ADAMTS proteoglycanases in the physiological and pathological central nervous system.

Lemarchant, Sighild; Pruvost, Mathilde; Montaner, Joan; Emery, Evelyne; Vivien, Denis; Kanninen, Katja; Koistinaho, Jari

doi:10.1186/1742-2094-10-133

Cited by 100Proteoglycans and glycosaminoglycans researchProtease and Inhibitor MechanismsNeuroinflammation and Neurodegeneration Mechanisms

ADAMTS proteoglycanases in the physiological and pathological central nervous system.

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Lemarchant, Sighild, Pruvost, Mathilde, Montaner, Joan, Emery, Evelyne, Vivien, Denis, Kanninen, Katja, Koistinaho, Jari·2013·Journal of Neuroinflammation

DOI 10.1186/1742-2094-10-133PMC PMC4228433

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Abstract

ADAMTS-1, -4, -5 and -9 belong to 'a disintegrin and metalloproteinase with thrombospondin motifs (ADAMTS)' family and more precisely to the proteoglycanases subgroup based on their common ability to degrade chondroitin sulfate proteoglycans. They have been extensively investigated for their involvement in inflammation-induced osteoarthritis, and a growing body of evidence indicates that they may be of key importance in the physiological and pathological central nervous system (CNS). In this review, we discuss the deregulated expression of ADAMTS proteoglycanases during acute CNS injuries, such as stroke and spinal cord injury. Then, we provide new insights on ADAMTS proteoglycanases mediating synaptic plasticity, neurorepair, angiogenesis and inflammation mechanisms. Altogether, this review allows us to propose that ADAMTS proteoglycanases may be original therapeutic targets for CNS injuries.

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Several ADAMTs are upregulated following spinal cord injury, stroke, and epilepsy.
“several ADAMTs are upregulated following spinal cord injury, stroke, and epilepsy (Lemarchant et al., 2013; Kim et al., 2016).”
From The Perineuronal ‘Safety’ Net? Perineuronal Net Abnormalities in Neurological Disorders (2018) · cites this paper as Lemarchant et al., 2013
Aggrecanases (ADAMTS-1, 4, 8, 15) and neprilysin are further candidate enzymes for stroke-induced degradation of net components.
“Further candidates for the stroke-induced degradation of net components are aggrecanases, e.g., disintegrin and metalloproteinase with thrompospondin motifs (ADAMTS-1, 4, 8 and 15) and neprilysin (Cross et al., 2006; Lemarchant et al., 2013; Levy et al., 2015; Rossier et al., 2015).”
From Damaged Neocortical Perineuronal Nets Due to Experimental Focal Cerebral Ischemia in Mice, Rats and Sheep (2017) · cites this paper as Lemarchant et al., 2013

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Background
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Background
A disintegrin-like and metalloprotease (reprolysin type) with thrombospondin type 1 motifs: the ADAMTS family
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Background
Chondroitin sulfate proteoglycans in demyelinated lesions impair remyelination
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Background
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Background
The Thrombospondin Motif of Aggrecanase-1 (ADAMTS-4) Is Critical for Aggrecan Substrate Recognition and Cleavage
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Background
ADAMTS4 (Aggrecanase-1) Activation on the Cell Surface Involves C-terminal Cleavage by Glycosylphosphatidyl Inositol-anchored Membrane Type 4-Matrix Metalloproteinase and Binding of the Activated Proteinase to Chondroitin Sulfate and Heparan Sulfate on Syndecan-1
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Background
Renal ischemia reperfusion inhibits VEGF expression and induces ADAMTS-1, a novel VEGF inhibitor
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“Both proteinase-dependent and independent antiangiogenic functions for most of the ADAMTS proteases, including proteoglycanases, have been described [42-45].”
Background
Regeneration of Axons after Nerve Transection Repair Is Enhanced by Degradation of Chondroitin Sulfate Proteoglycan
Zuo, J., Neubauer, D., Graham, J. B., Krekoski, C. A., Ferguson, T. A., & Muir, D. (2002) · Experimental Neurology · doi:10.1006/exnr.2002.7922 · Cited by 158 · cited 1× · see citing works
“The inhibition of CSPGs can be relieved by the bacterial enzyme chondroitinase ABC which removes the chondroitin sulfate chains from the core proteins, thus promoting axonal regeneration/collateral sprouting of a wide variety of neuron tracts and functional recovery after stroke or SCI [49-57].”
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The inhibitory effects of chondroitin sulfate proteoglycans on oligodendrocytes
Siebert, J. R., & Osterhout, D. J. (2011) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2011.07370.x · Cited by 158 · cited 1× · see citing works
“Interestingly, chondroitinase ABC can prevent CSPGs-inhibition of remyelination in vitro and in vivo after contusion-induced SCI in rats and in a lysolecithininduced demyelination model in mice [47,48,59].”
Background
Characterization of METH-1/ADAMTS1 Processing Reveals Two Distinct Active Forms
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Autocatalytic Cleavage of ADAMTS-4 (Aggrecanase-1) Reveals Multiple Glycosaminoglycan-binding Sites
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“When secreted, ADAMTS proteases are capable of binding ECM components via their thrombospondin motifs [3], which can be then cleaved by the metalloproteinase domain.”
Background
Combining Peripheral Nerve Grafts and Chondroitinase Promotes Functional Axonal Regeneration in the Chronically Injured Spinal Cord
Tom, V. J., Sandrow-Feinberg, H. R., Miller, K., Santi, L., Connors, T. M., Lemay, M. A., & Houlé, J. D. (2009) · Journal of Neuroscience · doi:10.1523/jneurosci.3641-09.2009 · Cited by 141 · cited 1× · see citing works
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Background
Cleavage of the ADAMTS13 Propeptide Is Not Required for Protease Activity
Majerus, E. M., Zheng, X. L., Tuley, E. A., & Sadler, J. E. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m309872200 · Cited by 129 · cited 1× · see citing works
“Prepro-ADAMTS proteases can be cleaved by furin or furinlike proteases at the N- and C-terminal positions triggering, respectively, their activity and their future location within the extracellular matrix (ECM) via the removal of the prodomain, and their substrate specificity [3-11].”
Background
Differential regulation of matrix degrading enzymes in a TNFα-induced model of nucleus pulposus tissue degeneration
Séguin, C. A., Bojarski, M., Pilliar, R. M., Roughley, P. J., & Kandel, R. A. (2006) · Matrix Biology · doi:10.1016/j.matbio.2006.07.002 · Cited by 124 · cited 1× · see citing works
“proteoglycanases in non-CNS cell types [28-31].”
