suche in Google Scholar PubMed

Armstrong, R.A. (2011). The pathogenesis of Alzheimer’s disease: a reevaluation of the “amyloid cascade hypothesis”. Int. J. Alzheimer’s Dis. 2011: 630865, https://doi.org/10.4061/2011/630865.Suche in Google Scholar PubMed PubMed Central

Atwood, C.S., Bishop, G.M., Perry, G., and Smith, M.A. (2002). Amyloid-beta: a vascular sealant that protects against hemorrhage? J. Neurosci. Res. 70: 356, https://doi.org/10.1002/jnr.10388.Suche in Google Scholar PubMed

Atwood, C.S., Bowen, R.L., Smith, M.A., and Perry, G. (2003). Cerebrovascular requirement for sealant, anti-coagulant and remodeling molecules that allow for the maintenance of vascular integrity and blood supply. Brain Res. Rev. 43: 164–178, https://doi.org/10.1016/s0165-0173(03)00206-6.Suche in Google Scholar PubMed

Bader, A.S., Gnädig, M.U., Fricke, M., Büschgens, L., Berger, L.J., Klafki, H.W., Meyer, T., Jahn, O., Weggen, S., and Wirths, O. (2023). Brain region-specific differences in amyloid-β plaque composition in 5XFAD mice. Life 13: 1053, https://doi.org/10.3390/life13041053.Suche in Google Scholar PubMed PubMed Central

Bayer, T.A. (2022). Pyroglutamate Aβ cascade as drug target in Alzheimer’s disease. Mol. Psychiatry 27: 880–1885, https://doi.org/10.1038/s41380-021-01409-2.Suche in Google Scholar PubMed PubMed Central

Bernabeu-Zornoza, A., Coronel, R., Palmer, C., Martín, A., López-Alonso, V., and Liste, I. (2022). Neurogenesis is increased in human neural stem cells by Aβ40 peptide. Int. J. Mol. Sci. 23: 5820, https://doi.org/10.3390/ijms23105820.Suche in Google Scholar PubMed PubMed Central

Bernstein, H.G., Schön, E., Ansorge, S., Röse, I., and Dorn, A. (1987). Immunolocalization of dipeptidyl aminopeptidase (dap iv) in the developing human brain. Int. J. Dev. Neurosci. 5: 237–242, https://doi.org/10.1016/0736-5748(87)90034-7.Suche in Google Scholar PubMed

Bernstein, H.-G., Dobrowolny, H., Keilhoff, G., and Steiner, J. (2018). Dipeptidyl peptidase IV, which probably plays important roles in Alzheimer disease (AD) pathology, is upregulated in AD brain neurons and associates with amyloid plaques. Neurochem. Int. 114: 55–57, https://doi.org/10.1016/j.neuint.2018.01.005.Suche in Google Scholar PubMed

Bernstein, H.-G., Keilhoff, G., Dobrowolny, H., and Steiner, J. (2022). The many facets of CD26/dipeptidyl peptidase 4 and its inhibitors in disorders of the CNS – a critical overview. Rev. Neurosci. 34: 1–24, https://doi.org/10.1515/revneuro-2022-0026.Suche in Google Scholar PubMed

Berntsson, E., Vosough, F., Svantesson, T., Pansieri, J., Iashchishyn, I.A., Ostojić, L., Dong, X., Paul, S., Jarvet, J., Roos, P.M., et al.. (2023). Residue-specific binding of Ni(II) ions influences the structure and aggregation of amyloid beta (Aβ) peptides. Sci. Rep. 13: 3341, https://doi.org/10.1038/s41598-023-29901-5.Suche in Google Scholar PubMed PubMed Central

Biron, K.E., Dickstein, D.L., Gopaul, R., and Jefferies, W.A. (2011). Amyloid triggers extensive cerebral angiogenesis causing blood brain barrier permeability and hypervascularity in Alzheimer’s disease. PLoS One 6: e23789, https://doi.org/10.1371/journal.pone.0023789.Suche in Google Scholar PubMed PubMed Central

Bourgade, K., Garneau, H., Giroux, G., Le Page, A.Y., Bocti, C., Dupuis, G., Frost, E.H., and Fülöp, T.Jr. (2015). β-Amyloid peptides display protective activity against the human Alzheimer’s disease-associated herpes simplex virus-1. Biogerontology 16: 85–98, https://doi.org/10.1007/s10522-014-9538-8.Suche in Google Scholar PubMed

Brothers, H.M., Gosztyla, M.L., and Robinson, S.R. (2018). The physiological roles of amyloid-β peptide hint at new ways to treat Alzheimer’s disease. Front Aging Neurosci 10: 118, https://doi.org/10.3389/fnagi.2018.00118.Suche in Google Scholar PubMed PubMed Central

Busek, P., Stremenova, J., Sromova, L., Hilser, M., Balaziova, E., Kosek, D., Trylcova, J., Strnad, H., Krepela, E., and Sedo, A. (2012). Dipeptidyl peptidase-IV inhibits glioma cell growth independent of its enzymatic activity. Int. J. Biochem. Cell Biol. 44: 738–747, https://doi.org/10.1016/j.biocel.2012.01.011.Suche in Google Scholar PubMed

