The DOI matches its Crossref record; 32 of the 32 references it cites were found in a registry or an index.
Metalloproteinases and their tissue inhibitors in Alzheimer’s disease and other neurodegenerative disorders.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
Matrix metalloproteinases including MMP-2, MMP-3, MMP-7 and MMP-9 also cleave within the Aβ sequence.
“Matrix metalloproteinases (MMPs), including MMP-2, MMP-3, MMP-7 and MMP-9 also cleave within the Aβ sequence (Rivera et al., 2019) and these cleavages have been compared to those of membrane-type MMPs (MT-MMPs) in Figure 1.”
From Emerging Alternative Proteinases in APP Metabolism and Alzheimer’s Disease Pathogenesis: A Focus on MT1-MMP and MT5-MMP (2019) · cites this paper as Rivera et al., 2019
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
The amyloid hypothesis of Alzheimer's disease at 25 years
Selkoe, D. J., & Hardy, J. (2016) · EMBO Molecular Medicine · doi:10.15252/emmm.201606210 · Cited by 6,164
Oakley, H., Cole, S. L., Logan, S., Maus, E., Shao, P., Craft, J., Guillozet-Bongaarts, A., Ohno, M., Disterhoft, J., Van Eldik, L., et al. (2006) · The Journal of Neuroscience · doi:10.1523/jneurosci.1202-06.2006 · Cited by 3,530 · cited 1×
“By the same time, our group tested the implication of MT5-MMP in AD using a different approach; we crossed transgenic 5xFAD mice carrying familial AD mutations in human APP and Psen1 genes [112] with MT5-MMP knockout mice [113].”
MethodA metalloproteinase disintegrin that releases tumour-necrosis factor-α from cells
Black, R. A., Rauch, C. T., Kozlosky, C. J., Peschon, J. J., Slack, J. L., Wolfson, M. F., Castner, B. J., Stocking, K. L., Reddy, P., Srinivasan, S., et al. (1997) · Nature · doi:10.1038/385729a0 · Cited by 3,149
Dominy, S. S., Lynch, C., Ermini, F., Benedyk, M., Marczyk, A., Konradi, A., Nguyen, M., Haditsch, U., Raha, D., Griffin, C., et al. (2019) · Science Advances · doi:10.1126/sciadv.aau3333 · Cited by 1,966
Kumar, D. K. V., 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. (2016) · Science Translational Medicine · doi:10.1126/scitranslmed.aaf1059 · Cited by 971
TREM2 mutations implicated in neurodegeneration impair cell surface transport and phagocytosis
Kleinberger, G., Yamanishi, Y., Suárez-Calvet, M., Czirr, E., Lohmann, E., Cuyvers, E., Struyfs, H., Pettkus, N., Wenninger-Weinzierl, A., Mazaheri, F., et al. (2014) · Science Translational Medicine · doi:10.1126/scitranslmed.3009093 · Cited by 798
Picomolar Amyloid-β Positively Modulates Synaptic Plasticity and Memory in Hippocampus
Puzzo, D., Privitera, L., Leznik, E., Fà, M., Staniszewski, A., Palmeri, A., & Arancio, O. (2008) · The Journal of Neuroscience · doi:10.1523/jneurosci.2692-08.2008 · Cited by 740
Not just amyloid: physiological functions of the amyloid precursor protein family
Müller, U. C., Deller, T., & Korte, M. (2017) · Nature Reviews Neuroscience · doi:10.1038/nrn.2017.29 · Cited by 634
Jawhar, S., Trawicka, A., Jenneckens, C., Bayer, T. A., & Wirths, O. (2012) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2010.05.027 · Cited by 623
Kuhn, P., Wang, H., Dislich, B., Colombo, A., Zeitschel, U., Ellwart, J. W., Kremmer, E., Roßner, S., & Lichtenthaler, S. F. (2010) · The EMBO Journal · doi:10.1038/emboj.2010.167 · Cited by 621
Endothelial LRP1 transports amyloid-β1–42 across the blood-brain barrier
Storck, S. E., Meister, S., Nahrath, J., Meißner, J. N., Schubert, N., Di Spiezio, A., Baches, S., Vandenbroucke, R. E., Bouter, Y., Prikulis, I., et al. (2015) · Journal of Clinical Investigation · doi:10.1172/jci81108 · Cited by 477
Proteases and Proteolysis in Alzheimer Disease: A Multifactorial View on the Disease Process
De Strooper, B. (2010) · Physiological Reviews · doi:10.1152/physrev.00023.2009 · Cited by 455
Human umbilical cord plasma proteins revitalize hippocampal function in aged mice
Castellano, J. M., Mosher, K. I., Abbey, R. J., McBride, A. A., James, M. L., Berdnik, D., Shen, J. C., Zou, B., Xie, X. S., Tingle, M., et al. (2017) · Nature · doi:10.1038/nature22067 · Cited by 445
η-Secretase processing of APP inhibits neuronal activity in the hippocampus
Willem, M., Tahirovic, S., Busche, M. A., Ovsepian, S. V., Chafai, M., Kootar, S., Hornburg, D., Evans, L. D. B., Moore, S., Daria, A., et al. (2015) · Nature · doi:10.1038/nature14864 · Cited by 398
Matrix Metalloproteinase-9 Degrades Amyloid-β Fibrils in Vitro and Compact Plaques in Situ
Yan, P., Hu, X., Song, H., Yin, K., Bateman, R. J., Cirrito, J. R., Xiao, Q., Hsu, F. F., Turk, J. W., Xu, J., et al. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m602440200 · Cited by 380
Backstrom, J. R., Lim, G. P., Cullen, M. J., & Tökés, Z. A. (1996) · The Journal of Neuroscience · doi:10.1523/jneurosci.16-24-07910.1996 · Cited by 331
White, A. R., Du, T., Laughton, K. M., Volitakis, I., Sharples, R. A., Xilinas, M. E., Hoke, D. E., Holsinger, R. M. D., Evin, G., Cherny, R. A., et al. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m602487200 · Cited by 284
Kim, J., Castellano, J. M., Jiang, H., Basak, J. M., Parsadanian, M., Pham, V., Mason, S. M., Paul, S. M., & Holtzman, D. M. (2009) · Neuron · doi:10.1016/j.neuron.2009.11.013 · Cited by 274
Astrocytic LRP1 Mediates Brain Aβ Clearance and Impacts Amyloid Deposition
Liu, C.-C., Hu, J., Zhao, N., Wang, J., Wang, N., Cirrito, J. R., Kanekiyo, T., Holtzman, D. M., & Bu, G. (2017) · The Journal of Neuroscience · doi:10.1523/jneurosci.3442-16.2017 · Cited by 267
The role of TREM2 in Alzheimer's disease and other neurodegenerative disorders
Carmona, S., Zahs, K., Wu, E., Dakin, K., Bras, J., & Guerreiro, R. (2018) · The Lancet Neurology · doi:10.1016/s1474-4422(18)30232-1 · Cited by 244 · cited 2×
“Of note, some authors have reported association between TREM2 variants and increased risk of PD, although the data are not conclusive for the moment [134].”
BackgroundThornton, P., Sevalle, J., Deery, M. J., Fraser, G., Zhou, Y., Ståhl, S., Franssen, E. H., Dodd, R. B., Qamar, S., Gomez Perez‐Nievas, B., et al. (2017) · EMBO Molecular Medicine · doi:10.15252/emmm.201707673 · Cited by 200
Gene expression correlates of neurofibrillary tangles in Alzheimer's disease
Dunckley, T., Beach, T. G., Ramsey, K. E., Grover, A., Mastroeni, D., Walker, D. G., LaFleur, B. J., Coon, K. D., Brown, K. M., Caselli, R., et al. (2006) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2005.08.013 · Cited by 177
Lewy pathology is not the first sign of degeneration in vulnerable neurons in Parkinson disease
Milber, J. M., Noorigian, J. V., Morley, J. F., Petrovitch, H., White, L., Ross, G. W., & Duda, J. E. (2012) · Neurology · doi:10.1212/wnl.0b013e318278fe32 · Cited by 163
Castellano, J. M., Deane, R., Gottesdiener, A. J., Verghese, P. B., Stewart, F. R., West, T., Paoletti, A. C., Kasper, T. R., DeMattos, R. B., Zlokovic, B. V., et al. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1206446109 · Cited by 154
Selective distribution of matrix metalloproteinase-3 (MMP-3) in Alzheimer’s disease brain
Yoshiyama, Y., Asahina, M., & Hattori, T. (2000) · Acta Neuropathologica · doi:10.1007/pl00007428 · Cited by 128
Role of Matrix Metalloproteinase 3-mediated α-Synuclein Cleavage in Dopaminergic Cell Death
Choi, D.-H., Kim, Y.-J., Kim, Y.-G., Joh, T. H., Beal, M. F., & Kim, Y.-S. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.222430 · Cited by 123
Girard, S. D., Jacquet, M., Baranger, K., Migliorati, M., Escoffier, G., Bernard, A., Khrestchatisky, M., Féron, F., Rivera, S., Roman, F. S., et al. (2014) · Hippocampus · doi:10.1002/hipo.22267 · Cited by 119
Self-citationGirard, S. D., Baranger, K., Gauthier, C., Jacquet, M., Bernard, A., Escoffier, G., Marchetti, E., Khrestchatisky, M., Rivera, S., & Roman, F. S. (2013) · Journal of Alzheimer s Disease · doi:10.3233/jad-2012-120982 · Cited by 107
Self-citationFang, F., Yu, Q., Arancio, O., Chen, D., Gore, S. S., Yan, S. S., & Yan, S. F. (2018) · Human Molecular Genetics · doi:10.1093/hmg/ddy017 · Cited by 103