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Background
Proprotein Convertase Furin Interacts with and Cleaves Pro-ADAMTS4 (Aggrecanase-1) in the trans-Golgi Network
Wang, P., Tortorella, M. D., England, K. A., Malfait, A., Thomas, G., Arner, E. C., & Pei, D. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m312797200 · Cited by 122 · cited 1× · see citing works
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Background
ADAMTS-4 and -8 are inflammatory regulated enzymes expressed in macrophage-rich areas of human atherosclerotic plaques
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“ADAMTS-4 is increased during the differentiation of human monocytes into macrophages in vitro [37] and is required for macrophages invasion in vitro [38].”
BackgroundInfluential
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BackgroundInfluential
Adamts9 is widely expressed during mouse embryo development
Jungers, K. A., Goff, C. L., Somerville, R. P. T., & Apte, S. (2005) · Gene Expression Patterns · doi:10.1016/j.modgep.2005.03.004 · Cited by 108 · cited 1× · see citing works
“ADAMTS proteoglycanases are present in several CNS structures, including the cortex, the hippocampus, the striatum and the spinal cord [16-21].”
Background
ADAMTS4 (aggrecanase-1) cleaves human brain versican V2 at Glu405-Gln406 to generate glial hyaluronate binding protein
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Extracellular Protease ADAMTS9 Suppresses Esophageal and Nasopharyngeal Carcinoma Tumor Formation by Inhibiting Angiogenesis
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“Although the degradation of the PNNs occurred predominantly in the lesion core and was associated with the invasion of monocytes/macrophages, the transient reduction of neurons containing PNNs in the periischemic area or the contralateral hemisphere is more likely associated with an attempt at neurorepair [49].”
Background
Intracerebral chondroitinase ABC and heparan sulfate proteoglycan glypican improve outcome from chronic stroke in rats
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“The inhibition of CSPGs can be relieved by the bacterial enzyme chondroitinase ABC which removes the chondroitin sulfate chains from the core proteins, thus promoting axonal regeneration/collateral sprouting of a wide variety of neuron tracts and functional recovery after stroke or SCI [49-57].”
Background
Functional evolution of ADAMTS genes: Evidence from analyses of phylogeny and gene organization
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“based on their preference to cleave specific ECM macromolecules as follows [12-14]: proteoglycans (ADAMTS-1, -4, -5, -8, -9, -15 and -20), pro-collagens (ADAMTS-2, -3 and -14) or the von Willebrand factor (ADAMTS-13).”
Background
The role of ADAMTSs in arthritis
Lin, E. A., & Liu, C.-J. (2010) · Protein & Cell · doi:10.1007/s13238-010-0002-5 · Cited by 95 · cited 1× · see citing works
“Prepro-ADAMTS proteases can be cleaved by furin or furinlike proteases at the N- and C-terminal positions triggering, respectively, their activity and their future location within the extracellular matrix (ECM) via the removal of the prodomain, and their substrate specificity [3-11].”
Background
Novel Role of ADAMTS-5 Protein in Proteoglycan Turnover and Lipoprotein Retention in Atherosclerosis
Didangelos, A., Mayr, U., Monaco, C. G., & Mayr, M. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.c112.350785 · Cited by 93 · cited 1× · see citing works
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Background
Identification and Characterization of ADAMTS-20 Defines a Novel Subfamily of Metalloproteinases-Disintegrins with Multiple Thrombospondin-1 Repeats and a Unique GON Domain
Prada, M. L., Cal, S., Quesada, V., & López-Otı́n, C. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m211900200 · Cited by 93 · cited 1× · see citing works
“based on their preference to cleave specific ECM macromolecules as follows [12-14]: proteoglycans (ADAMTS-1, -4, -5, -8, -9, -15 and -20), pro-collagens (ADAMTS-2, -3 and -14) or the von Willebrand factor (ADAMTS-13).”
Background
Regulated Proteolytic Processing of Reelin through Interplay of Tissue Plasminogen Activator (tPA), ADAMTS-4, ADAMTS-5, and Their Modulators
Krstic, D., Rodríguez, M. E., & Knuesel, I. (2012) · PLoS ONE · doi:10.1371/journal.pone.0047793 · Cited by 92 · cited 3× · see citing works
“Recently, Krstic and collaborators (2012) proposed ADAMTS-4 and ADAMTS-5 as proteases capable of cleaving Reelin, an extracellular molecule also involved in neurodevelopment and in synaptic plasticity induced learning and memory processes [20].”
Background
The endogenous proteoglycan-degrading enzyme ADAMTS-4 promotes functional recovery after spinal cord injury
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Chondroitinase treatment following spinal contusion injury increases migration of oligodendrocyte progenitor cells
Siebert, J. R., Stelzner, D. J., & Osterhout, D. J. (2011) · Experimental Neurology · doi:10.1016/j.expneurol.2011.05.002 · Cited by 89 · cited 2× · see citing works
“Neurorepair including neuroregeneration and remyelination is compromised in the chronic phase of stroke or SCI partly because of an overexpression of CSPGs [47,48].”
Background
Overcoming neurite‐inhibitory chondroitin sulfate proteoglycans in the astrocyte matrix
Cua, R. C., Lau, L. W., Keough, M. B., Midha, R., Apte, S., & Yong, V. W. (2013) · Glia · doi:10.1002/glia.22489 · Cited by 87 · cited 2× · see citing works
“While the expression and associated beneficial or deleterious effects of matrix metalloproteinases (MMPs) have been extensively reported in several CNS diseases, recent publications strongly suggest that the ADAMTS proteoglycanases may also be important in ECM proteolysis in CNS injuries.”
Background
Perilesional Treatment with Chondroitinase ABC and Motor Training Promote Functional Recovery After Stroke in Rats
Gherardini, L. M., Gennaro, M., & Pizzorusso, T. (2013) · Cerebral Cortex · doi:10.1093/cercor/bht217 · Cited by 86 · cited 1× · see citing works
“The inhibition of CSPGs can be relieved by the bacterial enzyme chondroitinase ABC which removes the chondroitin sulfate chains from the core proteins, thus promoting axonal regeneration/collateral sprouting of a wide variety of neuron tracts and functional recovery after stroke or SCI [49-57].”