Cai, W., Li, L., Sang, S., Pan, X., and Zhong, C. (2023). Physiological roles of β-amyloid in regulating synaptic function: implications for AD pathophysiology. Neurosci. Bull. 39: 1289–1308, https://doi.org/10.1007/s12264-022-00985-9.Suche in Google Scholar PubMed PubMed Central

Calderaro, A., Patanè, G.T., Tellone, E., Barreca, D., Ficarra, S., Misiti, F., and Laganà, G. (2022). The neuroprotective potentiality of flavonoids on Alzheimer’s disease. Int. J. Mol. Sci. 23: 14835, https://doi.org/10.3390/ijms232314835.Suche in Google Scholar PubMed PubMed Central

Carrillo-Mora, P., Luna, R., and Colín-Barenque, L. (2014). Amyloid beta: multiple mechanisms of toxicity and only some protective effects? Oxidat. Med. Cell Longev. 2014: 795375, https://doi.org/10.1155/2014/795375.Suche in Google Scholar PubMed PubMed Central

Coronel, R., Bernabeu-Zornoza, A., Palmer, C., González-Sastre, R., Rosca, A., Mateos-Martínez, P., López-Alonso, V., and Liste, I. (2023). Amyloid precursor protein (APP) regulates gliogenesis and neurogenesis of human neural stem cells by several signaling pathways. Int. J. Mol. Sci. 24: 12964, https://doi.org/10.3390/ijms241612964.Suche in Google Scholar PubMed PubMed Central

Cummings, J., Aisen, P., Apostolova, L.G., Atri, A., Salloway, S., and Weiner, M. (2021). Aducanumab: appropriate use recommendations. J. Prev. Alzheimers Dis. 8: 398–410.Suche in Google Scholar

Cummings, J., Rabinovici, G.D., Atri, A., Aisen, P., Apostolova, L.G., Hendrix, S., Sabbagh, M., Selkoe, D., Weiner, M., and Salloway, S., and Alzheimer’s Disease and Related Disorders Therapeutics Working Group (2022). Aducanumab: appropriate use recommendations update. J. Prev. Alzheimers Dis. 9: 221–230, https://doi.org/10.14283/jpad.2022.34.Suche in Google Scholar PubMed PubMed Central

Cynis, H., Scheel, E., Saido, T.C., Schilling, S., and Demuth, H.U. (2008). Amyloidogenic processing of amyloid precursor protein: evidence of a pivotal role of glutaminyl cyclase in generation of pyroglutamate-modified amyloid-β. Biochemistry 47: 7405–7413, https://doi.org/10.1021/bi800250p.Suche in Google Scholar PubMed

D’Amico, M., Di Filippo, C., Marfella, R., Abbatecola, A.M., Ferraraccio, F., Rossi, F., and Paolisso, G. (2010). Long-term inhibition of dipeptidyl peptidase-4 in Alzheimer’s prone mice. Exp. Gerontol. 45: 202–207, https://doi.org/10.1016/j.exger.2009.12.004.Suche in Google Scholar PubMed

Dammers, C., Gremer, L., Reiß, K., Klein, A.N., Neudecker, P., Hartmann, R., Sun, N., Demuth, H.-U., Schwarten, M., and Willbold, D. (2015). Structural analysis and aggregation propensity of pyroglutamate Aβ(3-40) in aqueous trifluoroethanol. PLoS One 10: e0143647, https://doi.org/10.1371/journal.pone.0143647.Suche in Google Scholar PubMed PubMed Central

de Souza, I.D. and Queiroz, M.E.C. (2023). Advances in sample preparation and HPLC-MS/MS methods for determining amyloid-β peptide in biological samples: a review. Anal. Bioanal. Chem. 415: 4003–4021, https://doi.org/10.1007/s00216-023-04631-9.Suche in Google Scholar PubMed

Del Carmen, S.M., Laura, G.V., Leonardo, O.L., Bernabé, R.G., and Antonio, M.M. (2020). Aβ40 oligomers promote survival and early neuronal differentiation of dentate gyrus-isolated precursor cells through activation of the Akt signaling pathway. Neurotox Res. 38: 611–625, https://doi.org/10.1007/s12640-020-00253-6.Suche in Google Scholar PubMed

Eimer, W.A., Vijaya Kumar, D.K., Navalpur Shanmugam, N.K., Rodriguez, A.S., Mitchell, T., Washicosky, K.J., György, B., Breakefield, X.O., Tanzi, R.E., and Moir, R.D. (2018). Alzheimer’s disease-associated β-amyloid is rapidly seeded by herpes-viridae to protect against brain infection. Neuron 99: 56–63.e3, https://doi.org/10.1016/j.neuron.2018.06.030.Suche in Google Scholar PubMed PubMed Central

Fagiani, F., Lanni, C., Marco, R., Alessia, P., and Stefano, G. (2019). Amyloid-β and synaptic vesicle dynamics: a cacophonic orchestra. J. Alzheimer’s Dis. 72: 1–14, https://doi.org/10.3233/jad-190771.Suche in Google Scholar PubMed

