Matrix metalloproteinase-9 (MMP-9) is synthesized in neurons of the human hippocampus and is capable of degrading the amyloid-β peptide (1–40).
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We reported earlier that the levels of Ca 2+ -dependent metalloproteinases are increased in Alzheimer’s disease (AD) specimens, relative to control specimens. Here we show that these enzymes are forms of the matrix metalloproteinase MMP-9 (EC 3.4.24.35 ) and are expressed in the human hippocampus. Affinity-purified antibodies to MMP-9 labeled pyramidal neurons, but not granular neurons or glial cells. MMP-9 mRNA is expressed in pyramidal neurons, as determined with digoxigenin-labeled MMP-9 riboprobes, and the presence of this mRNA is confirmed with reverse transcriptase PCR. The cellular distribution of MMP-9 is altered in AD because 76% of the total 100 kDa enzyme activity is found in the soluble fraction of control specimens, whereas only 51% is detectable in the same fraction from AD specimens. The accumulated 100 kDa enzyme from AD brain is latent and can be converted to an active form with aminophenylmercuric acetate. MMP-9 also is detected in close proximity to extracellular amyloid plaques. Because a major constituent of plaques is the 4 kDa β-amyloid peptide, synthetic Aβ 1–40 was incubated with activated MMP-9. The enzyme cleaves the peptide at several sites, predominantly at Leu 34 -Met 35 within the membrane-spanning domain. These results establish that neurons have the capacity to synthesize MMP-9, which, on activation, may degrade extracellular substrates such as β-amyloid. Because the latent form of MMP-9 accumulates in AD brain, it is hypothesized that the lack of enzyme activation contributes to the accumulation of insoluble β-amyloid peptides in plaques.
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A number of CNS diseases exhibit dysregulated expression of enzymes necessary for PNN cleavage and reorganization.
“In parallel, a number of these CNS diseases exhibit dysregulated expression of enzymes necessary for PNN cleavage and reorganization (Backstrom et al., 1996; Lorenzl et al., 2003; Rybakowski et al., 2009; Kim et al., 2009; Zhang et al., 2011; Yamamori et al., 2013; Liu et al., 2014; Rankin-Gee et al., 2015; Lepeta et al., 2017).”
From The Perineuronal ‘Safety’ Net? Perineuronal Net Abnormalities in Neurological Disorders (2018) · cites this paper as Backstrom et al., 1996
Plasma levels of MMP-9 are elevated in AD patients.
“plasma levels of MMP-9 are elevated in AD patients (Backstrom et al., 1996; Lorenzl et al., 2003).”
From The Perineuronal ‘Safety’ Net? Perineuronal Net Abnormalities in Neurological Disorders (2018) · cites this paper as Backstrom et al., 1996
MMP-9 is capable of cleaving Aβ in vitro.
“MMP-9 is capable of cleaving Aβ in vitro (Backstrom et al., 1996)”
From The Perineuronal ‘Safety’ Net? Perineuronal Net Abnormalities in Neurological Disorders (2018) · cites this paper as Backstrom et al., 1996
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Increased plasma levels of matrix metalloproteinase-9 in patients with Alzheimer’s disease.
Lorenzl, S. (2003) · Neurochemistry International · doi:10.1016/s0197-0186(03)00004-4 · Cited by 243 · see citing works
The Neurotoxicity of Tissue Plasminogen Activator?
Kaur, J., Zhao, Z., Klein, G., Lo, E. H., & Buchan, A. M. (2004) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1097/01.wcb.0000137868.50767.e8 · Cited by 242 · see citing works
“These results are indicative that the plasmin/plasminogen system can have opposing effects both in the CNS and vasculature (Gingrich and Traynelis, 2000).”
BackgroundInfluentialPérez, A., Morelli, L., Cresto, J. C., & Castaño, E. M. (2000) · Neurochemical Research · doi:10.1023/a:1007527721160 · Cited by 240 · see citing works
“Several well-characterized proteases have been reported to degrade A β in vivo or in vitro, including MMP-2 (7), MMP-9 (9), lysosomal cathepsin D (11) and neutral endopeptidase (10).”