Brain matrix metalloproteinase 1 levels are elevated in Alzheimer's disease
Leake, A., Morris, C. M., & Whateley, J. (2000) · Neuroscience Letters · doi:10.1016/s0304-3940(00)01418-x · Cited by 95
Chung, Y. C., Kim, Y.-S., Bok, E., Yune, T. Y., Maeng, S., & Jin, B. K. (2013) · Mediators of Inflammation · doi:10.1155/2013/370526 · Cited by 94
Spampinato, S. F., Merlo, S., Sano, Y., Kanda, T., & Sortino, M. A. (2017) · Journal of Neurochemistry · doi:10.1111/jnc.14068 · Cited by 90
Flagged first, then by citations
Research works printed but not linked: 192
- Hsia H-E, Tüshaus J, Brummer T, Zheng Y, Scilabra SD, Lichtenthaler SF (2019) Functions of ‘a disintegrin and metalloproteases (ADAMs)’ in the mammalian nervous system. Cell Mol Life Sci. https://doi.org/10.1007/s00018-019-03173-7 · DOI
- Rivera S, Khrestchatisky M, Kaczmarek L, Rosenberg GA, Jaworski DM (2010) Metzincin proteases and their inhibitors: foes or friends in nervous system physiology? J Neurosci 30(46):15337–15357. https://doi.org/10.1523/JNEUROSCI.3467-10.2010 · DOI · Paper page
- Baranger K, Rivera S, Liechti FD, Grandgirard D, Bigas J, Seco J, Tarrago T, Leib SL, Khrestchatisky M (2014) Endogenous and synthetic MMP inhibitors in CNS physiopathology. Prog Brain Res 214:313–351. https://doi.org/10.1016/B978-0-444-63486-3.00014-1 · DOI · Paper page
- Okada Y (2017) Proteinases and matrix degradation. In: Firestein GS, Budd RC, Gabriel SE, McInnes IB, O’Dell JR (eds) Kelley and Firestein’s textbook of rheumatology, vol 1, 10th edn. Elsevier, Philadelphia, pp 106–125. https://doi.org/10.1016/B978-0-323-31696-5.00008-5 · DOI
- Overall CM, Tam EM, Kappelhoff R, Connor A, Ewart T, Morrison CJ, Puente X, Lopez-Otin C, Seth A (2004) Protease degradomics: mass spectrometry discovery of protease substrates and the CLIP-CHIP, a dedicated DNA microarray of all human proteases and inhibitors. Biol Chem 385(6):493–504. https://doi.org/10.1515/BC.2004.058 · DOI
- Starr AE, Dufour A, Maier J, Overall CM (2012) Biochemical analysis of matrix metalloproteinase activation of chemokines CCL15 and CCL23 and increased glycosaminoglycan binding of CCL16. J Biol Chem 287(8):5848–5860. https://doi.org/10.1074/jbc.M111.314609 · DOI
- Hsu TI, Lin SC, Lu PS, Chang WC, Hung CY, Yeh YM, Su WC, Liao PC, Hung JJ (2015) MMP7-mediated cleavage of nucleolin at Asp255 induces MMP9 expression to promote tumor malignancy. Oncogene 34(7):826–837. https://doi.org/10.1038/onc.2014.22 · DOI
- Rosenberg GA (2017) Extracellular matrix inflammation in vascular cognitive impairment and dementia. Clin Sci 131(6):425–437. https://doi.org/10.1042/CS20160604 · DOI
- Wojcik L, Sawicka A, Rivera S, Zalewska T (2009) Neurogenesis in gerbil hippocampus following brain ischemia: focus on the involvement of metalloproteinases. Acta Neurobiol Exp 69(1):52–61 · DOI
- Ould-yahoui A, Tremblay E, Sbai O, Ferhat L, Bernard A, Charrat E, Gueye Y, Lim NH, Brew K, Risso JJ, Dive V, Khrestchatisky M, Rivera S (2009) A new role for TIMP-1 in modulating neurite outgrowth and morphology of cortical neurons. PLoS One 4(12):e8289. https://doi.org/10.1371/journal.pone.0008289 · DOI
- Ould-Yahoui A, Sbai O, Baranger K, Bernard A, Gueye Y, Charrat E, Clement B, Gigmes D, Dive V, Girard SD, Feron F, Khrestchatisky M, Rivera S (2013) Role of matrix metalloproteinases in migration and neurotrophic properties of nasal olfactory stem and ensheathing cells. Cell Transplant 22(6):993–1010. https://doi.org/10.3727/096368912X657468 · DOI
- Schonbeck U, Mach F, Libby P (1998) Generation of biologically active IL-1 beta by matrix metalloproteinases: a novel caspase-1-independent pathway of IL-1 beta processing. J Immunol 161(7):3340–3346 · DOI · Paper page
- Rosenberg GA (2002) Matrix metalloproteinases in neuroinflammation. Glia 39(3):279–291. https://doi.org/10.1002/glia.10108 · DOI
- Marchant DJ, Bellac CL, Moraes TJ, Wadsworth SJ, Dufour A, Butler GS, Bilawchuk LM, Hendry RG, Robertson AG, Cheung CT, Ng J, Ang L, Luo Z, Heilbron K, Norris MJ, Duan W, Bucyk T, Karpov A, Devel L, Georgiadis D, Hegele RG, Luo H, Granville DJ, Dive V, McManus BM, Overall CM (2014) A new transcriptional role for matrix metalloproteinase-12 in antiviral immunity. Nat Med 20(5):493–502. https://doi.org/10.1038/nm.3508 · DOI
- Nagase H, Brew K (2003) Designing TIMP (tissue inhibitor of metalloproteinases) variants that are selective metalloproteinase inhibitors. Bioch Soc Symp 70:201–212 · DOI
- Amour A, Knight CG, Webster A, Slocombe PM, Stephens PE, Knauper V, Docherty AJ, Murphy G (2000) The in vitro activity of ADAM-10 is inhibited by TIMP-1 and TIMP-3. FEBS Lett 473(3):275–279 · DOI
- Vandooren J, Van den Steen PE, Opdenakker G (2013) Biochemistry and molecular biology of gelatinase B or matrix metalloproteinase-9 (MMP-9): the next decade. Crit Rev Biochem Mol 48(3):222–272. https://doi.org/10.3109/10409238.2013.770819 · DOI
- Shofuda K, Moriyama K, Nishihashi A, Higashi S, Mizushima H, Yasumitsu H, Miki K, Sato H, Seiki M, Miyazaki K (1998) Role of tissue inhibitor of metalloproteinases-2 (TIMP-2) in regulation of pro-gelatinase A activation catalyzed by membrane-type matrix metalloproteinase-1 (MT1-MMP) in human cancer cells. J Biochem 124(2):462–470 · DOI
- Leco KJ, Apte SS, Taniguchi GT, Hawkes SP, Khokha R, Schultz GA, Edwards DR (1997) Murine tissue inhibitor of metalloproteinases-4 (Timp-4): cDNA isolation and expression in adult mouse tissues. FEBS Lett 401(2–3):213–217 · DOI
- Derry JM, Barnard PJ (1992) Physical linkage of the A-raf-1, properdin, synapsin I, and TIMP genes on the human and mouse X chromosomes. Genomics 12(4):632–638 · DOI
- Pohar N, Godenschwege TA, Buchner E (1999) Invertebrate tissue inhibitor of metalloproteinase: structure and nested gene organization within the synapsin locus is conserved from Drosophila to human. Genomics 57(2):293–296. https://doi.org/10.1006/geno.1999.5776 · DOI
- Rahkonen OP, Koskivirta IM, Oksjoki SM, Jokinen E, Vuorio EI (2002) Characterization of the murine Timp4 gene, localization within intron 5 of the synapsin 2 gene and tissue distribution of the mRNA. Biochim Biophys Acta 1577(1):45–52 · DOI
- Mullane K, Williams M (2013) Alzheimer’s therapeutics: continued clinical failures question the validity of the amyloid hypothesis-but what lies beyond? Biochem Pharmacol 85(3):289–305. https://doi.org/10.1016/j.bcp.2012.11.014 · DOI
- Mikulca JA, Nguyen V, Gajdosik DA, Teklu SG, Giunta EA, Lessa EA, Tran CH, Terak EC, Raffa RB (2014) Potential novel targets for Alzheimer pharmacotherapy: II Update on secretase inhibitors and related approaches. J Clin Pharm Ther 39(1):25–37. https://doi.org/10.1111/jcpt.12112 · DOI
- Mehta D, Jackson R, Paul G, Shi J, Sabbagh M (2017) Why do trials for Alzheimer’s disease drugs keep failing? A discontinued drug perspective for 2010-2015. Expert Opin Investig Drugs 26(6):735–739. https://doi.org/10.1080/13543784.2017.1323868 · DOI
- Lesne SE, Sherman MA, Grant M, Kuskowski M, Schneider JA, Bennett DA, Ashe KH (2013) Brain amyloid-beta oligomers in ageing and Alzheimer’s disease. Brain 136(Pt 5):1383–1398. https://doi.org/10.1093/brain/awt062 · DOI
- Tan JZA (1861) Gleeson PA (2019) The role of membrane trafficking in the processing of amyloid precursor protein and production of amyloid peptides in Alzheimer’s disease. BBA-Biomembranes 4:697–712. https://doi.org/10.1016/j.bbamem.2018.11.013 · DOI
- Basak JM, Verghese PB, Yoon H, Kim J, Holtzman DM (2012) Low-density lipoprotein receptor represents an apolipoprotein E-independent pathway of Abeta uptake and degradation by astrocytes. J Biol Chem 287(17):13959–13971. https://doi.org/10.1074/jbc.M111.288746 · DOI · Paper page
- Jaeger LB, Dohgu S, Hwang MC, Farr SA, Murphy MP, Fleegal-DeMotta MA, Lynch JL, Robinson SM, Niehoff ML, Johnson SN, Kumar VB, Banks WA (2009) Testing the neurovascular hypothesis of Alzheimer’s disease: LRP-1 antisense reduces blood-brain barrier clearance, increases brain levels of amyloid-beta protein, and impairs cognition. J Alzheimers Dis 17(3):553–570. https://doi.org/10.3233/JAD-2009-1074 · DOI