Fisher, R.A., Miners, J.S., and Love, S. (2022). Pathological changes within the cerebral vasculature in Alzheimer’s disease: new perspectives. Brain Pathol 32: e13061, https://doi.org/10.1111/bpa.13061.Suche in Google Scholar PubMed PubMed Central

Galanis, C., Fellenz, M., Becker, D., Bold, C., Lichtenthaler, S.F., Müller, U.C., Deller, T., and Vlachos, A. (2021). Amyloid-beta mediates homeostatic synaptic plasticity. J. Neurosci. 41: 5157–5172, https://doi.org/10.1523/jneurosci.1820-20.2021.Suche in Google Scholar PubMed PubMed Central

Grant, J.L., Ghosn, E.E., Axtell, R.C., Herges, K., Kuipers, H.F., Woodling, N.S., Andreasson, K., Herzenberg, L.A., Herzenberg, L.A., and Steinman, L. (2012). Reversal of paralysis and reduced inflammation from peripheral administration of β-amyloid in TH1 and TH17 versions of experimental autoimmune encephalomyelitis. Sci. Transl. Med. 4: 145ra105, https://doi.org/10.1126/scitranslmed.3004145.Suche in Google Scholar PubMed PubMed Central

Hartlage-Rübsamen, M., Morawski, M., Waniek, A., Jäger, C., Zeitschel, U., Koch, B., Cynis, H., Schilling, S., Schliebs, R., Demuth, H.U., et al.. (2011). Glutaminyl cyclase contributes to the formation of focal and diffuse pyroglutamate (pGlu)-Aβ deposits in hippocampus via distinct cellular mechanisms. Acta Neuropathol. 121: 705–719, https://doi.org/10.1007/s00401-011-0806-2.Suche in Google Scholar PubMed PubMed Central

Harutyunyan, H., Sharoyan, S., Antonyan, A., and Mardanyan, S. (2017a). Herb preparations improve the viability of hippocampal cells suppressed by amyloid beta (1-42) peptide. World J. Pharm. Sci. 5: 207–212.Suche in Google Scholar

Harutyunyan, H., Sharoyan, S., Antonyan, A., and Mardanyan, S. (2017b). Herbal preparations prevent Aβ peptides induced hippocampal cell damage. Intern. J. Herb Med. 5: 92–105.Suche in Google Scholar

Hoffmann, T., Meyer, A., Heiser, U., Kurat, S., Böhme, L., Kleinschmidt, M., Bühring, K.-U., Hutter-Paier, B., Farcher, M., Demuth, H.-U., et al.. (2017). Glutaminyl cyclase inhibitor PQ912 improves cognition in mouse models of Alzheimer’s disease – studies on relation to effective target occupancy. J. Pharmacol. Exp. Ther. 362: 119–130, https://doi.org/10.1124/jpet.117.240614.Suche in Google Scholar PubMed

Hovnanyan, K., Sharoyan, S., Antonyan, A., and Mardanyan, S. (2017). Influence of extract and phenol glycosides from rose petals on the fibrils of amyloid peptide Aβ(1-42). Study by transmission electron microscopy. Proc. YSU Chem. Biol. 3: 203–208.10.4236/oalib.1103343Suche in Google Scholar

Hu, Z.-W., Cruceta, L., Zhang, V., Sun, Y., and Qiang, W. (2021). Cross-seeded fibrillation induced by pyroglutamate-3 and truncated Aβ40 variants leads to Aβ40 structural polymorphism modulation and elevated toxicity. ACS Chem. Neurosci. 19: 3625–3637, https://doi.org/10.1021/acschemneuro.1c00341.Suche in Google Scholar PubMed

Huang, J., Huang, N., Mao, Q., Shi, J., and Qiu, Y. (2023). Natural bioactive compounds in Alzheimer’s disease: from the perspective of type 3 diabetes mellitus. Front. Aging Neurosci. 15: 1130253, https://doi.org/10.3389/fnagi.2023.1130253.Suche in Google Scholar PubMed PubMed Central

Huang, L.-K., Kuan, Y.-C., Lin, H.-W., and Hu, C.-J. (2023). Clinical trials of new drugs for Alzheimer disease: a 2020–2023 update. J. Biomed. Sci. 30: 83, https://doi.org/10.1186/s12929-023-00976-6.Suche in Google Scholar PubMed PubMed Central

Ikegawa, M., Kakuda, N., Miyasaka, T., Toyama, Y., Nirasawa, T., Minta, K., and Hanrieder, J. (2023). Mass spectrometry imaging in Alzheimer’s disease. Brain Connect. 13: 319–333, https://doi.org/10.1089/brain.2022.0057.Suche in Google Scholar PubMed PubMed Central

Inyushin, M., Zayas-Santiago, A., Rojas, L., and Kucheryavykh, L. (2020). On the role of platelet-generated amyloid beta peptides in certain amyloidosis health complications. Front. Immunol. 11: 571083, https://doi.org/10.3389/fimmu.2020.571083.Suche in Google Scholar PubMed PubMed Central

Jazvinscak Jembrek, M., Slade, N., Hof, P.R., and Simic, G. (2018). The interactions of p53 with tau and Aβ as potential therapeutic targets for Alzheimer’s disease. Prog. Neurobiol. 168: 104–127, https://doi.org/10.1016/j.pneurobio.2018.05.001.Suche in Google Scholar PubMed