Background
ADAMTS-1 and ADAMTS-4 Levels Are Elevated in Thoracic Aortic Aneurysms and Dissections
Ren, P., Zhang, L., Xu, G., Palmero, L. C., Albini, P. T., Coselli, J. S., Shen, Y. H., & LeMaire, S. A. (2012) · The Annals of Thoracic Surgery · doi:10.1016/j.athoracsur.2012.10.084 · Cited by 84 · see citing works
Comparative gene expression profiling of olfactory ensheathing cells from olfactory bulb and olfactory mucosa
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“Moreover, olfactory ensheathing cell-based therapies promote remyelination after acute injuries [60] and these cells were recently reported to express ADAMTS-4 [61,62].”
Background
ADAMTS5 Functions as an Anti-Angiogenic and Anti-Tumorigenic Protein Independent of Its Proteoglycanase Activity
Kumar, S., Sharghi-Namini, S., Rao, N., & Ge, R. (2012) · American Journal Of Pathology · doi:10.1016/j.ajpath.2012.05.022 · Cited by 74 · cited 1× · see citing works
“Both proteinase-dependent and independent antiangiogenic functions for most of the ADAMTS proteases, including proteoglycanases, have been described [42-45].”
Background
Reactive-site mutants of N-TIMP-3 that selectively inhibit ADAMTS-4 and ADAMTS-5: biological and structural implications
Lim, N. H., Kashiwagi, M., Visse, R., Jones, J. S., Enghild, J. J., Brew, K., & Nagase, H. (2010) · Biochemical Journal · doi:10.1042/bj20100725 · Cited by 69 · cited 1× · see citing works
“A combination approach may represent an attractive therapeutic opportunity: first, the administration of an inhibitor of ADAMTS proteoglycanases activity, such as TIMP-3 (tissue inhibitor of metalloproteinases-3) [63], or an inhibitor of their synthesis, such as the antiinflammatory compound WIN-34B [29], in the acute…”
Background
ADAMTS-1 and -4 are up-regulated following transient middle cerebral artery occlusion in the rat and their expression is modulated by TNF in cultured astrocytes
Cross, A. K., Haddock, G., Stock, C. J., Allan, S. M., Surr, J., Bunning, R. A. D., Buttle, D. J., & Woodroofe, M. N. (2006) · Brain Research · doi:10.1016/j.brainres.2006.02.136 · Cited by 68 · cited 6× · see citing works
“Primary cerebral cultures (human) [23]: Yes (mRNA/WB/ICC) Yes (mRNA/WB/ICC) Yes (mRNA/WB/ICC)”
BackgroundInfluential
Metalloproteinase ADAMTS-1 but not ADAMTS-5 is manifold overexpressed in neurodegenerative disorders as Down syndrome, Alzheimer's and Pick's disease
Miguel, R. F., Pollak, A., & Lubec, G. (2005) · Molecular Brain Research · doi:10.1016/j.molbrainres.2004.09.008 · Cited by 64 · cited 1× · see citing works
“ADAMTS proteoglycanases are present in several CNS structures, including the cortex, the hippocampus, the striatum and the spinal cord [16-21].”
Background
Multimodal signaling by the ADAMTSs (a disintegrin and metalloproteinase with thrombospondin motifs) promotes neurite extension
Hamel, M. G., Ajmo, J. M., Leonardo, C. C., Zuo, F., Sandy, J. D., & Gottschall, P. E. (2007) · Experimental Neurology · doi:10.1016/j.expneurol.2007.11.014 · Cited by 60 · cited 2× · see citing works
“Hamel and collaborators (2008) reported that a recombinant active ADAMTS-4 can promote neurite growth of cortical neurons in vitro dependently or independently of its proteolytic activity as described above [26].”
Background
Regulation of ADAMTS-1, -4 and -5 expression in human macrophages: Differential regulation by key cytokines implicated in atherosclerosis and novel synergism between TL1A and IL-17
Ashlin, T. G., Kwan, A. P. L., & Ramji, D. P. (2013) · Cytokine · doi:10.1016/j.cyto.2013.06.315 · Cited by 57 · cited 6× · see citing works
“- IFN-ɣ treatment [36,37] ↓ mRNA stable/↑ mRNA stable mRNA ↑ mRNA”
BackgroundInfluential
Altered production and proteolytic processing of brevican by transforming growth factor β in cultured astrocytes
Hamel, M. G., Mayer, J., & Gottschall, P. E. (2005) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2005.03144.x · Cited by 55 · cited 6× · see citing works
“Similarly, the expression of ADAMTS-4 was described in cortical neurons in vitro [25], but a more recent investigation failed to detect ADAMTS-4 in cerebellar granule neurons in vitro [24].”
BackgroundResultInfluential
Remyelination after olfactory ensheathing cell transplantation into diverse demyelinating environments
Sasaki, M., Lankford, K. L., Radtke, C., Honmou, O., & Kocsis, J. D. (2011) · Experimental Neurology · doi:10.1016/j.expneurol.2011.01.010 · Cited by 51 · cited 1× · see citing works
“Moreover, olfactory ensheathing cell-based therapies promote remyelination after acute injuries [60] and these cells were recently reported to express ADAMTS-4 [61,62].”
Background
Potential of Olfactory Ensheathing Cells from Different Sources for Spinal Cord Repair
Mayeur, A., Duclos, C., Honoré, A., Gauberti, M., Drouot, L., do-Rego, J.-C., Bon‐Mardion, N., Jean, L., Vérin, É., Emery, É., et al. (2013) · PLoS ONE · doi:10.1371/journal.pone.0062860 · Cited by 49 · cited 1× · see citing works
“Moreover, olfactory ensheathing cell-based therapies promote remyelination after acute injuries [60] and these cells were recently reported to express ADAMTS-4 [61,62].”
BackgroundSelf-citation
ADAMTS1, ADAMTS5, ADAMTS9 and aggrecanase-generated proteoglycan fragments are induced following spinal cord injury in mouse
Demircan, K., Yonezawa, T., Takigawa, T., Topçu, V., Erdoğan, S., Uçar, F., Armutçu, F., Yiǧitoǧlu, M. R., Ninomiya, Y., & Hirohata, S. (2013) · Neuroscience Letters · doi:10.1016/j.neulet.2013.02.064 · Cited by 48 · cited 8× · see citing works
“mRNA level ↑ (rat/mouse) [23,33] stable (rat) [23] stable (mouse) [34]”
BackgroundInfluential
Expression of ADAMTS-1, -4, -5 and TIMP-3 in normal and multiple sclerosis CNS white matter
Haddock, G., Cross, A. K., Plumb, J., Surr, J., Buttle, D. J., Bunning, R. A. D., & Woodroofe, M. N. (2006) · Multiple Sclerosis Journal · doi:10.1191/135248506ms1300oa · Cited by 45 · cited 2× · see citing works
“While it is clear that astrocytes express ADAMTS proteoglycanases in vitro and in vivo [22-25], their presence in neurons under physiological conditions is controversial.”