- Cai Z, Liu N, Wang C, Qin B, Zhou Y, Xiao M, Chang L, Yan LJ, Zhao B (2016) Role of RAGE in Alzheimer’s disease. Cell Mol Neurobiol 36(4):483–495. https://doi.org/10.1007/s10571-015-0233-3 · DOI
- Wan W, Cao L, Liu L, Zhang C, Kalionis B, Tai X, Li Y, Xia S (2015) Abeta(1-42) oligomer-induced leakage in an in vitro blood-brain barrier model is associated with up-regulation of RAGE and metalloproteinases, and down-regulation of tight junction scaffold proteins. J Neurochem 134(2):382–393. https://doi.org/10.1111/jnc.13122 · DOI
- Jorissen E, Prox J, Bernreuther C, Weber S, Schwanbeck R, Serneels L, Snellinx A, Craessaerts K, Thathiah A, Tesseur I, Bartsch U, Weskamp G, Blobel CP, Glatzel M, De Strooper B, Saftig P (2010) The disintegrin/metalloproteinase ADAM10 is essential for the establishment of the brain cortex. J Neurosci 30(14):4833–4844. https://doi.org/10.1523/JNEUROSCI.5221-09.2010 · DOI · Paper page
- Buxbaum JD, Liu KN, Luo Y, Slack JL, Stocking KL, Peschon JJ, Johnson RS, Castner BJ, Cerretti DP, Black RA (1998) Evidence that tumor necrosis factor alpha converting enzyme is involved in regulated alpha-secretase cleavage of the Alzheimer amyloid protein precursor. J Biol Chem 273(43):27765–27767 · DOI
- Chasseigneaux S, Allinquant B (2012) Functions of Abeta, sAPPalpha and sAPPbeta : similarities and differences. J Neurochem 120(Suppl 1):99–108. https://doi.org/10.1111/j.1471-4159.2011.07584.x · DOI
- Hick M, Herrmann U, Weyer SW, Mallm JP, Tschape JA, Borgers M, Mercken M, Roth FC, Draguhn A, Slomianka L, Wolfer DP, Korte M, Muller UC (2015) Acute function of secreted amyloid precursor protein fragment APPsalpha in synaptic plasticity. Acta Neuropathol 129(1):21–37. https://doi.org/10.1007/s00401-014-1368-x · DOI · Paper page
- Rose C, Dorard E, Audrain M, Gorisse-Hussonnois L, Cartier N, Braudeau J, Allinquant B (2018) Transient increase in sAPPalpha secretion in response to Abeta1-42 oligomers: an attempt of neuronal self-defense? Neurobiol Aging 61:23–35. https://doi.org/10.1016/j.neurobiolaging.2017.09.008 · DOI · Paper page
- Soscia SJ, Kirby JE, Washicosky KJ, Tucker SM, Ingelsson M, Hyman B, Burton MA, Goldstein LE, Duong S, Tanzi RE, Moir RD (2010) The Alzheimer’s disease-associated amyloid beta-protein is an antimicrobial peptide. PLoS One 5(3):e9505. https://doi.org/10.1371/journal.pone.0009505 · DOI · Paper page
- Eimer WA, Vijaya Kumar DK, Navalpur Shanmugam NK, Rodriguez AS, Mitchell T, Washicosky KJ, Gyorgy B, Breakefield XO, Tanzi RE, Moir RD (2018) Alzheimer’s disease-associated beta-amyloid is rapidly seeded by herpesviridae to protect against brain infection. Neuron 100(6):1527–1532. https://doi.org/10.1016/j.neuron.2018.11.043 · DOI
- Abramov E, Dolev I, Fogel H, Ciccotosto GD, Ruff E, Slutsky I (2009) Amyloid-beta as a positive endogenous regulator of release probability at hippocampal synapses. Nat Neurosci 12(12):1567–1576. https://doi.org/10.1038/nn.2433 · DOI · Paper page
- Morley JE, Farr SA, Banks WA, Johnson SN, Yamada KA, Xu L (2010) A physiological role for amyloid-beta protein:enhancement of learning and memory. J Alzheimers Dis 19(2):441–449. https://doi.org/10.3233/JAD-2009-1230 · DOI
- Puzzo D, Privitera L, Palmeri A (2012) Hormetic effect of amyloid-beta peptide in synaptic plasticity and memory. Neurobiol Aging 33(7):1484. https://doi.org/10.1016/j.neurobiolaging.2011.12.020 · DOI · Paper page
- Lawrence JL, Tong M, Alfulaij N, Sherrin T, Contarino M, White MM, Bellinger FP, Todorovic C, Nichols RA (2014) Regulation of presynaptic Ca2+, synaptic plasticity and contextual fear conditioning by a N-terminal beta-amyloid fragment. J Neurosci 34(43):14210–14218. https://doi.org/10.1523/JNEUROSCI.0326-14.2014 · DOI
- Palmeri A, Ricciarelli R, Gulisano W, Rivera D, Rebosio C, Calcagno E, Tropea MR, Conti S, Das U, Roy S, Pronzato MA, Arancio O, Fedele E, Puzzo D (2017) Amyloid-beta peptide is needed for cGMP-induced long-term potentiation and memory. J Neurosci 37(29):6926–6937. https://doi.org/10.1523/JNEUROSCI.3607-16.2017 · DOI
- Fragkouli A, Tsilibary EC, Tzinia AK (2014) Neuroprotective role of MMP-9 overexpression in the brain of Alzheimer’s 5xFAD mice. Neurobiol Dis 70:179–189. https://doi.org/10.1016/j.nbd.2014.06.021 · DOI
- Hernandez-Guillamon M, Mawhirt S, Blais S, Montaner J, Neubert TA, Rostagno A, Ghiso J (2015) Sequential amyloid-beta degradation by the matrix metalloproteases MMP-2 and MMP-9. J Biol Chem 290(24):15078–15091. https://doi.org/10.1074/jbc.M114.610931 · DOI · Paper page
- Yin KJ, Cirrito JR, Yan P, Hu X, Xiao Q, Pan X, Bateman R, Song H, Hsu FF, Turk J, Xu J, Hsu CY, Mills JC, Holtzman DM, Lee JM (2006) Matrix metalloproteinases expressed by astrocytes mediate extracellular amyloid-beta peptide catabolism. J Neurosci 26(43):10939–10948. https://doi.org/10.1523/JNEUROSCI.2085-06.2006 · DOI · Paper page
- Moore KM, Girens RE, Larson SK, Jones MR, Restivo JL, Holtzman DM, Cirrito JR, Yuede CM, Zimmerman SD, Timson BF (2016) A spectrum of exercise training reduces soluble Abeta in a dose-dependent manner in a mouse model of Alzheimer’s disease. Neurobiol Dis 85:218–224. https://doi.org/10.1016/j.nbd.2015.11.004 · DOI
- Taniguchi M, Matsuura K, Nakamura R, Kojima A, Konishi M, Akizawa T (2017) MMP-7 cleaves amyloid beta fragment peptides and copper ion inhibits the degradation. Biometals 30(5):797–807. https://doi.org/10.1007/s10534-017-0048-4 · DOI
- Liao MC, Van Nostrand WE (2010) Degradation of soluble and fibrillar amyloid beta-protein by matrix metalloproteinase (MT1-MMP) in vitro. Biochemistry 49(6):1127–1136. https://doi.org/10.1021/bi901994d · DOI · Paper page
- Montaner J, Ramiro L, Simats A, Hernández-Guillamon M, Delgado P, Bustamante A, Rosell A (2019) Matrix metalloproteinases and ADAMs in stroke. Cell Mol Life Sci. https://doi.org/10.1007/s00018-019-03175-5 · DOI
- Sweeney MD, Sagare AP, Zlokovic BV (2018) Blood-brain barrier breakdown in Alzheimer disease and other neurodegenerative disorders. Nat Rev Neurol 14(3):133–150. https://doi.org/10.1038/nrneurol.2017.188 · DOI · Paper page
- Giannoni P, Arango-Lievano M, Neves ID, Rousset MC, Baranger K, Rivera S, Jeanneteau F, Claeysen S, Marchi N (2016) Cerebrovascular pathology during the progression of experimental Alzheimer’s disease. Neurobiol Dis 88:107–117. https://doi.org/10.1016/j.nbd.2016.01.001 · DOI
- Mazzitelli S, Filipello F, Rasile M, Lauranzano E, Starvaggi-Cucuzza C, Tamborini M, Pozzi D, Barajon I, Giorgino T, Natalello A, Matteoli M (2016) Amyloid-beta 1-24 C-terminal truncated fragment promotes amyloid-beta 1-42 aggregate formation in the healthy brain. Acta Neuropathol Comm 4(1):110. https://doi.org/10.1186/s40478-016-0381-9 · DOI
- Brkic M, Balusu S, Van Wonterghem E, Gorle N, Benilova I, Kremer A, Van Hove I, Moons L, De Strooper B, Kanazir S, Libert C, Vandenbroucke RE (2015) Amyloid beta oligomers disrupt blood-CSF barrier integrity by activating matrix metalloproteinases. J Neurosci 35(37):12766–12778. https://doi.org/10.1523/JNEUROSCI.0006-15.2015 · DOI
- Garcia-Alloza M, Prada C, Lattarulo C, Fine S, Borrelli LA, Betensky R, Greenberg SM, Frosch MP, Bacskai BJ (2009) Matrix metalloproteinase inhibition reduces oxidative stress associated with cerebral amyloid angiopathy in vivo in transgenic mice. J Neurochem 109(6):1636–1647. https://doi.org/10.1111/j.1471-4159.2009.06096.x · DOI
- Prinz M, Priller J (2017) The role of peripheral immune cells in the CNS in steady state and disease. Nat Neurosci 20(2):136–144. https://doi.org/10.1038/nn.4475 · DOI · Paper page
- Jhang KA, Lee EO, Kim HS, Chang KA, Suh YH, Chong YH (2016) S100A9 exacerbates the Abeta1-42-mediated innate immunity in human THP-1 monocytes. CNS Neurol Disord-DR 15(8):910–917 · DOI