Jefferies, W.A., Price, K.A., Biron, K.E., Fenninger, F., Pfeifer, C.G., and Dickstein, D.L. (2013). Adjusting the compass: new insights into the role of angiogenesis in Alzheimer’s disease. Alzheimers Res. Ther. 5: 146–148, https://doi.org/10.1186/alzrt230.Suche in Google Scholar PubMed PubMed Central

Jeong, H., Shin, H., Hong, S., and Kim, Y.S. (2022). Physiological roles of monomeric amyloid-β and implications for Alzheimer’s disease. Therapeutics Exp. Neurobiol. 31: 65–88, https://doi.org/10.5607/en22004.Suche in Google Scholar PubMed PubMed Central

Kagan, B.L., Jang, H., Capone, R., Teran Arce, F., Ramachandran, S., Lal, R., and Nussinov, R. (2012). Antimicrobial properties of amyloid peptides. Mol. Pharm. 9: 708–717, https://doi.org/10.1021/mp200419b.Suche in Google Scholar PubMed PubMed Central

Karisetty, B.C., Bhatnagar, A., Armour, E.M., Beaver, M., Zhang, H., and Elefant, F. (2020). Amyloid-b peptide impact on synaptic function and neuroepigenetic gene control reveal new therapeutic strategies for AD. Front. Mol. Neurosci. 13: 577622, https://doi.org/10.3389/fnmol.2020.577622.Suche in Google Scholar PubMed PubMed Central

Kornelius, E., Lin, C.L., Chang, H.H., Li, H.H., Huang, W.N., Yang, Y.S., Lu, Y.L., Peng, C.H., and Huang, C.N. (2015). DPP-4 inhibitor linagliptin attenuates Aβ-induced cytotoxicity through activation of AMPK in neuronal cells. CNS Neurosci. Ther. 21: 549–557, https://doi.org/10.1111/cns.12404.Suche in Google Scholar PubMed PubMed Central

Korovesis, D., Rubio-Tomás, T., and Tavernarakis, N. (2023). Oxidative stress in age-related neurodegenerative diseases: an overview of recent tools and findings. Antioxidants 12: 131, https://doi.org/10.3390/antiox12010131.Suche in Google Scholar PubMed PubMed Central

Kosaraju, J., Murthy, V., Khatwal, R.B., Dubala, A., Chinni, S., Muthureddi Nataraj, S.K., and Basavan, D. (2013). Vildagliptin: an anti-diabetes agent ameliorates cognitive deficits and pathology observed in streptozotocin-induced Alzheimer´s disease. J. Pharm. Pharmacol. 65: 1773–1784, https://doi.org/10.1111/jphp.12148.Suche in Google Scholar PubMed

Kumar, D.K., Choi, S.H., Washicosky, K.J., Eimer, W.A., Tucker, S., Ghofrani, J., Lefkowitz, A., McColl, G., Goldstein, L.E., Tanzi, R.E., et al.. (2017). Amyloid-β peptide protects against microbial infection in mouse and worm models of Alzheimer’s disease. Sci. Transl. Med. 8: 340ra72, https://doi.org/10.1126/scitranslmed.aaf1059.Suche in Google Scholar PubMed PubMed Central

Kumar, S., Gautam, V., Singh, B.P., and Kumar, D. (2023). Editorial: investigating the impact of bioactive metabolites and extracts in human health and disease. Front. Mol. Biosci. 10: 1244316, https://doi.org/10.3389/fmolb.2023.1244316.Suche in Google Scholar PubMed PubMed Central

Kummer, M.P. and Heneka, M.T. (2014). Truncated and modified amyloid-beta species. Alzheimers Res. Ther. 6: 28, https://doi.org/10.1186/alzrt258.Suche in Google Scholar PubMed PubMed Central

Liao, M.Q., Tzeng, Y.J., Chang, L.Y.X., Huang, H.B., Lin, T.H., Chyan, C.L., and Chen, Y.C. (2007). The correlation between neurotoxicity, aggregative ability and secondary structure studied by sequence truncated Ab peptides. FEBS Lett. 581: 1161–1165, https://doi.org/10.1016/j.febslet.2007.02.026.Suche in Google Scholar PubMed

Liu, K., Solano, I., Mann, D., Lemere, C., Mercken, M., Trojanowski, J.Q., and Lee, V.M.Y. (2006). Characterization of Aß11-40/42 peptide deposition in Alzheimer’s disease and young Down’s syndrome brains: implication of N-terminally truncated Aß species in the pathogenesis of Alzheimer’s disease. Acta Neuropathol 112: 163–174, https://doi.org/10.1007/s00401-006-0077-5.Suche in Google Scholar PubMed

Liu, Y., Shi, Y., and Wang, P. (2023). Functions of glutaminyl cyclase and its isoform in diseases. Visualized Cancer Med. 4: 1, https://doi.org/10.1051/vcm/2022008.Suche in Google Scholar

Loeffler, D.A. (2023). Experimental approaches for altering the expression of Abeta-degrading enzymes. J. Neurochem. 164: 725–763, https://doi.org/10.1111/jnc.15762.Suche in Google Scholar PubMed