Background
Interleukin‐6 upregulates expression of ADAMTS‐4 in fibroblast‐like synoviocytes from patients with rheumatoid arthritis
Mimata, Y., Kamataki, A., Oikawa, S., Murakami, K., Uzuki, M., Shimamura, T., & Sawai, T. (2011) · International Journal of Rheumatic Diseases · doi:10.1111/j.1756-185x.2011.01656.x · Cited by 45 · cited 1× · see citing works
“proteoglycanases in non-CNS cell types [28-31].”
Anti‐angiogenic properties of ADAMTS‐4 in vitro
Hsu, Y., Staton, C. A., Cross, N. A., & Buttle, D. J. (2012) · International Journal of Experimental Pathology · doi:10.1111/j.1365-2613.2011.00802.x · Cited by 43 · cited 2× · see citing works
“It would be consistent with local degradation of versican by ADAMTS proteoglycanases synthesized by endothelial cells [40-42] and/or monocytes/ macrophages [36].”
Background
A disintegrin and metalloprotease with thrombospondin type1 motifs (ADAMTS-1) and IL-1 receptor type 1 mRNAs are simultaneously induced in nerve injured motor neurons
Sasaki, M., Kiryu‐Seo, S., Kato, R., Shin-ichi, K. I. T. A., & Kiyama, H. (2001) · Molecular Brain Research · doi:10.1016/s0169-328x(01)00046-8 · Cited by 34 · cited 1× · see citing works
“neuroblast cell line in vitro and in motoneurons after nerve injury in vivo [35].”
Background
Differential expression of ADAMTS-1, -4, -5 and TIMP-3 in rat spinal cord at different stages of acute experimental autoimmune encephalomyelitis
Cross, A. K., Haddock, G., Surr, J., Plumb, J., Bunning, R. A. D., Buttle, D. J., & Woodroofe, M. N. (2005) · Journal of Autoimmunity · doi:10.1016/j.jaut.2005.09.026 · Cited by 31 · cited 2× · see citing works
“Spinal cord white matter (rat) [21] Yes (IHC) Yes (IHC) Yes (IHC)”
Background
Vascular Endothelial Growth Factor and Other Angioglioneurins
Lafuente, J. V., Ortuzar, N., Bengoetxea, H., Bulnes, S., & Argandoña, E. (2012) · International review of neurobiology · doi:10.1016/b978-0-12-386986-9.00012-0 · Cited by 27 · cited 1× · see citing works
“Besides its pro-angiogenic effect, VEGF has also been shown to promote vascular permeability, neuroinflammation, neuritic growth and neuroprotection particularly after ischemic stroke or SCI [46].”
Background
Cloning of the rat ADAMTS‐1 gene and its down regulation in endothelial cells in cirrhotic rats
Diamantis, I. D., Lüthi, M., Hösli, M., & Reichen, J. (2000) · Liver International · doi:10.1034/j.1600-0676.2000.020002165.x · Cited by 23 · cited 1× · see citing works
“It would be consistent with local degradation of versican by ADAMTS proteoglycanases synthesized by endothelial cells [40-42] and/or monocytes/ macrophages [36].”
Background
Selective Decline of Synaptic Protein Levels in the Frontal Cortex of Female Mice Deficient in the Extracellular Metalloproteinase ADAMTS1
Howell, M. D., Torres‐Collado, A. X., Iruela‐Arispe, M. L., & Gottschall, P. E. (2012) · PLoS ONE · doi:10.1371/journal.pone.0047226 · Cited by 21 · cited 3× · see citing works
“ADAMTS proteoglycanases are present in several CNS structures, including the cortex, the hippocampus, the striatum and the spinal cord [16-21].”
Background
WIN-34B, a new herbal medicine, inhibits the inflammatory response by inactivating IκB-α phosphorylation and mitogen activated protein kinase pathways in fibroblast-like synoviocytes
Huh, J., Seo, B.-K., Park, Y., Kim, J., Lee, J.-D., Choi, D., Baek, Y.-H., & Park, D. (2012) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2012.06.041 · Cited by 18 · cited 2× · see citing works
“A combination approach may represent an attractive therapeutic opportunity: first, the administration of an inhibitor of ADAMTS proteoglycanases activity, such as TIMP-3 (tissue inhibitor of metalloproteinases-3) [63], or an inhibitor of their synthesis, such as the antiinflammatory compound WIN-34B [29], in the acute…”
Background
ADAMTS-9 expression is up-regulated following transient middle cerebral artery occlusion (tMCAo) in the rat
Reid, M. J., Cross, A. K., Haddock, G., Allan, S. M., Stock, C. J., Woodroofe, M. N., Buttle, D. J., & Bunning, R. A. D. (2009) · Neuroscience Letters · doi:10.1016/j.neulet.2009.01.058 · Cited by 17 · cited 5× · see citing works
“Injured cerebral cortex, tMCAO (rat) [32] Yes (mRNA)”
BackgroundInfluential

Flagged first, then by citations

Sorted by citations

Crosstalk between glia, extracellular matrix and neurons
Song, I., & Dityatev, A. E. (2017) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2017.03.003 · Cited by 263 · see citing works
MMPs and ADAMTSs in intervertebral disc degeneration
Wang, W., Yu, X., Wang, C., Yang, W. Y., He, W., Zhang, S., Yan, Y., & Zhang, J. (2015) · Clinica Chimica Acta · doi:10.1016/j.cca.2015.06.023 · Cited by 210 · see citing works
The 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
Microglia as hackers of the matrix: sculpting synapses and the extracellular space
Crapser, J. D., Arreola, M. A., Tsourmas, K. I., & Green, K. N. (2021) · Cellular & Molecular Immunology · doi:10.1038/s41423-021-00751-3 · Cited by 178 · see citing works
“Furthermore, the effects of MMP-2 and ADAMTS-4 are additive in degrading brevican [247], which may offer one plausible explanation for the ability of exogenous ADAMTS-4 to degrade PNNs in amyotrophic lateral sclerosis model SOD1G93A mice in which PNN breakdown had already occurred, but not WT mice [262, 263].”