BackgroundInfluentialProteolytic Cleavage of Extracellular Secreted α-Synuclein via Matrix Metalloproteinases
Sung, J. Y., Park, S., Lee, C.-H., Um, J. W., Lee, H. J., Kim, J., Oh, Y. J., Lee, S., Paik, S. R., & Chung, K. C. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m503341200 · Cited by 238 · see citing works
Planas, A. M., Solé, S., & Justicia, C. (2001) · Neurobiology of Disease · doi:10.1006/nbdi.2001.0435 · Cited by 231 · see citing works
Metabolism of amyloid-β peptide and Alzheimer's disease
Iwata, N., Higuchi, M., & Saido, T. C. (2005) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2005.03.010 · Cited by 216 · see citing works
Gelatinase B/MMP-9 in Tumour Pathogenesis and Progression
Farina, A., & Mackay, A. (2014) · Cancers · doi:10.3390/cancers6010240 · Cited by 213 · see citing works
Alpha-secretase in Alzheimer’s disease: molecular identity, regulation and therapeutic potential
Lichtenthaler, S. F. (2010) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2010.07081.x · Cited by 207 · see citing works
Brkic, M., Balusu, S., Libert, C., & Vandenbroucke, R. E. (2015) · Mediators of Inflammation · doi:10.1155/2015/620581 · Cited by 205 · see citing works
The Role of Microglia and Matrix Metalloproteinases Involvement in Neuroinflammation and Gliomas
Könnecke, H., & Bechmann, I. (2013) · Clinical and Developmental Immunology · doi:10.1155/2013/914104 · Cited by 199 · see citing works
Milardi, D., Gazit, E., Radford, S. E., Xu, Y., Gallardo, R. U., Caflisch, A., Westermark, G. T., Westermark, P., Rosa, C. L., & Ramamoorthy, A. (2021) · Chemical Reviews · doi:10.1021/acs.chemrev.0c00981 · Cited by 199 · see citing works
Donnelly, P. S., Caragounis, A., Du, T., Laughton, K. M., Volitakis, I., Cherny, R. A., Sharples, R. A., Hill, A. F., Li, Q., Masters, C. L., et al. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m705957200 · Cited by 196 · see citing works
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“…AD patients, an increase in MMP-9 expression is detected in neurons, neurofibrillary tangles, senile plaques and plasma but not in CSF, while also here, MMP-2 levels are unchanged in CSF, plasma or brain (Adair et al., 2004; Asahina et al., 2001; Backstrom et al., 1992, 1996; Lorenzl et al., 2003).”
Behl, T., Kaur, G., Sehgal, A., Bhardwaj, S., Singh, S., Buhaș, C. L., Pusta, C. T. J., Uivaroșan, D., Munteanu, M. A., & BUNGAU, S. G. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22031413 · Cited by 192 · see citing works
Are amyloid‐degrading enzymes viable therapeutic targets in Alzheimer’s disease?
Nalivaeva, N., Beckett, C. S., Belyaev, N. D., & Turner, A. J. (2012) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2011.07510.x · Cited by 178 · see citing works
“…and, of these, MMP-2, -3, -6 and -9 have been reported to degrade Ab1-40, although most attention has focused on MMP-2 (gelatinase A) (Roher et al. 1994) and MMP-9 (gelatinase B) (Backstrom et al. 1996), which can also degrade the fibrillar form of Ab, as well as compact plaques (Yan et al. 2006).”
BackgroundCorona, C., Masciopinto, F., Silvestri, E., Viscovo, A. D., Lattanzio, R., Sorda, R. L., Ciavardelli, D., Goglia, F., Piantelli, M., Canzoniero, L. M. T., et al. (2010) · Cell Death and Disease · doi:10.1038/cddis.2010.73 · Cited by 189 · see citing works
β ‐Amyloid Degradation and Alzheimer′s Disease
Wang, D.-S., Dickson, D. W., & Malter, J. S. (2006) · BioMed Research International · doi:10.1155/jbb/2006/58406 · Cited by 185 · see citing works
“These include neprilysin (NEP) [14– 16], endothelin-converting enzyme (ECE)-1 [17], insulindegrading enzyme (IDE) [18–20], angiotensin-converting enzyme (ACE) [21], uPA/tPA-plasmin system [22, 23], cathepsin D [24, 25], gelatinase A [26], gelatinase B [27], matrix metalloendopeptidase-9 [28], coagulation factor XIa [2…”
BackgroundThe Perineuronal ‘Safety’ Net? Perineuronal Net Abnormalities in Neurological Disorders
Wen, T. H., Binder, D. K., Ethell, I. M., & Razak, K. A. (2018) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2018.00270 · Cited by 170 · see citing works
“Interestingly, some studies suggest that MMP-9 may be a key molecular target in treating AD, as MMP-9 is capable of cleaving Aβ in vitro (Backstrom et al., 1996), and plasma levels of MMP-9 are elevated in AD patients (Backstrom et al., 1996; Lorenzl et al., 2003).”