Lukiw, W.J., Cui, J.G., Yuan, L.Y., Bhattacharjee, P.S., Corkern, M., Clement, C., Kammerman, E.M., Ball, M.J., Zhao, Y., Sullivan, P.M., et al.. (2010). Acyclovir or Aβ42 peptides attenuate HSV1-induced miRNA-146a levels in human primary brain cells. Neuroreport 21: 922–927, https://doi.org/10.1097/wnr.0b013e32833da51a.Suche in Google Scholar

Maitra, S., Sornjai, W., Smith, D., and Vincent, B. (2021). Phenanthroline impairs βAPP processing and expression, increases p53 protein levels and induces cell cycle arrest in human neuroblastoma cells. Brain Res. Bull. 170: 29–38, https://doi.org/10.1016/j.brainresbull.2021.02.001.Suche in Google Scholar PubMed

Masi, M., Biundo, F., Fiou, A., Racchi, M., Pascale, A., and Buoso, E. (2023). The labyrinthine landscape of APP processing: state of the art and possible novel soluble APP-related molecular players in traumatic brain injury and neurodegeneration. Int. J. Mol. Sci. 24: 6639, https://doi.org/10.3390/ijms24076639.Suche in Google Scholar PubMed PubMed Central

Matos, J.O., Goldblatt, G., Jeon, J., Chen, B., and Tatulian, S.A. (2014). Pyroglutamylated amyloid-β peptide reverses cross β-sheets by a prion-like mechanism. J. Phys. Chem. B 118: 5637–5643, https://doi.org/10.1021/jp412743s.Suche in Google Scholar PubMed PubMed Central

Moir, R.D., Lathe, R., and Tanzi, R.E. (2018). The antimicrobial protection hypothesis of Alzheimer’s disease. Alzheimers Dement. 14: 1602–1614, https://doi.org/10.1016/j.jalz.2018.06.3040.Suche in Google Scholar PubMed

Mondello, S., Buki, A., Barzo, P., Randall, J., Provuncher, G., Hanlon, D., Wilson, D., Kobeissy, F., and Jeromin, A. (2014). CSF and plasma amyloid-β temporal profiles and relationships with neurological status and mortality after severe traumatic brain injury. Sci. Rep. 4: 6446, https://doi.org/10.1038/srep06446.Suche in Google Scholar PubMed PubMed Central

Morató, X., Pytel, V., Jofresa, S., Ruiz, A., and Boada, M. (2022). Symptomatic and disease-modifying therapy pipeline for Alzheimer’s disease: towards a personalized polypharmacology patient-centered approach. Int. J. Mol. Sci. 23: 9305, https://doi.org/10.3390/ijms23169305.Suche in Google Scholar PubMed PubMed Central

Morawski, M., Schilling, S., Kreuzberger, M., Waniek, A., Jäger, C., Koch, B., Cynis, H., Kehlen, A., Arendt, T., Hartlage-Rübsamen, M., et al.. (2014). Glutaminyl cyclase in human cortex: correlation with (pGlu)-amyloid-β load and cognitive decline in Alzheimer’s disease. J. Alzheimers Dis. 39: 385–400, https://doi.org/10.3233/jad-131535.Suche in Google Scholar

Mori, H., Takio, K., Ogawara, M., and Selkoe, D.J. (1992). Mass spectrometry of purified amyloid beta protein in Alzheimer’s disease. J. Biol. Chem. 267: 17082–17086, https://doi.org/10.1016/s0021-9258(18)41896-0.Suche in Google Scholar

Morley, J.E., Farr, S.A., Nguyen, A.D., and Xu, F. (2019). What is the physiological function of amyloid-beta protein? J. Nutr. Health Aging 23: 225–226, https://doi.org/10.1007/s12603-019-1162-5.Suche in Google Scholar PubMed

Movsisyan, N.M., Sharoyan, S.G., Antonyan, A.A., and Mardanyan, S.S. (2013). Breakdown of some neuronal peptides with dipeptidyl peptidase IV. Proc. YSU Chem. Biol. 1: 36–39.Suche in Google Scholar

Murariu, M., Habasescu, L., Ciobanu, C.-I., Gradinaru, R.V., Pui, A., Drochioiu, G., and Mangalagiu, I. (2019). Interaction of amyloid Aβ(9–16) peptide fragment with metal ions: CD, FT-IR, and fluorescence spectroscopic studies. Int. J. Peptide Res. Ther. 25: 897–909, https://doi.org/10.1007/s10989-018-9738-1.Suche in Google Scholar

Nussbaum, J.M., Schilling, S., Cynis, H., Silva, A., Swanson, E., Wangsanut, T., Tayler, K., Wiltgen, B., Hatami, A., Rönicke, R., et al.. (2012). Prion-like behavior and tau-dependent cytotoxicity of pyroglutamylated β-amyloid. Nature 485: 651–655, https://doi.org/10.1038/nature11060.Suche in Google Scholar PubMed PubMed Central