Background
Shaping Synapses by the Neural Extracellular Matrix
Ferrer-Ferrer, M., & Dityatev, A. (2018) · Frontiers in Neuroanatomy · doi:10.3389/fnana.2018.00040 · Cited by 169 · see citing works
“In vivo data supports the view that most ADAMTSs are produced by astrocytes, especially after injury, although ADAMTSs are also produced by neurons and microglia (Lemarchant et al., 2013).”
Background
Altered neuro-inflammatory gene expression in hippocampus in major depressive disorder
Mahajan, G., Vallender, E. J., Garrett, M. R., Challagundla, L., Overholser, J. C., Jurjus, G., Dieter, L., Syed, M., Romero, D. G., Benghuzzi, H., et al. (2017) · Progress in Neuro-Psychopharmacology and Biological Psychiatry · doi:10.1016/j.pnpbp.2017.11.017 · Cited by 159 · see citing works
“ADAMTS proteoglycanases are also involved in neural repair and synaptic plasticity (Lemarchant et al., 2013).”
Background
Stress-induced blood brain barrier disruption: Molecular mechanisms and signaling pathways
Welcome, M. O., & Mastorakis, N. E. (2020) · Pharmacological Research · doi:10.1016/j.phrs.2020.104769 · Cited by 139 · see citing works
MMP9/RAGE pathway overactivation mediates redox dysregulation and neuroinflammation, leading to inhibitory/excitatory imbalance: a reverse translation study in schizophrenia patients
Dwir, D., Giangreco, B., Xin, L., Tenenbaum, L., Cabungcal, J.-H., Steullet, P., Goupil, A., Cleusix, M., Jenni, R., Chtarto, A., et al. (2019) · Molecular Psychiatry · doi:10.1038/s41380-019-0393-5 · Cited by 137 · see citing works
“To date, CSPG degradation primarily involves ADAMTS4 and ADAMTS5 [66].”
Background
MicroRNA-146a Mimics Reduce the Peripheral Neuropathy in Type 2 Diabetic Mice
Liu, X., Fan, B., Szalad, A., Jia, L., Wang, L., Wang, X., Pan, W., Zhang, L., Zhang, R., Hu, J., et al. (2017) · Diabetes · doi:10.2337/db16-1182 · Cited by 127 · see citing works
“7C) which plays an important role in the inflammation (34).”
Background
ADAMTS expression and function in central nervous system injury and disorders
Gottschall, P. E., & Howell, M. D. (2015) · Matrix Biology · doi:10.1016/j.matbio.2015.01.014 · Cited by 100 · see citing works
“In vivo data supports that most ADAMTSs are produced by astrocytes, especially after injury, although ADAMTSs are also produced by neurons and microglia [33].”
BackgroundInfluential
Vascular Signal Transducer and Activator of Transcription-3 Promotes Angiogenesis and Neuroplasticity Long-Term After Stroke
Hoffmann, C. J., Harms, U., Rex, A., Szulzewsky, F., Wolf, S. A., Grittner, U., Lättig-Tünnemann, G., Sendtner, M., Kettenmann, H., Dirnagl, U., et al. (2015) · Circulation · doi:10.1161/circulationaha.114.013003 · Cited by 96 · see citing works
“Adamts proteases are classified in 3 subfamilies based on their preference for cleaving specific ECM components.(33)”
Background
Nutritional regulation of oligodendrocyte differentiation regulates perineuronal net remodeling in the median eminence
Kohnke, S., Buller, S. A., Nuzzaci, D., Ridley, K., Lam, B., Pivoňková, H., Bentsen, M. A., Alonge, K. M., Zhao, C., Tadross, J. A., et al. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.109362 · Cited by 74 · see citing works
Matrix metalloproteinases and ADAMs in stroke
Montaner, J., Ramiro, L., Simats, A., Hernández‐Guillamón, M., Delgado, P., Bustamante, A., & Rosell, A. (2019) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-019-03175-5 · Cited by 66 · see citing works
Self-citation
tPA promotes ADAMTS-4-induced CSPG degradation, thereby enhancing neuroplasticity following spinal cord injury
Lemarchant, S., Pruvost, M., Hébert, M., Gauberti, M., Hommet, Y., Briens, A., Maubert, E., Gueye, Y., Feron, F. P., Petite, D., et al. (2014) · Neurobiology of Disease · doi:10.1016/j.nbd.2014.02.005 · Cited by 59 · see citing works
“Interestingly, some metalloproteinases of the ADAMTS family are involved in the clearance of CSPGs (Lemarchant et al., 2013; Shiomi et al., 2010).”
Self-citation
Inhibition of 2-AG hydrolysis differentially regulates blood brain barrier permeability after injury
Piro, J. R., Suidan, G. L., Quan, J., Pi, Y., O'Neill, S., Ilardi, M. C., Pozdnyakov, N., Lanz, T. A., Xi, H. S., Bell, R. D., et al. (2018) · Journal of Neuroinflammation · doi:10.1186/s12974-018-1166-9 · Cited by 55 · see citing works
“The role of ADAMTS family of proteins has been extensively studied for their ability to remodel extracellular matrix (ECM) in the context of osteoarthritis.”
Background
The Balance Between Metalloproteinases and TIMPs
Masciantonio, M. G., Lee, C. K. S., Arpino, V., Mehta, S., & Gill, S. E. (2017) · Progress in molecular biology and translational science · doi:10.1016/bs.pmbts.2017.01.001 · Cited by 54 · see citing works
Damaged Neocortical Perineuronal Nets Due to Experimental Focal Cerebral Ischemia in Mice, Rats and Sheep
Härtig, W., Mages, B., Aleithe, S., Nitzsche, B., Altmann, S., Barthel, H., Krueger, M., & Michalski, D. (2017) · Frontiers in Integrative Neuroscience · doi:10.3389/fnint.2017.00015 · Cited by 53 · see citing works
“, disintegrin and metalloproteinase with thrompospondin motifs (ADAMTS-1, 4, 8 and 15) and neprilysin (Cross et al., 2006; Lemarchant et al., 2013; Levy et al., 2015; Rossier et al., 2015).”