BackgroundWalker, D. G., Link, J., Lue, L., Dalsing-Hernandez, J. E., & Boyes, B. E. (2005) · Journal of Leukocyte Biology · doi:10.1189/jlb.0705377 · Cited by 180 · see citing works
Patel, J. P., & Frey, B. N. (2015) · Neural Plasticity · doi:10.1155/2015/708306 · Cited by 182 · see citing works
Jourquin, J., Tremblay, E., Décanis, N., Charton, G., Hanessian, S., Chollet, A., Le Diguardher, T., Khrestchatisky, M., & Rivera, S. (2003) · European Journal of Neuroscience · doi:10.1046/j.1460-9568.2003.02876.x · Cited by 178 · see citing works
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 · see citing works
“Further, matrix metalloproteinase 9, which is a target of TIMP inhibition, has been reported to be upregulated in plasma of AD patients [23] and has been implicated in the degradation of toxic β-amyloid species [2].”
BackgroundRegulation of Matrix Metalloproteinase Gene Expression
Fini, M. E., Cook, J. R., Mohan, R., & Brinckerhoff, C. (1998) · Elsevier eBooks · doi:10.1016/b978-012545090-4/50013-6 · Cited by 177 · see citing works
Gelatinase B: Structure, Regulation, and Function
Vu, T. H., & Werb, Z. (1998) · Elsevier eBooks · doi:10.1016/b978-012545090-4/50006-9 · Cited by 174 · see citing works
Miners, J. S., Ashby, E., Helmond, Z. V., Chalmers, K. A., Palmer, L. E., Love, S., & Kehoe, P. G. (2007) · Neuropathology and Applied Neurobiology · doi:10.1111/j.1365-2990.2007.00885.x · Cited by 165 · see citing works
Localization and Regulation of the Tissue Plasminogen Activator–Plasmin System in the Hippocampus
Sallés, F. J., & Strickland, S. (2002) · Journal of Neuroscience · doi:10.1523/jneurosci.22-06-02125.2002 · Cited by 166 · see citing works
“…synaptic plasticity Extracellular proteases are expressed by neurons in the CNS (Sappino et al., 1993; Chen et al., 1995; Nishibori et al., 1995; Backstrom et al., 1996; Gschwend et al., 1997; Scarisbrick et al., 2001), and their function can vary from potentiating synaptic transmission…”
BackgroundLorenzl, S., Albers, D. S., LeWitt, P., Chirichigno, J. W., Hilgenberg, S. L., Cudkowicz, M., & Beal, M. (2003) · Journal of Neurological Sciences · doi:10.1016/s0022-510x(02)00398-2 · Cited by 162 · see citing works
“One family of proteases, namely matrix metalloproteinases (MMPs), can remodel the extracellular matrix and additionally digest pathologically accumulated extracellular proteins like amyloid [2].”
BackgroundIncreased Matrix Metalloproteinase 9 Activity in Mild Cognitive Impairment
Bruno, M. A., Mufson, E. J., Wuu, J., & Cuello, A. C. (2009) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0b013e3181c22569 · Cited by 163 · see citing works
“Matrix metalloproteinase 9 induces amyloid-A peptides (AA) (14, 15), degrades amyloid A (16, 17) and compact plaques (18), and is released, along with proNGF, in an activitydependent manner (10).”
MMP-9 triggered self-assembly of doxorubicin nanofiber depots halts tumor growth.