Ospina-Romero, M., Glymour, M.M., Hayes-Larson, E., Mayeda, E.R., Graff, R.E., Brenowitz, W.D., Ackley, S.F., Witte, J.S., and Kobayashi, L.C. (2020). Association between Alzheimer disease and cancer with evaluation of study biases: a systematic review and meta-analysis. JAMA Netw. Open 3: e2025515, https://doi.org/10.1001/jamanetworkopen.2020.25515.Suche in Google Scholar PubMed PubMed Central

Pajoohesh-Ganji, A., Burns, M.P., Pal-Ghosh, S., Tadvalkar, G., Hokenbury, N.G., Stepp, M.A., and Faden, A.I. (2014). Inhibition of amyloid precursor protein secretases reduces recovery after spinal cord injury. Brain Res. 1560: 73–82, https://doi.org/10.1016/j.brainres.2014.02.049.Suche in Google Scholar PubMed PubMed Central

Paris, D., Ganey, N., Banasiak, M., Laporte, V., Patel, N., Mullan, M., Murphy, S.F., Yee, G.T., Bachmeier, C., Ganey, C., et al.. (2010). Impaired orthotopic glioma growth and vascularization in transgenic mouse models of Alzheimer’s disease. J. Neurosci. 30: 11251–11258, https://doi.org/10.1523/jneurosci.2586-10.2010.Suche in Google Scholar PubMed PubMed Central

Perez-Garmendia, R. and Gevorkian, G. (2013). Pyroglutamate-Modified amyloid beta peptides: emerging targets for Alzheimer’s disease immunotherapy. Curr. Neuropharmacol. 11: 491–498, https://doi.org/10.2174/1570159x11311050004.Suche in Google Scholar

Perez-Garmendia, R., Hernandez-Zimbron, L.F., Morales, M.A., Luna-Muñoz, J., Mena, R., Nava-Catorce, M., Acero, G., Vasilevko, V., Viramontes-Pintos, A., Cribbs, D.H., et al.. (2014). Identification of N-terminally truncated pyroglutamate amyloid-β in cholesterol-enriched diet-fed rabbit and AD brain. J. Alzheimer’s Dis. 39: 441–455, https://doi.org/10.3233/jad-130590.Suche in Google Scholar PubMed

Piccini, A., Russo, C., Gliozzi, A., Relini, A., Vitali, A., Borghi, R., Giliberto, L., Armirotti, A., D’Arrigo, C., Bachi, A., et al.. (2005). β-Amyloid is different in normal aging and in Alzheimer disease. J. Biol. Chem. 280: 34186–34192, https://doi.org/10.1074/jbc.m501694200.Suche in Google Scholar PubMed

Pluta, R., Miziak, B., and Czuczwar, S.J. (2023). Post-ischemic permeability of the blood–brain barrier to amyloid and platelets as a factor in the maturation of Alzheimer’s disease-type brain neurodegeneration. Int. J. Mol. Sci. 24: 10739, https://doi.org/10.3390/ijms241310739.Suche in Google Scholar PubMed PubMed Central

Portelius, E., Bogdanovic, N., Gustavsson, M.K., Volkmann, I., Brinkmalm, G., Zetterberg, H., Winblad, B., and Blennow, K. (2010). Mass spectrometric characterization of brain amyloid beta isoform signatures in familial and sporadic Alzheimer’s disease. Acta Neuropathol. 120: 185–193, https://doi.org/10.1007/s00401-010-0690-1.Suche in Google Scholar PubMed PubMed Central

Ristori, E., Donnini, S., and Ziche, M. (2020). New insights into blood-brain barrier aintenance: the homeostatic role of β-amyloid precursor protein in cerebral vasculature. Front. Physiol. 11: 1056, https://doi.org/10.3389/fphys.2020.01056.Suche in Google Scholar PubMed PubMed Central

Robinson, S.R. and Bishop, G.M. (2002). Abeta as a bioflocculant: implications for the amyloid hypothesis of Alzheimer’s disease. Neurobiol. Aging 23: 1051–1072, https://doi.org/10.1016/s0197-4580(01)00342-6.Suche in Google Scholar PubMed

Röhnert, P., Schmidt, W., Emmerlich, P., Goihl, A., Wrenger, S., Bank, U., Nordhoff, K., Täger, M., Ansorge, S., Reinhold, D., et al.. (2012). Dipeptidyl peptidase IV, aminopeptidase N and DPIV/APN-like proteases in cerebral ischemia. J. Neuroinflamm. 9: 44, https://doi.org/10.1186/1742-2094-9-44.Suche in Google Scholar PubMed PubMed Central

Scheltens, P., Hallikainen, M., Grimmer, T., Duning, T., Gouw, A.A., Teunissen, C.E., Wink, A.M., Maruff, P., Harrison, J., Van Baal, C.M., et al.. (2018). Safety, tolerability and efficacy of the glutaminyl cyclase inhibitor PQ912 in Alzheimer’s disease: results of a randomized, double-blind, placebo-controlled phase 2a study. Alzheimer’s Res. Ther. 10: 107, https://doi.org/10.1186/s13195-018-0431-6.Suche in Google Scholar PubMed PubMed Central

Schilling, S., Hoffman, T., Manhart, S., Hoffman, and Demuth, H.-U. (2004). Glutaminyl cyclases unfold glutamyl cyclase activity under mild acid conditions. FEBS Lett. 563: 191–196, https://doi.org/10.1016/s0014-5793(04)00300-x.Suche in Google Scholar PubMed