- Achilli C, Ciana A, Minetti G (2014) Amyloid-beta (25-35) peptide induces the release of pro-matrix metalloprotease 9 (pro-MMP-9) from human neutrophils. Mol Cell Biochem 397(1–2):117–123. https://doi.org/10.1007/s11010-014-2178-0 · DOI
- Zenaro E, Pietronigro E, Della Bianca V, Piacentino G, Marongiu L, Budui S, Turano E, Rossi B, Angiari S, Dusi S, Montresor A, Carlucci T, Nani S, Tosadori G, Calciano L, Catalucci D, Berton G, Bonetti B, Constantin G (2015) Neutrophils promote Alzheimer’s disease-like pathology and cognitive decline via LFA-1 integrin. Nat Med 21(8):880–886. https://doi.org/10.1038/nm.3913 · DOI · Paper page
- Deb S, Gottschall PE (1996) Increased production of matrix metalloproteinases in enriched astrocyte and mixed hippocampal cultures treated with beta-amyloid peptides. J Neurochem 66(4):1641–1647 · DOI
- Py NA, Bonnet AE, Bernard A, Marchalant Y, Charrat E, Checler F, Khrestchatisky M, Baranger K, Rivera S (2014) Differential spatio-temporal regulation of MMPs in the 5xFAD mouse model of Alzheimer’s disease: evidence for a pro-amyloidogenic role of MT1-MMP. Front Aging Neurosci 6:247. https://doi.org/10.3389/fnagi.2014.00247 · DOI · Paper page
- Seo JH, Guo S, Lok J, Navaratna D, Whalen MJ, Kim KW, Lo EH (2012) Neurovascular matrix metalloproteinases and the blood–brain barrier. Curr Pharm Design 18(25):3645–3648 · DOI
- Jourquin J, Tremblay E, Decanis N, Charton G, Hanessian S, Chollet AM, Le Diguardher T, Khrestchatisky M, Rivera S (2003) Neuronal activity-dependent increase of net matrix metalloproteinase activity is associated with MMP-9 neurotoxicity after kainate. Eur J Neurosci 18(6):1507–1517 · DOI · Paper page
- Hernandez-Guillamon M, Mawhirt S, Fossati S, Blais S, Pares M, Penalba A, Boada M, Couraud PO, Neubert TA, Montaner J, Ghiso J, Rostagno A (2010) Matrix metalloproteinase 2 (MMP-2) degrades soluble vasculotropic amyloid-beta E22Q and L34V mutants, delaying their toxicity for human brain microvascular endothelial cells. J Biol Chem 285(35):27144–27158. https://doi.org/10.1074/jbc.M110.135228 · DOI
- Mizoguchi H, Takuma K, Fukuzaki E, Ibi D, Someya E, Akazawa KH, Alkam T, Tsunekawa H, Mouri A, Noda Y, Nabeshima T, Yamada K (2009) Matrix metalloprotease-9 inhibition improves amyloid beta-mediated cognitive impairment and neurotoxicity in mice. J Pharmacol Exp Ther 331(1):14–22. https://doi.org/10.1124/jpet.109.154724 · DOI
- Langenfurth A, Rinnenthal JL, Vinnakota K, Prinz V, Carlo AS, Stadelmann C, Siffrin V, Peaschke S, Endres M, Heppner F, Glass R, Wolf SA, Kettenmann H (2014) Membrane-type 1 metalloproteinase is upregulated in microglia/brain macrophages in neurodegenerative and neuroinflammatory diseases. J Neurosci Res 92(3):275–286. https://doi.org/10.1002/jnr.23288 · DOI
- Ito S, Koshikawa N, Mochizuki S, Takenaga K (2007) 3-Methyladenine suppresses cell migration and invasion of HT1080 fibrosarcoma cells through inhibiting phosphoinositide 3-kinases independently of autophagy inhibition. Int J Oncol 31(2):261–268
- Ierusalimsky VN, Kuleshova EP, Balaban PM (2013) Expression of the type 1 metalloproteinase in the rat hippocampus after the intracerebroventricular injection of beta-amyloid peptide (25-35). Acta Neurobiol Exp 73(4):571–578 · DOI
- Jung SS, Zhang W, Van Nostrand WE (2003) Pathogenic A beta induces the expression and activation of matrix metalloproteinase-2 in human cerebrovascular smooth muscle cells. J Neurochem 85(5):1208–1215 · DOI
- Walker DG, Link J, Lue LF, Dalsing-Hernandez JE, Boyes BE (2006) Gene expression changes by amyloid beta peptide-stimulated human postmortem brain microglia identify activation of multiple inflammatory processes. J Leuk Biol 79(3):596–610. https://doi.org/10.1189/jlb.0705377 · DOI
- Sekine-Aizawa Y, Hama E, Watanabe K, Tsubuki S, Kanai-Azuma M, Kanai Y, Arai H, Aizawa H, Iwata N, Saido TC (2001) Matrix metalloproteinase (MMP) system in brain: identification and characterization of brain-specific MMP highly expressed in cerebellum. Eur J Neurosci 13(5):935–948 · DOI · Paper page
- Mroczko B, Groblewska M, Zboch M, Kulczynska A, Koper OM, Szmitkowski M, Kornhuber J, Lewczuk P (2014) Concentrations of matrix metalloproteinases and their tissue inhibitors in the cerebrospinal fluid of patients with Alzheimer’s disease. J Alzheimers Dis 40(2):351–357. https://doi.org/10.3233/JAD-131634 · DOI · Paper page
- Horstmann S, Budig L, Gardner H, Koziol J, Deuschle M, Schilling C, Wagner S (2010) Matrix metalloproteinases in peripheral blood and cerebrospinal fluid in patients with Alzheimer’s disease. Int Psychogeriatr 22(6):966–972. https://doi.org/10.1017/S1041610210000827 · DOI
- Lorenzl S, Albers DS, Relkin N, Ngyuen T, Hilgenberg SL, Chirichigno J, Cudkowicz ME, Beal MF (2003) Increased plasma levels of matrix metalloproteinase-9 in patients with Alzheimer’s disease. Neurochem Int 43(3):191–196 · DOI · Paper page
- Lorenzl S, Buerger K, Hampel H, Beal MF (2008) Profiles of matrix metalloproteinases and their inhibitors in plasma of patients with dementia. Int Psychogeriatr 20(1):67–76. https://doi.org/10.1017/S1041610207005790 · DOI
- Stomrud E, Bjorkqvist M, Janciauskiene S, Minthon L, Hansson O (2010) Alterations of matrix metalloproteinases in the healthy elderly with increased risk of prodromal Alzheimer’s disease. Alz Res Ther 2(3):20. https://doi.org/10.1186/alzrt44 · DOI
- Hanzel CE, Iulita MF, Eyjolfsdottir H, Hjorth E, Schultzberg M, Eriksdotter M, Cuello AC (2014) Analysis of matrix metallo-proteases and the plasminogen system in mild cognitive impairment and Alzheimer’s disease cerebrospinal fluid. J Alzheimers Dis 40(3):667–678. https://doi.org/10.3233/JAD-132282 · DOI
- Peng M, Jia J, Qin W (2015) Plasma gelsolin and matrix metalloproteinase 3 as potential biomarkers for Alzheimer disease. Neurosci Lett 595:116–121. https://doi.org/10.1016/j.neulet.2015.04.014 · DOI
- Selvais C, D’Auria L, Tyteca D, Perrot G, Lemoine P, Troeberg L, Dedieu S, Noel A, Nagase H, Henriet P, Courtoy PJ, Marbaix E, Emonard H (2011) Cell cholesterol modulates metalloproteinase-dependent shedding of low-density lipoprotein receptor-related protein-1 (LRP-1) and clearance function. FASEB J 25(8):2770–2781. https://doi.org/10.1096/fj.10-169508 · DOI
- Liu Q, Zhang J, Tran H, Verbeek MM, Reiss K, Estus S, Bu G (2009) LRP1 shedding in human brain: roles of ADAM10 and ADAM17. Mol Neurodegener 4:17. https://doi.org/10.1186/1750-1326-4-17 · DOI · Paper page
- Raucci A, Cugusi S, Antonelli A, Barabino SM, Monti L, Bierhaus A, Reiss K, Saftig P, Bianchi ME (2008) A soluble form of the receptor for advanced glycation endproducts (RAGE) is produced by proteolytic cleavage of the membrane-bound form by the sheddase a disintegrin and metalloprotease 10 (ADAM10). FASEB J 22(10):3716–3727. https://doi.org/10.1096/fj.08-109033 · DOI
- Zhang L, Bukulin M, Kojro E, Roth A, Metz VV, Fahrenholz F, Nawroth PP, Bierhaus A, Postina R (2008) Receptor for advanced glycation end products is subjected to protein ectodomain shedding by metalloproteinases. J Biol Chem 283(51):35507–35516. https://doi.org/10.1074/jbc.M806948200 · DOI
- Metz VV, Kojro E, Rat D, Postina R (2012) Induction of RAGE shedding by activation of G protein-coupled receptors. PLoS One 7(7):e41823. https://doi.org/10.1371/journal.pone.0041823 · DOI
- Sagare A, Deane R, Bell RD, Johnson B, Hamm K, Pendu R, Marky A, Lenting PJ, Wu Z, Zarcone T, Goate A, Mayo K, Perlmutter D, Coma M, Zhong Z, Zlokovic BV (2007) Clearance of amyloid-beta by circulating lipoprotein receptors. Nat Med 13(9):1029–1031. https://doi.org/10.1038/nm1635 · DOI · Paper page
- Terni B, Ferrer I (2015) Abnormal expression and distribution of MMP2 at initial stages of Alzheimer’s disease-related pathology. J Alzheimers Dis 46(2):461–469. https://doi.org/10.3233/JAD-142460 · DOI
- Nubling G, Levin J, Bader B, Israel L, Botzel K, Lorenzl S, Giese A (2012) Limited cleavage of tau with matrix-metalloproteinase MMP-9, but not MMP-3, enhances tau oligomer formation. Exp Neurol 237(2):470–476. https://doi.org/10.1016/j.expneurol.2012.07.018 · DOI