Kalafatovic, D., Nobis, M., Son, J., Anderson, K., & Ulijn, R. (2016) · Biomaterials · doi:10.1016/j.biomaterials.2016.04.039 · Cited by 140 · see citing works
Miners, J. S., Helmond, Z. V., Chalmers, K. A., Wilcock, G. K., Love, S., & Kehoe, P. G. (2006) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/01.jnen.0000240463.87886.9a · Cited by 153 · see citing works
Wright, J. W., & Harding, J. W. (2004) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2004.03.003 · Cited by 156 · see citing works
Rivera, S., Ogier, C., Jourquin, J., Timsit, S., Szklarczyk, A., Miller, K., Gearing, A. J. H., Kaczmarek, L., & Khrestchatisky, M. (2002) · European Journal of Neuroscience · doi:10.1046/j.0953-816x.2001.01838.x · Cited by 152 · see citing works
Alzheimer’s disease: How metal ions define β-amyloid function
Kepp, K. P. (2017) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2017.05.007 · Cited by 151 · see citing works
Lee, K., Kim, J., Seo, J., Kim, T., Im, J., Baek, I., Kim, K., Lee, J., & Han, P. (2008) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2008.05769.x · Cited by 145 · see citing works
DeLeve, L. D., Wang, X., Tsai, J., Kanel, G. C., Strasberg, S. M., & Tökés, Z. A. (2003) · Gastroenterology · doi:10.1016/s0016-5085(03)01056-4 · Cited by 144 · see citing works
Self-citationSequential Amyloid-β Degradation by the Matrix Metalloproteases MMP-2 and MMP-9*
Hernández-Guillamon, M., Mawhirt, S., Blais, S., Montaner, J., Neubert, T., Rostagno, A., & Ghiso, J. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.610931 · Cited by 110 · see citing works
The TIMPs tango with MMPs and more in the central nervous system
Crocker, S. J., Pagenstecher, A., & Campbell, I. L. (2003) · Journal of Neuroscience Research · doi:10.1002/jnr.10836 · Cited by 134 · see citing works
“…proteolysis regulated by TIMPs may participate in other pathological changes in AD, including neurite outgrowth though the mobilization of growth factors from the ECM (McFarlane, 2003) and formation of amyloid plaques and fibrillary tangles in AD (Peress et al., 1995; Backstrom et al., 1996).”
BackgroundKauwe, J. S. K., Bailey, M. H., Ridge, P. G., Perry, R., Wadsworth, M. E., Hoyt, K. L., Staley, L. A., Karch, C. M., Harari, O., Cruchaga, C., et al. (2014) · PLoS Genetics · doi:10.1371/journal.pgen.1004758 · Cited by 125 · see citing works
“MMP9 can degrade fibrillar Ab in vitro and plaques in hippocampal slice cultures [52,56,57].”
Baranger, K., Marchalant, Y., Bonnet, A., Crouzin, N., Carreté, A., Paumier, J.-M., Py, N., Bernard, A., Bauer, C., Charrat, E., et al. (2015) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-015-1992-1 · Cited by 110 · see citing works
Ward, N. L., & Lamanna, J. C. (2004) · Neurological Research · doi:10.1179/016164104x3798 · Cited by 122 · see citing works
Neuronal death in the central nervous system demonstrates a non-fibrin substrate for plasmin
Tsirka, S. E., Bugge, T. H., Degen, J. L., & Strickland, S. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.18.9779 · Cited by 125 · see citing works
Alzheimer’s disease due to loss of function: A new synthesis of the available data
Kepp, K. P. (2016) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2016.06.004 · Cited by 123 · see citing works
In Sickness and in Health: Perineuronal Nets and Synaptic Plasticity in Psychiatric Disorders
Pantazopoulos, H., & Berretta, S. (2015) · Neural Plasticity · doi:10.1155/2016/9847696 · Cited by 118 · see citing works
Loss of perineuronal net N-acetylgalactosamine in Alzheimer’s disease
Baig, S., Wilcock, G. K., & Love, S. (2005) · Acta Neuropathologica · doi:10.1007/s00401-005-1060-2 · Cited by 112 · see citing works
“Other possible sources of PN-degrading proteases include astrocytes [14, 22, 23, 50, 53] and the neurons themselves [ 3 , 50, 53].”