Schreiner, T.G., Schreiner, O.D., Adam, M., and Popescu, B.O. (2023). The roles of the amyloid β monomers in physiological and pathological conditions. Biomedicines 11: 1411, https://doi.org/10.3390/biomedicines11051411.Suche in Google Scholar PubMed PubMed Central

Sehar, U., Rawat, P., Reddy, A.P., Kopel, J., and Reddy, P.H. (2022). Amyloid beta in aging and Alzheimer’s disease. Int. J. Mol. Sci. 23: 12924, https://doi.org/10.3390/ijms232112924.Suche in Google Scholar PubMed PubMed Central

Sharoyan, S., Antonyan, A., Mardanyan, S., Harutyunyan, H., Movsisyan, N., Hovnanyan, N., and Hovnanyan, K. (2013). Interaction of dipeptidyl peptidase IV with amyloid peptides. Neurochem. Int. 62: 1048–1054, https://doi.org/10.1016/j.neuint.2013.03.017.Suche in Google Scholar PubMed

Sharoyan, S., Antonyan, A., Harutyunyan, H., and Mardanyan, S. (2015). Plant preparations suppress the aggregation of amyloid beta peptides and promote their disaggregation. Proc. YSU Chem. Biol. 3: 40–46.Suche in Google Scholar

Shirotani, K., Tsubuki, S., Lee, H.J., Maruyama, K., and Saido, T.C. (2002). Generation of amyloid beta peptide with pyroglutamate at position 3 in primary cortical neurons. Neurosci. Lett. 327: 25–28, https://doi.org/10.1016/s0304-3940(02)00351-8.Suche in Google Scholar PubMed

Sinha, M., Bhowmick, P., Banerjee, A., and Chakrabarti, S. (2013). Antioxidant role of amyloid β protein in cell-free and biological systems: implication for the pathogenesis of Alzheimer disease. Free Radic. Biol. Med. 56: 184–192, https://doi.org/10.1016/j.freeradbiomed.2012.09.036.Suche in Google Scholar PubMed

Soscia, S.J., Kirby, J.E., Washicosky, K.J., Tucker, S.M., Ingelsson, M., Hyman, B., Burton, M.A., Goldstein, L.E., Duong, S., Tanzi, R.E., et al.. (2010). The Alzheimer’s disease-associated amyloid beta-protein is an antimicrobial peptide. PLoS One 5: e9505, https://doi.org/10.1371/journal.pone.0009505.Suche in Google Scholar PubMed PubMed Central

Spitzer, P., Condic, M., Herrmann, M., Oberstein, T.J., Scharin-Mehlmann, M., Gilbert, D.F., Friedrich, O., Grömer, T., Kornhuber, J., Lang, R., et al.. (2016). Amyloidogenic amyloid-β-peptide variants induce microbial agglutination and exert antimicrobial activity. Sci. Rep. 6: 32228, https://doi.org/10.1038/srep32228.Suche in Google Scholar PubMed PubMed Central

Stremenova, J., Krepela, E., Mares, V., Trim, J., Dbaly, V., Marek, J., Vanickova, Z., Lisa, V., Yea, C., and Sedo, A. (2007). Expression and enzymatic activity of dipeptidyl peptidase-IV in human astrocytic tumours are associated with tumour grade. Int. J. Oncol. 31: 785–792, https://doi.org/10.3892/ijo.31.4.785.Suche in Google Scholar

Stremenová, J., Mares, V., Lisá, V., Hilser, M., Krepela, E., Vanicková, Z., Syrucek, M., Soula, O., and Sedo, A. (2010). Expression of dipeptidyl peptidase-IV activity and/or structure homologs in human meningiomas. Int. J. Oncol. 36: 351–358, https://doi.org/10.3892/ijo_00000506.Suche in Google Scholar

Sturchio, A., Dwivedi, A.K., Malm, T., Wood, M.J.A., Cilia, R., Sharma, J.S., Hill, E.J., Schneider, L.S., Graff-Radford, N.R., Mori, H., et al.. (2022). Dominantly inherited Alzheimer consortia (DIAN) high soluble amyloid-β42 predicts normal cognition in amyloid-positive individuals with Alzheimer’s disease-causing mutations. J. Alzheimers Dis. 90: 333–348, https://doi.org/10.3233/jad-220808.Suche in Google Scholar

van Dyck, C.H., Swanson, C.J., Aisen, P., Bateman, R.J., Chen, C., Gee, M., Kanekiyo, M., Li, D., Reyderman, L., Cohen, S., et al.. (2023). Lecanemab in early Alzheimer’s disease. N. Engl. J. Med. 388: 9–21, https://doi.org/10.1056/nejmoa2212948.Suche in Google Scholar PubMed

Vijverberg, E.G.B., Axelsen, T.M., Bihlet, A.R., Henriksen, K., Weber, F., Fuchs, K., Harrison, J.E., Kühn-Wache, K., Alexandersen, P., Prins, N.D., et al.. (2021). Rationale and study design of a randomized, placebo-controlled, double blind phase 2b trial to evaluate efficacy, safety, and tolerability of an oral glutaminyl cyclase inhibitor varoglutamstat (PQ912) in study participants with MCI and mild AD–VIVIAD. Alzheimer’s Res. Ther. 13: 142, https://doi.org/10.1186/s13195-021-00882-9.Suche in Google Scholar PubMed PubMed Central