- Bjerke M, Zetterberg H, Edman A, Blennow K, Wallin A, Andreasson U (2011) Cerebrospinal fluid matrix metalloproteinases and tissue inhibitor of metalloproteinases in combination with subcortical and cortical biomarkers in vascular dementia and Alzheimer’s disease. J Alzheimers Dis 27(3):665–676. https://doi.org/10.3233/JAD-2011-110566 · DOI · Paper page
- Higashi S, Miyazaki K (2003) Novel processing of beta-amyloid precursor protein catalyzed by membrane type 1 matrix metalloproteinase releases a fragment lacking the inhibitor domain against gelatinase A. Biochemistry 42(21):6514–6526. https://doi.org/10.1021/bi020643m · DOI · Paper page
- Miyazaki K, Hasegawa M, Funahashi K, Umeda M (1993) A metalloproteinase inhibitor domain in Alzheimer amyloid protein precursor. Nature 362(6423):839–841. https://doi.org/10.1038/362839a0 · DOI
- Ahmad M, Takino T, Miyamori H, Yoshizaki T, Furukawa M, Sato H (2006) Cleavage of amyloid-beta precursor protein (APP) by membrane-type matrix metalloproteinases. J Biochem 139(3):517–526. https://doi.org/10.1093/jb/mvj054 · DOI · Paper page
- Komori K, Nonaka T, Okada A, Kinoh H, Hayashita-Kinoh H, Yoshida N, Yana I, Seiki M (2004) Absence of mechanical allodynia and Abeta-fiber sprouting after sciatic nerve injury in mice lacking membrane-type 5 matrix metalloproteinase. FEBS Lett 557(1–3):125–128 · DOI
- Baranger K, Marchalant Y, Bonnet AE, Crouzin N, Carrete A, Paumier JM, Py NA, Bernard A, Bauer C, Charrat E, Moschke K, Seiki M, Vignes M, Lichtenthaler SF, Checler F, Khrestchatisky M, Rivera S (2016) MT5-MMP is a new pro-amyloidogenic proteinase that promotes amyloid pathology and cognitive decline in a transgenic mouse model of Alzheimer’s disease. Cell Mol Life Sci 73(1):217–236. https://doi.org/10.1007/s00018-015-1992-1 · DOI · Paper page
- Baranger K, Bonnet AE, Girard SD, Paumier JM, Garcia-Gonzalez L, Elmanaa W, Bernard A, Charrat E, Stephan D, Bauer C, Moschke K, Lichtenthaler SF, Roman FS, Checler F, Khrestchatisky M, Rivera S (2017) MT5-MMP Promotes Alzheimer’s Pathogenesis in the Frontal Cortex of 5xFAD Mice and APP Trafficking in vitro. Front Mol Neurosci 9:163. https://doi.org/10.3389/fnmol.2016.00163 · DOI · Paper page
- Kimura R, Ohno M (2009) Impairments in remote memory stabilization precede hippocampal synaptic and cognitive failures in 5XFAD Alzheimer mouse model. Neurobiol Dis 33(2):229–235. https://doi.org/10.1016/j.nbd.2008.10.006 · DOI · Paper page
- Crouzin N, Baranger K, Cavalier M, Marchalant Y, Cohen-Solal C, Roman FS, Khrestchatisky M, Rivera S, Feron F, Vignes M (2013) Area-specific alterations of synaptic plasticity in the 5XFAD mouse model of Alzheimer’s disease: dissociation between somatosensory cortex and hippocampus. PLoS One 8(9):e74667. https://doi.org/10.1371/journal.pone.0074667 · DOI
- Baranger K, Giannoni P, Girard SD, Girot S, Gaven F, Stephan D, Migliorati M, Khrestchatisky M, Bockaert J, Marchetti-Gauthier E, Rivera S, Claeysen S, Roman FS (2017) Chronic treatments with a 5-HT4 receptor agonist decrease amyloid pathology in the entorhinal cortex and learning and memory deficits in the 5xFAD mouse model of Alzheimer’s disease. Neuropharmacology 126:128–141. https://doi.org/10.1016/j.neuropharm.2017.08.031 · DOI
- Wang P, Wang X, Pei D (2004) Mint-3 regulates the retrieval of the internalized membrane-type matrix metalloproteinase, MT5-MMP, to the plasma membrane by binding to its carboxyl end motif EWV. J Biol Chem 279(19):20461–20470. https://doi.org/10.1074/jbc.M400264200 · DOI · Paper page
- Laulagnier K, Javalet C, Hemming FJ, Chivet M, Lachenal G, Blot B, Chatellard C, Sadoul R (2018) Amyloid precursor protein products concentrate in a subset of exosomes specifically endocytosed by neurons. Cell Mol Life Sci 75(4):757–773. https://doi.org/10.1007/s00018-017-2664-0 · DOI · Paper page
- Zhang Z, Song M, Liu X, Su Kang S, Duong DM, Seyfried NT, Cao X, Cheng L, Sun YE, Ping YuS, Jia J, Levey AI, Ye K (2015) Delta-secretase cleaves amyloid precursor protein and regulates the pathogenesis in Alzheimer’s disease. Nat Comm 6:8762. https://doi.org/10.1038/ncomms9762 · DOI · Paper page
- Paumier JM, Py NA, Garcia-Gonzalez L, Bernard A, Stephan D, Louis L, Checler F, Khrestchatisky M, Baranger K, Rivera S (2018) Proamyloidogenic effects of membrane type 1 matrix metalloproteinase involve MMP-2 and BACE-1 activities, and the modulation of APP trafficking. FASEB J. https://doi.org/10.1096/fj.201801076r · DOI · Paper page
- Uekita T, Itoh Y, Yana I, Ohno H, Seiki M (2001) Cytoplasmic tail-dependent internalization of membrane-type 1 matrix metalloproteinase is important for its invasion-promoting activity. J Cell Biol 155(7):1345–1356. https://doi.org/10.1083/jcb.200108112 · DOI
- Perez RG, Soriano S, Hayes JD, Ostaszewski B, Xia W, Selkoe DJ, Chen X, Stokin GB, Koo EH (1999) Mutagenesis identifies new signals for beta-amyloid precursor protein endocytosis, turnover, and the generation of secreted fragments, including Abeta42. J Biol Chem 274(27):18851–18856 · DOI
- Caster AH, Kahn RA (2013) Recruitment of the Mint3 adaptor is necessary for export of the amyloid precursor protein (APP) from the Golgi complex. J Biol Chem 288(40):28567–28580. https://doi.org/10.1074/jbc.M113.481101 · DOI · Paper page
- Vincent B, Checler F (2012) alpha-Secretase in Alzheimer’s disease and beyond: mechanistic, regulation and function in the shedding of membrane proteins. Curr Alz Res 9(2):140–156 · DOI
- Saftig P, Lichtenthaler SF (2015) The alpha secretase ADAM10: a metalloprotease with multiple functions in the brain. Prog Neurobiol 135:1–20. https://doi.org/10.1016/j.pneurobio.2015.10.003 · DOI
- Letronne F, Laumet G, Ayral AM, Chapuis J, Demiautte F, Laga M, Vandenberghe ME, Malmanche N, Leroux F, Eysert F, Sottejeau Y, Chami L, Flaig A, Bauer C, Dourlen P, Lesaffre M, Delay C, Huot L, Dumont J, Werkmeister E, Lafont F, Mendes T, Hansmannel F, Dermaut B, Deprez B, Herard AS, Dhenain M, Souedet N, Pasquier F, Tulasne D, Berr C, Hauw JJ, Lemoine Y, Amouyel P, Mann D, Deprez R, Checler F, Hot D, Delzescaux T, Gevaert K, Lambert JC (2016) ADAM30 Downregulates APP-Linked defects through cathepsin D activation in Alzheimer’s disease. EBioMedicine 9:278–292. https://doi.org/10.1016/j.ebiom.2016.06.002 · DOI
- Feuerbach D, Schindler P, Barske C, Joller S, Beng-Louka E, Worringer KA, Kommineni S, Kaykas A, Ho DJ, Ye C, Welzenbach K, Elain G, Klein L, Brzak I, Mir AK, Farady CJ, Aichholz R, Popp S, George N, Neumann U (2017) ADAM17 is the main sheddase for the generation of human triggering receptor expressed in myeloid cells (hTREM2) ectodomain and cleaves TREM2 after Histidine 157. Neurosci Lett 660:109–114. https://doi.org/10.1016/j.neulet.2017.09.034 · DOI
- Decourt B, Lahiri DK, Sabbagh MN (2017) Targeting tumor necrosis factor alpha for Alzheimer’s disease. Curr Alz Res 14(4):412–425. https://doi.org/10.2174/1567205013666160930110551 · DOI
- Peress N, Perillo E, Zucker S (1995) Localization of tissue inhibitor of matrix metalloproteinases in Alzheimer’s disease and normal brain. J Neuropathol Exp Neurol 54(1):16–22 · DOI · Paper page
- Lorenzl S, Albers DS, LeWitt PA, Chirichigno JW, Hilgenberg SL, Cudkowicz ME, Beal MF (2003) Tissue inhibitors of matrix metalloproteinases are elevated in cerebrospinal fluid of neurodegenerative diseases. J Neurol Sci 207(1–2):71–76 · DOI
- Marksteiner J, Imarhiagbe D, Defrancesco M, Deisenhammer EA, Kemmler G, Humpel C (2014) Analysis of 27 vascular-related proteins reveals that NT-proBNP is a potential biomarker for Alzheimer’s disease and mild cognitive impairment: a pilot-study. Exp Gerontol 50:114–121. https://doi.org/10.1016/j.exger.2013.12.001 · DOI
- Ridnour LA, Dhanapal S, Hoos M, Wilson J, Lee J, Cheng RY, Brueggemann EE, Hines HB, Wilcock DM, Vitek MP, Wink DA, Colton CA (2012) Nitric oxide-mediated regulation of beta-amyloid clearance via alterations of MMP-9/TIMP-1. J Neurochem 123(5):736–749. https://doi.org/10.1111/jnc.12028 · DOI · Paper page