Background
Perineuronal Nets: Subtle Structures with Large Implications
Carceller, H., Gramuntell, Y., Klimczak, P., & Nácher, J. (2022) · The Neuroscientist · doi:10.1177/10738584221106346 · Cited by 48 · see citing works
Genetic Biomarkers on Age-Related Cognitive Decline
Lin, C., Lin, E., & Lane, H. (2017) · Frontiers in Psychiatry · doi:10.3389/fpsyt.2017.00247 · Cited by 46 · see citing works
Anti‐inflammatory effects of ADAMTS‐4 in a mouse model of ischemic stroke
Lemarchant, S., Dhungana, H., Pomeshchik, Y., Leinonen, H., Kołosowska, N., Korhonen, P., Kanninen, K. M., García‐Berrocoso, T., Montaner, J., Malm, T., et al. (2016) · Glia · doi:10.1002/glia.23017 · Cited by 45 · see citing works
“A disintegrin and metalloproteinase with thrombospondin motifs type 4, ADAMTS-4, belongs to the subfamily of ADAMTS proteases capable of degrading proteoglycans (Hamel et al., 2008; Lemarchant et al., 2013).”
BackgroundSelf-citation
Dopamine Receptor Activation Modulates the Integrity of the Perisynaptic Extracellular Matrix at Excitatory Synapses
Mitlöhner, J., Kaushik, R., Niekisch, H., Blondiaux, A., Gee, C. E., Happel, M. F. K., Gundelfinger, E., Dityatev, A., Frischknecht, R., & Seidenbecher, C. (2020) · Cells · doi:10.3390/cells9020260 · Cited by 47 · see citing works
“Enzymes of the ADAMTS family are synthesized as pro-enzymes, which are cleaved at their Cor N-termini by furin or furin-like PPCs such as PACE4, resulting in mature and potentially active enzymes [73,74].”
Curcumin downregulates expression of opioid-related nociceptin receptor gene (OPRL1) in isolated neuroglia cells
Seo, E., Efferth, T., & Panossian, A. G. (2018) · Phytomedicine · doi:10.1016/j.phymed.2018.09.202 · Cited by 43 · see citing works
RNA‐sequencing reveals oligodendrocyte and neuronal transcripts in microglia relevant to central nervous system disease
Solga, A. C., Pong, W. W., Walker, J., Wylie, T., Magrini, V. J., Apicelli, A. J., Griffith, M., Griffith, O. L., Kohsaka, S., Wu, G. F., et al. (2014) · Glia · doi:10.1002/glia.22754 · Cited by 43 · see citing works
“Other transcripts included those relevant to lymphocyte function (e.g., Slamf1, Tagap; Veillette et al., 2007), cholesterol transport (e.g., Abcb1b, Abca1; Oram and Vaughan, 2000), and inflammatory processes (e.g., Cxcl10, Adamts1; Klein, 2004; Lemarchant et al., 2013; Fig.”
Harnessing the Benefits of Neuroinflammation: Generation of Macrophages/Microglia with Prominent Remyelinating Properties
Mishra, M. K., Rawji, K. S., Keough, M. B., Kappen, J., Dowlatabadi, R., Vogel, H. J., Chopra, S., Distéfano‐Gagné, F., Dufour, A., Gosselin, D., et al. (2021) · Journal of Neuroscience · doi:10.1523/jneurosci.1948-20.2021 · Cited by 42 · see citing works
“Pro-inflammatory and highly activated macrophages have cytotoxic properties (Laskin and Pendino, 1995), and excessive LPS stimulation has the capacity to injure CNS cells, including in coculture of oligodendrocytes and macrophages and microglia (Fabian and Rea, 1993; Li et al., 2008).”
Influential
Extracellular matrix modulation is driven by experience-dependent plasticity during stroke recovery.
Quattromani, M. J., Pruvost, M., Guerreiro, C., Backlund, F., Englund, E., Aspberg, A., Jaworski, T., Hakon, J., Ruscher, K., Kaczmarek, L., et al. (2018) · Molecular Neurobiology · doi:10.1007/s12035-017-0461-2 · Cited by 39 · see citing works
“several central nervous system (CNS) functions, including neurorepair, remyelination, angiogenesis, and inflammation [30].”
BackgroundSelf-citation
New Insights into ADAMTS Metalloproteases in the Central Nervous System
Mohamedi, Y., Fontanil, T., Cobo, T., Cal, S., & Obaya, Á. J. (2020) · Biomolecules · doi:10.3390/biom10030403 · Cited by 39 · see citing works
“In vivo and in vitro data have shown that although microglia and neurons also express ADAMTSs, most of them are produced by astrocytes, specifically after a brain injury [90].”
BackgroundInfluential
The ADAMTS9 gene is associated with cognitive aging in the elderly in a Taiwanese population
Lin, E., Tsai, S., Kuo, P., Liu, Y., Yang, A. C., Kao, C., & Yang, C. (2017) · PLoS ONE · doi:10.1371/journal.pone.0172440 · Cited by 39 · see citing works
Insights into the Role of MicroRNAs in the Onset and Development of Diabetic Neuropathy
Simeoli, R., & Fierabracci, A. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20184627 · Cited by 37 · see citing works
“gene confirming its role in the inflammatory processes [53].”
BackgroundMethod
ADAMTS-4 promotes neurodegeneration in a mouse model of amyotrophic lateral sclerosis
Lemarchant, S., Pomeshchik, Y., Kidin, I., Kärkkäinen, V., Valonen, P. K., Lehtonen, Š., Goldsteins, G., Malm, T., Kanninen, K. M., & Koıstınaho, J. (2016) · Molecular Neurodegeneration · doi:10.1186/s13024-016-0078-3 · Cited by 36 · see citing works
“Modifications of ADAMTS-4 expression/activity have been reported during spinal cord injury (SCI), experimental autoimmune encephalomyelitis and multiple sclerosis [1].”
BackgroundSelf-citation
Non-Cell-Autonomous Factors Implicated in Parvalbumin Interneuron Maturation and Critical Periods
Gibel-Russo, R., Benacom, D., & Nardo, A. A. D. (2022) · Frontiers in Neural Circuits · doi:10.3389/fncir.2022.875873 · Cited by 36 · see citing works
“While they are mainly expressed by astrocytes (Lemarchant et al., 2013), ADAMTS-8 and -15 were found to be expressed in somatosensory FS-PV cells (Rossier et al.”