BackgroundKoronyo‐Hamaoui, M., Ko, M. K., Koronyo, Y., Azoulay, D., Seksenyan, A., Kunis, G., Pham, M. D., Bakhsheshian, J., Rogeri, P. S., Black, K. L., et al. (2009) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2009.06402.x · Cited by 113 · see citing works
Rivera, S., García‐González, L., Khrestchatisky, M., & Baranger, K. (2019) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-019-03178-2 · Cited by 112 · see citing works
Recent therapeutic strategies targeting beta amyloid and tauopathies in Alzheimer's disease
Madav, Y., Wairkar, S., & Prabhakar, B. R. (2019) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2019.01.004 · Cited by 116 · see citing works
Horstmann, S., Budig, L., Gardner, H., Koziol, J. A., Deuschle, M., Schilling, C., & Wagner, S. (2010) · International Psychogeriatrics · doi:10.1017/s1041610210000827 · Cited by 111 · see citing works
“Backstrom et al. argued that the inflammatory protein α1antichymotrypsin, which accumulates in amyloid plaques and which is a known inhibitor of serine proteinases, may prevent activation of MMP-9 and thereby contribute to reduced cleavage of amyloid β (Backstrom et al., 1996).”
BackgroundInfluentialBi, X., Gall, C. M., Zhou, J., & LYNCH, G. S. (2002) · Neuroscience · doi:10.1016/s0306-4522(02)00132-x · Cited by 108 · see citing works
Nagai, T., Yamada, K., Yoshimura, M., Ishikawa, K., Miyamoto, Y., Hashimoto, K., Noda, Y., Nitta, A., & Nabeshima, T. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0306587101 · Cited by 110 · see citing works
Kolb, S., Lahrtz, F., Paul, R. H., Leppert, D., Nadal, D., Pfister, H., & Fontana, A. (1998) · Journal of Neuroimmunology · doi:10.1016/s0165-5728(97)00247-6 · Cited by 110 · see citing works
Stargardt, A., Swaab, D. F., & Bossers, K. (2015) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2014.08.014 · Cited by 109 · see citing works
“In addition to NEP, the matrix metalloproteinase-9 (MMP-9) has received considerable attention for its Ab degrading capacity (Backstrom et al., 1996; Merlo and Sortino, 2012; Yan et al., 2006) and its ability to elevate secreted APPa levels, the product of the nonamyloidogenic pathway of APP processing (Fragkouli et a…”
Zhang, J. W., Deb, S., & Gottschall, P. E. (1998) · European Journal of Neuroscience · doi:10.1046/j.1460-9568.1998.00347.x · Cited by 109 · see citing works
“Because latent forms of MMP-9 accumulate in the brain tissue of Alzheimer’s patients, the lack of enzyme activation has been suggested to contribute to the accumulation of insolubleβ-amyloid peptides in plaques (Backstrom et al., 1996).”
BackgroundSekine‐Aizawa, Y., Hama, E., Watanabe, K., Tsubuki, S., Kanai‐Azuma, M., Kanai, Y., Arai, H., Aizawa, H., Iwata, N., & Saido, T. C. (2001) · European Journal of Neuroscience · doi:10.1046/j.0953-816x.2001.01462.x · Cited by 108 · see citing works
“This possibility follows from studies showing that MMP-2 and MMP-9 proteolyse synthetic Ab peptides (Miyazaki et al., 1993; Backstrom et al., 1996).”
BackgroundStomrud, E., Björkqvist, M., Janciauskiene, S. M., Minthon, L., & Hansson, O. (2010) · Alzheimer s Research & Therapy · doi:10.1186/alzrt44 · Cited by 105 · see citing works
“In light of these possible AD protecting effects of MMP-9, it has been suggested that the increased MMP-9 levels observed in AD might be of the inactive form [2,8,12].”
BackgroundResultInfluentialMorita‐Fujimura, Y., Fujimura, M., Gasche, Y. G., Copin, J., & Chan, P. H. (2000) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1097/00004647-200001000-00017 · Cited by 105 · see citing works
Mohan, R., Rinehart, W. B., Bargagna‐Mohan, P., & Fini, M. E. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.40.25903 · Cited by 99 · see citing works
Imperlini, E., Gnecchi, M., Rognoni, P., Sabidó, E., Ciuffreda, M. C., Palladini, G. O., Espadas, G., Mancuso, F. M., Bozzola, M., Malpasso, G., et al. (2017) · Scientific Reports · doi:10.1038/s41598-017-15424-3 · Cited by 97 · see citing works
Pihlaja, R., Koistinaho, J., Kauppinen, R., Sandholm, J., Tanila, H., & Koistinaho, M. (2011) · Glia · doi:10.1002/glia.21212 · Cited by 96 · see citing works
“Also insulin-degrading enzyme (Kurochin and Goto, 1994; Qiu et al., 1998), plasmin (Tucker et al., 2000), matrix metalloproteases (MMP-2 and -9) (Backstrom et al., 1996; Roher et al., 1994), angiotensin-converting enzyme (ACE) (Hu et al., 2001), and cathepsin D (McDermott and Gibson, 1996) have…”
BackgroundMatrix Metalloproteinases in Non-Neoplastic Disorders
Tokito, A., & Jougasaki, M. (2016) · International Journal of Molecular Sciences · doi:10.3390/ijms17071178 · Cited by 96 · see citing works
“MMP-9 has also been indicated to exert a neuroprotective effect via Aβ clearance, reducing the aggregation of the peptide [140,141].”