- Duits FH, Hernandez-Guillamon M, Montaner J, Goos JD, Montanola A, Wattjes MP, Barkhof F, Scheltens P, Teunissen CE, van der Flier WM (2015) Matrix metalloproteinases in Alzheimer’s disease and concurrent cerebral microbleeds. J Alzheimers Dis 48(3):711–720. https://doi.org/10.3233/JAD-143186 · DOI · Paper page
- Hernandez-Guillamon M, Delgado P, Ortega L, Pares M, Rosell A, Garcia-Bonilla L, Fernandez-Cadenas I, Borrell-Pages M, Boada M, Montaner J (2009) Neuronal TIMP-1 release accompanies astrocytic MMP-9 secretion and enhances astrocyte proliferation induced by beta-amyloid 25-35 fragment. J Neurosci Res 87(9):2115–2125. https://doi.org/10.1002/jnr.22034 · DOI · Paper page
- Ogier C, Creidy R, Boucraut J, Soloway PD, Khrestchatisky M, Rivera S (2005) Astrocyte reactivity to Fas activation is attenuated in TIMP-1 deficient mice, an in vitro study. BMC Neurosci 6:68. https://doi.org/10.1186/1471-2202-6-68 · DOI · Paper page
- Thirumangalakudi L, Samany PG, Owoso A, Wiskar B, Grammas P (2006) Angiogenic proteins are expressed by brain blood vessels in Alzheimer’s disease. J Alzheimers Dis 10(1):111–118 · DOI
- Park SK, Hwang YS, Park KK, Park HJ, Seo JY, Chung WY (2009) Kalopanaxsaponin A inhibits PMA-induced invasion by reducing matrix metalloproteinase-9 via PI3K/Akt- and PKCdelta-mediated signaling in MCF-7 human breast cancer cells. Carcinogenesis 30(7):1225–1233. https://doi.org/10.1093/carcin/bgp111 · DOI
- Hoe HS, Cooper MJ, Burns MP, Lewis PA, van der Brug M, Chakraborty G, Cartagena CM, Pak DT, Cookson MR, Rebeck GW (2007) The metalloprotease inhibitor TIMP-3 regulates amyloid precursor protein and apolipoprotein E receptor proteolysis. J Neurosci 27(40):10895–10905. https://doi.org/10.1523/JNEUROSCI.3135-07.2007 · DOI · Paper page
- Qin W, Jia X, Wang F, Zuo X, Wu L, Zhou A, Li D, Min B, Wei C, Tang Y, Xing Y, Dong X, Wang Q, Gao Y, Li Y, Jia J (2015) Elevated plasma angiogenesis factors in Alzheimer’s disease. J Alzheimers Dis 45(1):245–252. https://doi.org/10.3233/JAD-142409 · DOI
- Polymeropoulos MH, Lavedan C, Leroy E, Ide SE, Dehejia A, Dutra A, Pike B, Root H, Rubenstein J, Boyer R, Stenroos ES, Chandrasekharappa S, Athanassiadou A, Papapetropoulos T, Johnson WG, Lazzarini AM, Duvoisin RC, Di Iorio G, Golbe LI, Nussbaum RL (1997) Mutation in the alpha-synuclein gene identified in families with Parkinson’s disease. Science 276(5321):2045–2047 · DOI · Paper page
- Kruger R, Kuhn W, Muller T, Woitalla D, Graeber M, Kosel S, Przuntek H, Epplen JT, Schols L, Riess O (1998) Ala30Pro mutation in the gene encoding alpha-synuclein in Parkinson’s disease. Nat Genet 18(2):106–108. https://doi.org/10.1038/ng0298-106 · DOI · Paper page
- Singleton AB, Farrer M, Johnson J, Singleton A, Hague S, Kachergus J, Hulihan M, Peuralinna T, Dutra A, Nussbaum R, Lincoln S, Crawley A, Hanson M, Maraganore D, Adler C, Cookson MR, Muenter M, Baptista M, Miller D, Blancato J, Hardy J, Gwinn-Hardy K (2003) alpha-Synuclein locus triplication causes Parkinson’s disease. Science 302(5646):841. https://doi.org/10.1126/science.1090278 · DOI · Paper page
- Chartier-Harlin MC, Kachergus J, Roumier C, Mouroux V, Douay X, Lincoln S, Levecque C, Larvor L, Andrieux J, Hulihan M, Waucquier N, Defebvre L, Amouyel P, Farrer M, Destee A (2004) Alpha-synuclein locus duplication as a cause of familial Parkinson’s disease. Lancet 364(9440):1167–1169. https://doi.org/10.1016/S0140-6736(04)17103-1 · DOI · Paper page
- Zarranz JJ, Alegre J, Gomez-Esteban JC, Lezcano E, Ros R, Ampuero I, Vidal L, Hoenicka J, Rodriguez O, Atares B, Llorens V, Gomez Tortosa E, del Ser T, Munoz DG, de Yebenes JG (2004) The new mutation, E46K, of alpha-synuclein causes Parkinson and Lewy body dementia. Ann Neurol 55(2):164–173. https://doi.org/10.1002/ana.10795 · DOI · Paper page
- Ghosh D, Mehra S, Sahay S, Singh PK, Maji SK (2017) alpha-synuclein aggregation and its modulation. Int J Biol Macromol 100:37–54. https://doi.org/10.1016/j.ijbiomac.2016.10.021 · DOI
- Longhena F, Faustini G, Missale C, Pizzi M, Spano P, Bellucci A (2017) The contribution of alpha-synuclein spreading to Parkinson’s disease synaptopathy. Neural Plast 2017:5012129. https://doi.org/10.1155/2017/5012129 · DOI
- Olanow CW, Brundin P (2013) Parkinson’s disease and alpha synuclein: is Parkinson’s disease a prion-like disorder? Mov Dis 28(1):31–40. https://doi.org/10.1002/mds.25373 · DOI
- Wakabayashi K, Tanji K, Odagiri S, Miki Y, Mori F, Takahashi H (2013) The Lewy body in Parkinson’s disease and related neurodegenerative disorders. Mol Neurobiol 47(2):495–508. https://doi.org/10.1007/s12035-012-8280-y · DOI
- Ding TT, Lee SJ, Rochet JC, Lansbury PT Jr (2002) Annular alpha-synuclein protofibrils are produced when spherical protofibrils are incubated in solution or bound to brain-derived membranes. Biochemistry 41(32):10209–10217 · DOI
- Lashuel HA, Hartley D, Petre BM, Walz T, Lansbury PT Jr (2002) Neurodegenerative disease: amyloid pores from pathogenic mutations. Nature 418(6895):291. https://doi.org/10.1038/418291a · DOI
- Lashuel HA, Petre BM, Wall J, Simon M, Nowak RJ, Walz T, Lansbury PT Jr (2002) Alpha-synuclein, especially the Parkinson’s disease-associated mutants, forms pore-like annular and tubular protofibrils. J Mol Biol 322(5):1089–1102 · DOI
- Baba M, Nakajo S, Tu PH, Tomita T, Nakaya K, Lee VM, Trojanowski JQ, Iwatsubo T (1998) Aggregation of alpha-synuclein in Lewy bodies of sporadic Parkinson’s disease and dementia with Lewy bodies. Am J Pathol 152(4):879–884
- Lee MK, Stirling W, Xu Y, Xu X, Qui D, Mandir AS, Dawson TM, Copeland NG, Jenkins NA, Price DL (2002) Human alpha-synuclein-harboring familial Parkinson’s disease-linked Ala-53 –> Thr mutation causes neurodegenerative disease with alpha-synuclein aggregation in transgenic mice. Proc Natl Acad Sci USA 99(13):8968–8973. https://doi.org/10.1073/pnas.132197599 · DOI · Paper page
- Crowther RA, Jakes R, Spillantini MG, Goedert M (1998) Synthetic filaments assembled from C-terminally truncated alpha-synuclein. FEBS Lett 436(3):309–312 · DOI
- Kanda S, Bishop JF, Eglitis MA, Yang Y, Mouradian MM (2000) Enhanced vulnerability to oxidative stress by alpha-synuclein mutations and C-terminal truncation. Neuroscience 97(2):279–284 · DOI
- Sung JY, Park SM, Lee CH, Um JW, Lee HJ, Kim J, Oh YJ, Lee ST, Paik SR, Chung KC (2005) Proteolytic cleavage of extracellular secreted {alpha}-synuclein via matrix metalloproteinases. J Biol Chem 280(26):25216–25224. https://doi.org/10.1074/jbc.M503341200 · DOI
- Levin J, Giese A, Boetzel K, Israel L, Hogen T, Nubling G, Kretzschmar H, Lorenzl S (2009) Increased alpha-synuclein aggregation following limited cleavage by certain matrix metalloproteinases. Exp Neurol 215(1):201–208. https://doi.org/10.1016/j.expneurol.2008.10.010 · DOI
- Kim YS, Choi DH, Block ML, Lorenzl S, Yang L, Kim YJ, Sugama S, Cho BP, Hwang O, Browne SE, Kim SY, Hong JS, Beal MF, Joh TH (2007) A pivotal role of matrix metalloproteinase-3 activity in dopaminergic neuronal degeneration via microglial activation. FASEB J 21(1):179–187. https://doi.org/10.1096/fj.06-5865com · DOI
- Choi DH, Kim EM, Son HJ, Joh TH, Kim YS, Kim D, Flint Beal M, Hwang O (2008) A novel intracellular role of matrix metalloproteinase-3 during apoptosis of dopaminergic cells. J Neurochem 106(1):405–415. https://doi.org/10.1111/j.1471-4159.2008.05399.x · DOI
- Kim YS, Kim SS, Cho JJ, Choi DH, Hwang O, Shin DH, Chun HS, Beal MF, Joh TH (2005) Matrix metalloproteinase-3: a novel signaling proteinase from apoptotic neuronal cells that activates microglia. J Neurosci 25(14):3701–3711. https://doi.org/10.1523/JNEUROSCI.4346-04.2005 · DOI
- Lee EJ, Woo MS, Moon PG, Baek MC, Choi IY, Kim WK, Junn E, Kim HS (2010) Alpha-synuclein activates microglia by inducing the expressions of matrix metalloproteinases and the subsequent activation of protease-activated receptor-1. J Immunol 185(1):615–623. https://doi.org/10.4049/jimmunol.0903480 · DOI