Background
Pathophysiological function of ADAMTS enzymes on molecular mechanism of Alzheimer’s disease
Gurses, M. S., Ural, M. N., Gulec, M. A., Akyol, O., & Akyol, S. (2016) · Aging and disease · doi:10.14336/ad.2016.0111 · Cited by 35 · see citing works
“[61] Lemarchant S, Pruvost M, Montaner J, Emery E, Vivien”
Background
Mapping the cortico-striatal transcriptome in attention deficit hyperactivity disorder
Sudre, G. P., Gildea, D. E., Shastri, G. G., Sharp, W. S., Jung, B., Xu, Q., Auluck, P. K., Elnitski, L. L., Baxevanis, A. D., Marenco, S., et al. (2022) · Molecular Psychiatry · doi:10.1038/s41380-022-01844-9 · Cited by 32 · see citing works
“In this regard, it is notable that several of the most significantly differentially expressed genes play a role in neuroplastic processes, promoting neurogenesis (ANGPTL4), neural progenitor cell proliferation (PDPN) and synaptic plasticity (ADAMTS9) [45, 46].”
Background
The Role of Perineuronal Nets in Physiology and Disease: Insights from Recent Studies
Auer, S., Schicht, M., Hoffmann, L., Budday, S., Frischknecht, R., Blümcke, I., & Paulsen, F. P. (2025) · Cells · doi:10.3390/cells14050321 · Cited by 30 · see citing works
“They are capable in degrading CSPGs, mainly aggrecan and brevican [74–77].”
Telmisartan Protects a Microglia Cell Line from LPS Injury Beyond AT1 Receptor Blockade or PPARγ Activation
ELKAHLOUN, A. G., Rodríguez, Y., Alaiyed, S., Wenzel, E. D., & Saavedra, J. M. (2018) · Molecular Neurobiology · doi:10.1007/s12035-018-1300-9 · Cited by 30 · see citing works
“The genes upregulated by LPS and downregulated by Telmisartan include the pro-inflammatory cytokines IL1-β and IL-6, NFκB and its activator miR221, miR155, the TNF superfamily, TLR2, Adamts1 and miR129–2 (Supplemental Tables 3 and 6).”
ADAMTS8 inhibited lung cancer progression through suppressing VEGFA
Zhang, Y., Hu, K., Qu, Z., Xie, Z., & Tian, F. (2022) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2022.01.110 · Cited by 29 · see citing works
ADAMTS18 Deficiency Affects Neuronal Morphogenesis and Reduces the Levels of Depression-like Behaviors in Mice
Zhu, R., Pan, Y.-H., Sun, L., Zhang, T., Wang, C., Ye, S., Yang, N., Lu, T., Wısnıewskı, T., Dang, S., et al. (2018) · Neuroscience · doi:10.1016/j.neuroscience.2018.12.025 · Cited by 28 · see citing works
“Most ADAMTSs are produced by astrocytes, neurons, and microglia (Lemarchant et al., 2013).”
Background
Current Agents and Related Therapeutic Targets for Inflammation Following Acute Traumatic Spinal Cord Injury.
Jorge, A., Taylor, T., Agarwal, N., & Hamilton, D. (2019) · World Neurosurgery · doi:10.1016/j.wneu.2019.08.108 · Cited by 16 · see citing works
Peptide-Based Inhibitors of ADAM and ADAMTS Metalloproteinases
Pluda, S., Mazzocato, Y., & Angelini, A. (2021) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2021.703715 · Cited by 27 · see citing works
Methylomic changes in individuals with psychosis, prenatally exposed to endocrine disrupting compounds: Lessons from diethylstilbestrol
Rivollier, F., Chaumette, B., Bendjemaa, N., Chayet, M., Millet, B., Jaafari, N., Barhdadi, A., Perreault, L. L., Provost, S., Dubé, M., et al. (2017) · PLoS ONE · doi:10.1371/journal.pone.0174783 · Cited by 27 · see citing works
“Indeed, several functions in the physiological and pathological CNS, such as neuroplasticity, neurorepair, inflammation and angiogenesis, may be achieved via the cleavage of their substrate (chondroitin sulfate proteoglycans or Reelin), but also independently of their proteolytic activity [37].”
Background
Hevin–calcyon interaction promotes synaptic reorganization after brain injury
Kim, J.-H., Jung, H., Kim, A., Shim, H. S., Hyeon, S. J., Lee, Y., Han, J., Jung, J. H., Lee, J., Ryu, H., et al. (2021) · Cell Death and Differentiation · doi:10.1038/s41418-021-00772-5 · Cited by 25 · see citing works
A view of the genetic and proteomic profile of extracellular matrix molecules in aging and stroke
Chmelová, M., Androvic, P., Kirdajová, D., Turečková, J., Kriška, J., Valihrach, L., Anděrová, M., & Vargová, L. (2023) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2023.1296455 · Cited by 23 · see citing works
Role of ADAM and ADAMTS disintegrin and metalloproteinases in normal pregnancy and preeclampsia
Qu, H., & Khalil, R. A. (2022) · Biochemical Pharmacology · doi:10.1016/j.bcp.2022.115266 · Cited by 24 · see citing works
ADAMTS‐4 in oligodendrocytes contributes to myelination with an impact on motor function
Pruvost, M., Lépine, M., Leonetti, C., Etard, O., Naveau, M., Agin, V., Docagne, F., Maubert, E., Ali, C., Emery, É., et al. (2017) · Glia · doi:10.1002/glia.23207 · Cited by 22 · see citing works
“The ADAMTS proteases, especially ADAMTS-1, 24, 25, and 29 play roles in the CNS such as neuroplasticity, neuroregeneration, inflammation, and angiogenesis (Gottschall & Howell, 2015; Lemarchant et al., 2013).”
BackgroundSelf-citation
ADAMTS4 Enhances Oligodendrocyte Differentiation and Remyelination by Cleaving NG2 Proteoglycan and AttenuatingPDGFRα Signaling
Jiang, C., Qiu, W., Yang, Y., Huang, H., Dai, Z., Yang, A., Tang, T., Zhao, X., & Qiu, M. S. (2023) · Journal of Neuroscience · doi:10.1523/jneurosci.2146-22.2023 · Cited by 22 · see citing works
The bone transcription factor Osterix controls extracellular matrix- and node of Ranvier-related gene expression in oligodendrocytes
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ADAM and ADAMTS disintegrin and metalloproteinases as major factors and molecular targets in vascular malfunction and disease
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Inhibition of Aggrecanases as a Therapeutic Strategy in Osteoarthritis
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Keratan Sulphate in the Tumour Environment
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ADAMTS4 is involved in the production of the Alzheimer disease amyloid biomarker APP669-711
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“implicated in the development of osteoarthritis [24, 25].”