BackgroundProfiles of matrix metalloproteinases and their inhibitors in plasma of patients with dementia
Lorenzl, S., Büerger, K., Hampel, H. J., & Beal, M. F. (2007) · International Psychogeriatrics · doi:10.1017/s1041610207005790 · Cited by 96 · see citing works
“MMP-9 is localized to neurons of the hippocampus and is capable of degrading Aβ (Backstrom et al. 1996).”
BackgroundHernández‐Guillamón, M., Martínez-Sáez, E. A., Delgado, P., Domingues‐Montanari, S., Boada, C., Peñalba, A., Boada, M., Pagola, J., Maisterra, O., Rodríguez‐Luna, D., et al. (2011) · Brain Pathology · doi:10.1111/j.1750-3639.2011.00512.x · Cited by 96 · see citing works
“Despite the ability to degrade a range of protein substrates, as certain components of the basal lamina, MMP-2 and MMP-9 can proteolyse different Ab peptides in vitro (4, 7, 10, 20, 32).”
BackgroundLiao, M.-C., & Nostrand, W. V. V. (2010) · Biochemistry · doi:10.1021/bi901994d · Cited by 91 · see citing works
“MMP9, like MT1-MMP, cleaves between residues Ala30-Ile31 (37).”
InfluentialMatrix 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 · see citing works
Ma, Z., Yang, J., Han, J., Gao, L., Liu, H., Lu, Z., Zhao, H., & Bie, X. (2016) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.6b00922 · Cited by 94 · see citing works
The Aluminium-Amyloid Cascade Hypothesis and Alzheimer’s Disease
Exley, C. (2005) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/0-387-23226-5_11 · Cited by 93 · see citing works
Cattaud, V., Bezzina, C., Rey, C. C., Lejards, C., Dahan, L., & Verret, L. (2018) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2018.08.024 · Cited by 88 · see citing works
Mizoguchi, H., Takuma, K., Fukuzaki, E., Ibi, D., Someya, E., Akazawa, K., Alkam, T., Tsunekawa, H., Mouri, A., Noda, Y., et al. (2009) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.109.154724 · Cited by 87 · see citing works
“It is interesting that MMP-9 is increased in the brains of AD patients (Backstrom et al., 1996).”
BackgroundInfluential
- Authors
- Backstrom, J. R., Lim, G. P., Cullen, M. J., & Tökés, Z. A.
- Affiliations
- University of Southern California (US)
- ORCID
- Cullen, Michael J.
- Venue
- The Journal of Neuroscience
- Publisher
- Society for Neuroscience
- Published
- 1996-12-15
- Volume
- 16
- Issue
- 24
- Pages
- 7910-7919
- ISSN
- 0270-6474 (ISSN-L)
- 1529-2401
- OpenAlex
- W4296941341
- Cited by
- 331
- References
- 46
- Citations by year
- 2026: 7 · 2025: 6 · 2024: 9 · 2023: 6 · 2022: 10 · 2021: 16 · 2020: 21 · 2019: 5 · 2018: 13 · 2017: 15 · 2016: 11 · 2015: 18 · 2014: 18 · 2013: 8 · 2012: 12
- FWCI
- 3.67
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Neuroscience (publishedVersion, cc-by-nc-sa)
- Funders
- National Institute on Aging (R01-AG09681)
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Protease and Inhibitor Mechanisms
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Keywords
- MMP-9, Alzheimer's disease, Aβ40, hippocampal pyramidal neurons, MMP-9 mRNA expression, extracellular matrix metalloproteinases, transmembrane domain
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