Vojtechova, I., Machacek, T., Kristofikova, Z., Stuchlik, A., and Petrasek, T. (2022). Infectious origin of Alzheimer’s disease: amyloid beta as a component of brain antimicrobial immunity. PLoS Pathog. 18: e1010929, https://doi.org/10.1371/journal.ppat.1010929.Suche in Google Scholar PubMed PubMed Central

Walter, S., Jumpertz, T., Hüttenrauch, M., Ogorek, I., Gerber, H., Storck, S.E., Zampar, S., Dimitrov, M., Lehmann, S., Lepka, K., et al.. (2019). The metalloprotease ADAMTS4 generates N-truncated Aβ4–x species and marks oligodendrocytes as a source of amyloidogenic peptides in Alzheimer’s disease. Acta Neuropathol. 137: 239–257, https://doi.org/10.1007/s00401-018-1929-5.Suche in Google Scholar PubMed

White, M.R., Kandel, R., Tripathi, S., Condon, D., Qi, L., Taubenberger, J., and Hartshorn, K.L. (2014). Alzheimer’s associated β-amyloid protein inhibits influenza A virus and modulates viral interactions with phagocytes. PLoS One 9: e101364, https://doi.org/10.1371/journal.pone.0101364.Suche in Google Scholar PubMed PubMed Central

White, M.R., Kandel, R., Hsieh, I.N., De Luna, X., and Hartshorn, K.L. (2018). Critical role of C-terminal residues of the Alzheimer’s associated β-amyloid protein in mediating antiviral activity and modulating viral and bacterial interactions with neutrophils. PLoS One 13: e0194001, https://doi.org/10.1371/journal.pone.0194001.Suche in Google Scholar PubMed PubMed Central

Wiatrak, B. and Balon, K. (2021). Protective activity of Aβ on cell cultures (PC12 and THP-1 after differentiation) preincubated with lipopolysaccharide (LPS). Mol. Neurobiol. 8: 1453–1464, https://doi.org/10.1007/s12035-020-02204-w.Suche in Google Scholar PubMed PubMed Central

Wirths, O., Walter, S., Kraus, I., Klafki, H.W., Stazi, M., Oberstein, T.J., Ghiso, J., Wiltfang, J., Bayer, T.A., and Weggen, S. (2017). N-truncated Aβ4–x peptides in sporadic Alzheimer’s disease cases and transgenic Alzheimer mouse models. Alzheimers Res. Ther. 9: 80, https://doi.org/10.1186/s13195-017-0309-z.Suche in Google Scholar PubMed PubMed Central

Yadollahikhales, G. and Rojas, J.C. (2023). Anti-amyloid immunotherapies for Alzheimer’s disease: a 2023 clinical update. Neurotherapeutics 20: 914–931, https://doi.org/10.1007/s13311-023-01405-0.Suche in Google Scholar PubMed PubMed Central

Zampar, S., Klafki, H.W., Sritharen, K., Bayer, T.A., Wiltfang, J., Rostagno, A., Ghiso, J., Miles, L.A., and Wirths, O. (2020). N-terminal heterogeneity of parenchymal and vascular amyloid-β deposits in Alzheimer’s disease. Neuropathol. Appl. Neurobiol. 46: 673–685, https://doi.org/10.1111/nan.12637.Suche in Google Scholar PubMed PubMed Central

Zhang, H., Li, X., Wang, X., Xu, J., Elefant, F., and Wang, J. (2023). Cellular response to β-amyloid neurotoxicity in Alzheimer’s disease and implications in new therapeutics. Anim. Models Exp. Med. 6: 3, https://doi.org/10.1002/ame2.12313.Suche in Google Scholar PubMed PubMed Central

Zhang, Y., Chen, H., Li, R., Sterling, K., and Song, W.S. (2023). Amyloid β-based therapy for Alzheimer’s disease: challenges, successes and future. Transduct. Target Ther. 8: 248, https://doi.org/10.1038/s41392-023-01484-7.Suche in Google Scholar PubMed PubMed Central

Zhao, H., Zhu, J., Cui, K., Xu, X., O’Brien, M., Wong, K.K., Kesari, S., Xia, W., and Wong, S.T. (2009). Bioluminescence imaging reveals inhibition of tumor cell proliferation by Alzheimer’s amyloid beta protein. Cancer Cell Int. 9: 15, https://doi.org/10.1186/1475-2867-9-15.Suche in Google Scholar PubMed PubMed Central

Zimbone, S., Monaco, I., Gianì, F., Pandini, G., Copani, A.G., Giuffrida, M.L., and Rizzarelli, E. (2018). Amyloid Beta monomers regulate cyclic adenosine monophosphate response element binding protein functions by activating type-1 insulin-like growth factor receptors in neuronal cells. Aging Cell 17: e12684, https://doi.org/10.1111/acel.12684.Suche in Google Scholar PubMed PubMed Central