- Bonifati V, Rizzu P, van Baren MJ, Schaap O, Breedveld GJ, Krieger E, Dekker MC, Squitieri F, Ibanez P, Joosse M, van Dongen JW, Vanacore N, van Swieten JC, Brice A, Meco G, van Duijn CM, Oostra BA, Heutink P (2003) Mutations in the DJ-1 gene associated with autosomal recessive early-onset parkinsonism. Science 299(5604):256–259. https://doi.org/10.1126/science.1077209 · DOI
- Choi DH, Hwang O, Lee KH, Lee J, Beal MF, Kim YS (2011) DJ-1 cleavage by matrix metalloproteinase 3 mediates oxidative stress-induced dopaminergic cell death. Antiox Redox Sign 14(11):2137–2150. https://doi.org/10.1089/ars.2009.3059 · DOI
- Miller DW, Ahmad R, Hague S, Baptista MJ, Canet-Aviles R, McLendon C, Carter DM, Zhu PP, Stadler J, Chandran J, Klinefelter GR, Blackstone C, Cookson MR (2003) L166P mutant DJ-1, causative for recessive Parkinson’s disease, is degraded through the ubiquitin-proteasome system. J Biol Chem 278(38):36588–36595. https://doi.org/10.1074/jbc.M304272200 · DOI
- Kim YS, Joh TH (2012) Matrix metalloproteinases, new insights into the understanding of neurodegenerative disorders. Biomol Ther 20(2):133–143. https://doi.org/10.4062/biomolther.2012.20.2.133 · DOI
- Shendelman S, Jonason A, Martinat C, Leete T, Abeliovich A (2004) DJ-1 is a redox-dependent molecular chaperone that inhibits alpha-synuclein aggregate formation. PLoS Biol 2(11):e362. https://doi.org/10.1371/journal.pbio.0020362 · DOI
- Butler GS, Dean RA, Tam EM, Overall CM (2008) Pharmacoproteomics of a metalloproteinase hydroxamate inhibitor in breast cancer cells: dynamics of membrane type 1 matrix metalloproteinase-mediated membrane protein shedding. Mol Cell Biol 28(15):4896–4914. https://doi.org/10.1128/MCB.01775-07 · DOI
- Joo SH, Kwon KJ, Kim JW, Kim JW, Hasan MR, Lee HJ, Han SH, Shin CY (2010) Regulation of matrix metalloproteinase-9 and tissue plasminogen activator activity by alpha-synuclein in rat primary glial cells. Neurosci Lett 469(3):352–356. https://doi.org/10.1016/j.neulet.2009.12.026 · DOI
- Kim S, Cho SH, Kim KY, Shin KY, Kim HS, Park CH, Chang KA, Lee SH, Cho D, Suh YH (2009) Alpha-synuclein induces migration of BV-2 microglial cells by up-regulation of CD44 and MT1-MMP. J Neurochem 109(5):1483–1496. https://doi.org/10.1111/j.1471-4159.2009.06075.x · DOI
- Paisan-Ruiz C, Jain S, Evans EW, Gilks WP, Simon J, van der Brug M, Lopez de Munain A, Aparicio S, Gil AM, Khan N, Johnson J, Martinez JR, Nicholl D, Carrera IM, Pena AS, de Silva R, Lees A, Marti-Masso JF, Perez-Tur J, Wood NW, Singleton AB (2004) Cloning of the gene containing mutations that cause PARK8-linked Parkinson’s disease. Neuron 44(4):595–600. https://doi.org/10.1016/j.neuron.2004.10.023 · DOI
- Cookson MR (2010) The role of leucine-rich repeat kinase 2 (LRRK2) in Parkinson’s disease. Nat Rev Neurosci 11(12):791–797. https://doi.org/10.1038/nrn2935 · DOI
- Caesar M, Felk S, Zach S, Bronstad G, Aasly JO, Gasser T, Gillardon F (2014) Changes in matrix metalloprotease activity and progranulin levels may contribute to the pathophysiological function of mutant leucine-rich repeat kinase 2. Glia 62(7):1075–1092. https://doi.org/10.1002/glia.22663 · DOI
- Suh HS, Choi N, Tarassishin L, Lee SC (2012) Regulation of progranulin expression in human microglia and proteolysis of progranulin by matrix metalloproteinase-12 (MMP-12). PLoS One 7(4):e35115. https://doi.org/10.1371/journal.pone.0035115 · DOI
- Bachiller S, Jimenez-Ferrer I, Paulus A, Yang Y, Swanberg M, Deierborg T, Boza-Serrano A (2018) Microglia in neurological diseases: a road map to brain-disease dependent-inflammatory response. Front Cell Neurosci 12:488. https://doi.org/10.3389/fncel.2018.00488 · DOI
- Oh SH, Kim HN, Park HJ, Shin JY, Kim DY, Lee PH (2017) The cleavage effect of mesenchymal stem cell and its derived matrix metalloproteinase-2 on extracellular alpha-synuclein aggregates in Parkinsonian models. Stem Cells Translat Med 6(3):949–961. https://doi.org/10.5966/sctm.2016-0111 · DOI
- Lorenzl S, Albers DS, Narr S, Chirichigno J, Beal MF (2002) Expression of MMP-2, MMP-9, and MMP-1 and their endogenous counterregulators TIMP-1 and TIMP-2 in postmortem brain tissue of Parkinson’s disease. Exp Neurol 178(1):13–20 · DOI
- Kim SY, Woo MS, Park JS, Hyun JW, Kim YS, Kim HS (2010) The neuroprotective role of tissue inhibitor of metalloproteinase-2 in MPP+- or 6-OHDA-treated SK-N-BE(2)C and SH-SY5Y human neuroblastoma cells. Neurosci Lett 468(2):136–140. https://doi.org/10.1016/j.neulet.2009.10.084 · DOI
- Kim J, Jeong YH, Lee EJ, Park JS, Seo H, Kim HS (2017) Suppression of neuroinflammation by matrix metalloproteinase-8 inhibitor in aged normal and LRRK2 G2019S Parkinson’s disease model mice challenged with lipopolysaccharide. Biochem Biophys Res Comm 493(2):879–886. https://doi.org/10.1016/j.bbrc.2017.09.129 · DOI
- Lorenzl S, Calingasan N, Yang L, Albers DS, Shugama S, Gregorio J, Krell HW, Chirichigno J, Joh T, Beal MF (2004) Matrix metalloproteinase-9 is elevated in 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine-induced parkinsonism in mice. Neuromol Med 5(2):119–132. https://doi.org/10.1385/nmm:5:2:119 · DOI
- Logroscino G, Tortelli R, Rizzo G, Marin B, Preux P, Malaspina A (2015) Amyotrophic lateral sclerosis: an aging-related disease. Curr Geri Rep 4:142. https://doi.org/10.1007/s13670-015-0127-8 · DOI
- Lukaszewicz-Zajac M, Mroczko B, Slowik A (2014) Matrix metalloproteinases (MMPs) and their tissue inhibitors (TIMPs) in amyotrophic lateral sclerosis (ALS). J Neural Trans 121(11):1387–1397. https://doi.org/10.1007/s00702-014-1205-3 · DOI
- Dewil M, Schurmans C, Starckx S, Opdenakker G, Van Den Bosch L, Robberecht W (2005) Role of matrix metalloproteinase-9 in a mouse model for amyotrophic lateral sclerosis. NeuroReport 16(4):321–324 · DOI
- Kiaei M, Kipiani K, Calingasan NY, Wille E, Chen J, Heissig B, Rafii S, Lorenzl S, Beal MF (2007) Matrix metalloproteinase-9 regulates TNF-alpha and FasL expression in neuronal, glial cells and its absence extends life in a transgenic mouse model of amyotrophic lateral sclerosis. Exp Neurol 205(1):74–81. https://doi.org/10.1016/j.expneurol.2007.01.036 · DOI
- Kaplan A, Spiller KJ, Towne C, Kanning KC, Choe GT, Geber A, Akay T, Aebischer P, Henderson CE (2014) Neuronal matrix metalloproteinase-9 is a determinant of selective neurodegeneration. Neuron 81(2):333–348. https://doi.org/10.1016/j.neuron.2013.12.009 · DOI
- Morisaki Y, Niikura M, Watanabe M, Onishi K, Tanabe S, Moriwaki Y, Okuda T, Ohara S, Murayama S, Takao M, Uchida S, Yamanaka K, Misawa H (2016) Selective expression of osteopontin in ALS-resistant motor neurons is a critical determinant of late phase neurodegeneration mediated by matrix metalloproteinase-9. Sci Rep 6:27354. https://doi.org/10.1038/srep27354 · DOI
- Lorenzl S, Narr S, Angele B, Krell HW, Gregorio J, Kiaei M, Pfister HW, Beal MF (2006) The matrix metalloproteinases inhibitor Ro 28-2653 [correction of Ro 26-2853] extends survival in transgenic ALS mice. Exp Neurol 200(1):166–171. https://doi.org/10.1016/j.expneurol.2006.01.026 · DOI · Paper page
- Vaz AR, Cunha C, Gomes C, Schmucki N, Barbosa M, Brites D (2015) Glycoursodeoxycholic acid reduces matrix metalloproteinase-9 and caspase-9 activation in a cellular model of superoxide dismutase-1 neurodegeneration. Mol Neurobiol 51(3):864–877. https://doi.org/10.1007/s12035-014-8731-8 · DOI
- Spiller KJ, Khan T, Dominique MA, Restrepo CR, Cotton-Samuel D, Levitan M, Jafar-Nejad P, Zhang B, Soriano A, Rigo F, Trojanowski JQ, Lee VM (2019) Reduction of matrix metalloproteinase 9 (MMP-9) protects motor neurons from TDP-43-triggered death in rNLS8 mice. Neurobiol Dis 124:133–140. https://doi.org/10.1016/j.nbd.2018.11.013 · DOI
- Soon CP, Crouch PJ, Turner BJ, McLean CA, Laughton KM, Atkin JD, Masters CL, White AR, Li QX (2010) Serum matrix metalloproteinase-9 activity is dysregulated with disease progression in the mutant SOD1 transgenic mice. Neuromusc Disord 20(4):260–266. https://doi.org/10.1016/j.nmd.2009.11.015 · DOI
- Izrael M, Slutsky SG, Admoni T, Cohen L, Granit A, Hasson A, Itskovitz-Eldor J, Krush Paker L, Kuperstein G, Lavon N, Yehezkel Ionescu S, Solmesky LJ, Zaguri R, Zhuravlev A, Volman E, Chebath J, Revel M (2018) Safety and efficacy of human embryonic stem cell-derived astrocytes following intrathecal transplantation in SOD1(G93A) and NSG animal models. Stem Cell Res Ther 9(1):152. https://doi.org/10.1186/s13287-018-0890-5 · DOI
- Lee JK, Shin JH, Suh J, Choi IS, Ryu KS, Gwag BJ (2008) Tissue inhibitor of metalloproteinases-3 (TIMP-3) expression is increased during serum deprivation-induced neuronal apoptosis in vitro and in the G93A mouse model of amyotrophic lateral sclerosis: a potential modulator of Fas-mediated apoptosis. Neurobiol Dis 30(2):174–185. https://doi.org/10.1016/j.nbd.2008.01.004 · DOI
- Lim GP, Backstrom JR, Cullen MJ, Miller CA, Atkinson RD, Tokes ZA (1996) Matrix metalloproteinases in the neocortex and spinal cord of amyotrophic lateral sclerosis patients. J Neurochem 67(1):251–259 · DOI
- Beuche W, Yushchenko M, Mader M, Maliszewska M, Felgenhauer K, Weber F (2000) Matrix metalloproteinase-9 is elevated in serum of patients with amyotrophic lateral sclerosis. NeuroReport 11(16):3419–3422 · DOI
- Fang L, Huber-Abel F, Teuchert M, Hendrich C, Dorst J, Schattauer D, Zettlmeissel H, Wlaschek M, Scharffetter-Kochanek K, Tumani H, Ludolph AC, Brettschneider J (2009) Linking neuron and skin: matrix metalloproteinases in amyotrophic lateral sclerosis (ALS). J Neurol Sci 285(1–2):62–66. https://doi.org/10.1016/j.jns.2009.05.025 · DOI
- Niebroj-Dobosz I, Janik P, Sokolowska B, Kwiecinski H (2010) Matrix metalloproteinases and their tissue inhibitors in serum and cerebrospinal fluid of patients with amyotrophic lateral sclerosis. Eur J Neurol 17(2):226–231. https://doi.org/10.1111/j.1468-1331.2009.02775.x · DOI
- Liu Y, Hao W, Dawson A, Liu S, Fassbender K (2009) Expression of amyotrophic lateral sclerosis-linked SOD1 mutant increases the neurotoxic potential of microglia via TLR2. J Biol Chem 284(6):3691–3699. https://doi.org/10.1074/jbc.M804446200 · DOI
- Lee JK, Shin JH, Gwag BJ, Choi EJ (2015) Iron accumulation promotes TACE-mediated TNF-alpha secretion and neurodegeneration in a mouse model of ALS. Neurobiol Dis 80:63–69. https://doi.org/10.1016/j.nbd.2015.05.009 · DOI
- Lemarchant S, Pomeshchik Y, Kidin I, Karkkainen V, Valonen P, Lehtonen S, Goldsteins G, Malm T, Kanninen K, Koistinaho J (2016) ADAMTS-4 promotes neurodegeneration in a mouse model of amyotrophic lateral sclerosis. Mol Neurodegener 11:10. https://doi.org/10.1186/s13024-016-0078-3 · DOI
- DiFiglia M, Sapp E, Chase KO, Davies SW, Bates GP, Vonsattel JP, Aronin N (1997) Aggregation of huntingtin in neuronal intranuclear inclusions and dystrophic neurites in brain. Science 277(5334):1990–1993 · DOI · Paper page
- Sapp E, Schwarz C, Chase K, Bhide PG, Young AB, Penney J, Vonsattel JP, Aronin N, DiFiglia M (1997) Huntingtin localization in brains of normal and Huntington’s disease patients. Ann Neurol 42(4):604–612. https://doi.org/10.1002/ana.410420411 · DOI
- Wheeler VC, White JK, Gutekunst CA, Vrbanac V, Weaver M, Li XJ, Li SH, Yi H, Vonsattel JP, Gusella JF, Hersch S, Auerbach W, Joyner AL, MacDonald ME (2000) Long glutamine tracts cause nuclear localization of a novel form of huntingtin in medium spiny striatal neurons in HdhQ92 and HdhQ111 knock-in mice. Hum Mol Genet 9(4):503–513 · DOI
- Wellington CL, Singaraja R, Ellerby L, Savill J, Roy S, Leavitt B, Cattaneo E, Hackam A, Sharp A, Thornberry N, Nicholson DW, Bredesen DE, Hayden MR (2000) Inhibiting caspase cleavage of huntingtin reduces toxicity and aggregate formation in neuronal and nonneuronal cells. J Biol Chem 275(26):19831–19838. https://doi.org/10.1074/jbc.M001475200 · DOI
- Hermel E, Gafni J, Propp SS, Leavitt BR, Wellington CL, Young JE, Hackam AS, Logvinova AV, Peel AL, Chen SF, Hook V, Singaraja R, Krajewski S, Goldsmith PC, Ellerby HM, Hayden MR, Bredesen DE, Ellerby LM (2004) Specific caspase interactions and amplification are involved in selective neuronal vulnerability in Huntington’s disease. Cell Death Diff 11(4):424–438. https://doi.org/10.1038/sj.cdd.4401358 · DOI
- Gafni J, Hermel E, Young JE, Wellington CL, Hayden MR, Ellerby LM (2004) Inhibition of calpain cleavage of huntingtin reduces toxicity: accumulation of calpain/caspase fragments in the nucleus. J Biol Chem 279(19):20211–20220. https://doi.org/10.1074/jbc.M401267200 · DOI
- Miller JP, Holcomb J, Al-Ramahi I, de Haro M, Gafni J, Zhang N, Kim E, Sanhueza M, Torcassi C, Kwak S, Botas J, Hughes RE, Ellerby LM (2010) Matrix metalloproteinases are modifiers of huntingtin proteolysis and toxicity in Huntington’s disease. Neuron 67(2):199–212. https://doi.org/10.1016/j.neuron.2010.06.021 · DOI
- Naphade S, Embusch A, Madushani KL, Ring KL, Ellerby LM (2017) Altered expression of matrix metalloproteinases and their endogenous inhibitors in a human isogenic stem cell model of Huntington’s disease. Front Neurosci 11:736. https://doi.org/10.3389/fnins.2017.00736 · DOI
- Silvestroni A, Faull RL, Strand AD, Moller T (2009) Distinct neuroinflammatory profile in post-mortem human Huntington’s disease. NeuroReport 20(12):1098–1103. https://doi.org/10.1097/WNR.0b013e32832e34ee · DOI
- Chang KH, Wu YR, Chen YC, Chen CM (2015) Plasma inflammatory biomarkers for Huntington’s disease patients and mouse model. Brain Behav Immun 44:121–127. https://doi.org/10.1016/j.bbi.2014.09.011 · DOI
- Connolly C, Magnusson-Lind A, Lu G, Wagner PK, Southwell AL, Hayden MR, Bjorkqvist M, Leavitt BR (2016) Enhanced immune response to MMP3 stimulation in microglia expressing mutant huntingtin. Neuroscience 325:74–88. https://doi.org/10.1016/j.neuroscience.2016.03.031 · DOI
- Duran-Vilaregut J, del Valle J, Manich G, Camins A, Pallas M, Vilaplana J, Pelegri C (2011) Role of matrix metalloproteinase-9 (MMP-9) in striatal blood-brain barrier disruption in a 3-nitropropionic acid model of Huntington’s disease. Neuropathol Appl Neuro 37(5):525–537. https://doi.org/10.1111/j.1365-2990.2010.01157.x · DOI
- Vinther-Jensen T, Bornsen L, Budtz-Jorgensen E, Ammitzboll C, Larsen IU, Hjermind LE, Sellebjerg F, Nielsen JE (2016) Selected CSF biomarkers indicate no evidence of early neuroinflammation in Huntington disease. Neurol Neuroimmun Neuroinfln 3(6):e287. https://doi.org/10.1212/NXI.0000000000000287 · DOI
- Lo Sardo V, Zuccato C, Gaudenzi G, Vitali B, Ramos C, Tartari M, Myre MA, Walker JA, Pistocchi A, Conti L, Valenza M, Drung B, Schmidt B, Gusella J, Zeitlin S, Cotelli F, Cattaneo E (2012) An evolutionary recent neuroepithelial cell adhesion function of huntingtin implicates ADAM10-Ncadherin. Nat Neurosci 15(5):713–721. https://doi.org/10.1038/nn.3080 · DOI
Cited by
Sorted by citations
Matrix Metalloproteinases as New Targets in Alzheimer’s Disease: Opportunities and Challenges
Zipfel, P., Rochais, C., Baranger, K., Rivera, S., & Dallemagne, P. (2020) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.0c00352 · Cited by 94
Self-citationGarcía-González, L., Pilat, D., Baranger, K., & Rivera, S. (2019) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2019.00244 · Cited by 88
Self-citationPilat, D., Paumier, J.-M., García-González, L., Louis, L., Stephan, D., Manrique, C., Khrestchatisky, M., Di Pasquale, E., Baranger, K., & Rivera, S. (2022) · Journal of Neuroinflammation · doi:10.1186/s12974-022-02407-z · Cited by 28
Self-citation
Metadata
- Authors
- Rivera, S., García-González, L., Khrestchatisky, M., & Baranger, K.
- ORCID
- Rivera, Santiago
- Venue
- Cellular and Molecular Life Sciences
- Published
- 2019-06-13
- Volume
- 76
- Issue
- 16
- Pages
- 3167-3191
- ISSN
- 1420-682X
- 1420-9071
- Cited by
- 111
- References
- 32
- Language
- en
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review