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Selective dysfunction of fast-spiking inhibitory interneurons and disruption of perineuronal nets in a tauopathy mouse model
Kudo, T., Takuwa, H., Takahashi, M., Urushihata, T., Shimojo, M., Sampei, K., Yamanaka, M., Tomita, Y., Sahara, N., Suhara, T., et al. (2023) · iScience · doi:10.1016/j.isci.2023.106342 · Cited by 16 · see citing works
ADAMTS‐4 in central nervous system pathologies
Lemarchant, S., Wojciechowski, S., Vivien, D., & Koıstınaho, J. (2017) · Journal of Neuroscience Research · doi:10.1002/jnr.24021 · Cited by 16 · see citing works
“CSPGs are ECM-macromolecules composed of a core protein (lecticans, phosphacan or type 2 neuroglycan) and chondroitin sulfate moieties.”
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A comprehensive atlas of Aggrecan, Versican, Neurocan and Phosphacan expression across time in wildtype retina and in retinal degeneration
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Diethylstilbestrol and autism
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“Therefore , deregulated expression of ADAMTS proteoglycanases might influence fetal neuroplasticity by affecting the extracellular matrix structure and function in nervous system cells (34, 35).”
Background
Therapeutic administration of mouse mast cell protease 6 improves functional recovery after traumatic spinal cord injury in mice by promoting remyelination and reducing glial scar formation
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“However, at later time points, extracellular proteases can improve recovery by stimulating axon growth, synaptic plasticity, remyelination, and angiogenesis (52-55).”
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Genome-wide association study of cerebrospinal fluid neurofilament light levels in non-demented elders
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“Only recently more attention is paid to its role in the central nervous system (CNS) (24).”
BackgroundInfluential
CNS / PNS proteoglycans functionalize neuronal and astrocyte niche microenvironments optimizing cellular activity by preserving membrane polarization dynamics, ionic microenvironments, ion fluxes, neuronal activation, and network neurotransductive capacity
Melrose, J. (2024) · Journal of Neuroscience Research · doi:10.1002/jnr.25361 · Cited by 15 · see citing works
“ADAMTS-4 promotes functional recovery after spinal cord injury (Lemarchant et al., 2013; Tauchi et al., 2012). tPA promotes activation of ADAMTS-4 and, in turn, CSPG degradation, thereby enhancing neuroplasticity following spinal cord injury and functional neuronal recovery in gliotic scars…”
Hyalectanase Activities by the ADAMTS Metalloproteases
Fontanil, T., Mohamedi, Y., Casado, J. E., Obaya, Á. J., Cobo, T., & Cal, S. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22062988 · Cited by 13 · see citing works
“Other findings supporting the role of brevican cleavage by ADAMTSs in this type of tumor is that the highly invasive rat CNS-1 glioma cell line produces and cleaves brevican when grown as an intracranial graft [135].”
BackgroundInfluential
Extracellular Matrix Recycling as a Novel Plasticity Mechanism With a Potential Role in Disease
Dankovich, T. M., & Rizzoli, S. O. (2022) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2022.854897 · Cited by 12 · see citing works
Longitudinal in vivo imaging of perineuronal nets
Benbenishty, A., Peled-Hajaj, S., Krishnaswamy, V. R., Har-Gil, H., Havusha-Laufer, S., Ruggiero, A., Slutsky, I., Blinder, P., & Sagi, I. (2023) · Neurophotonics · doi:10.1117/1.nph.10.1.015008 · Cited by 11 · see citing works
Sequesterpene Lactones Isolated from a Brazilian Cerrado Plant (Eremanthus spp.) as Anti-Proliferative Compounds, Characterized by Functional and Proteomic Analysis, Are Candidates for New Therapeutics in Glioblastoma
Izumi, C., Laure, H. J., Barbosa, N. G., Thomé, C. H., Ferreira, G. A., Sousa, J. P., Lopes, N. P., & Rosa, J. C. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21134713 · Cited by 11 · see citing works
“Endogenous ADAMTS proteoglycanases can negatively regulate by sequestration of VEGF, a potent pro-angiogenesis factor, thus affecting the formation of new blood vessels [12].”
Background
Neurodevelopmental disorders in children exposed in utero to synthetic progestins: analysis from the national cohort of the Hhorages Association*
Soyer‐Gobillard, M., Gaspari, L., Courtet, P., Puillandre, M., Paris, F., & Sultan, C. (2019) · Gynecological Endocrinology · doi:10.1080/09513590.2018.1512968 · Cited by 10 · see citing works
Induction of A Disintegrin and Metalloproteinase with Thrombospondin motifs 1 by a rare variant or cognitive activities reduces hippocampal amyloid-β and consequent Alzheimer’s disease risk
Qiu, Y., Sha, L., Zhang, X., Li, G., Zhu, W., & Xu, Q. (2022) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2022.896522 · Cited by 9 · see citing works
“ADAMTS1 encodes a zinc metalloprotease belonging to the ADAMTS secretase family (Lemarchant et al., 2013) that functions on extracellular matrix (ECM) hydrolysis (Zhong and Khalil, 2019).”
Background
Effects of prenatal exposure to synthetic sex hormones on neurodevelopment: a biological mechanism.
Soyer‐Gobillard, M., Gaspari, L., Paris, F., Courtet, P., & Sultan, C. (2023) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2023.1237429 · Cited by 7 · see citing works
“…also is involved in CNS development and more precisely in synaptic plasticity, neurorepair, angiogenesis and inflammation mechanisms (Lemarchant et al., 2013) and in regulating organ morphology, particularly uterus and reproductive system (Mittaz et al., 2004), which are often…”
Background
ADAMTS4 is upregulated in colorectal cancer and could be a useful prognostic indicator of colorectal cancer
Shang, X., Liu, K.-L., Li, Q., Lao, Y., Li, N.-S., & Wu, J. (2020) · Revista da Associação Médica Brasileira · doi:10.1590/1806-9282.66.1.42 · Cited by 7 · see citing works
Screening of hub inflammatory bowel disease biomarkers and identification of immune-related functions based on basement membrane genes
Lin, P., Jin, H., Teng, Z., Lin, C., Liu, S., He, R., Chen, H., Yao, H., Ye, J., & Zhu, G. (2023) · European journal of medical research · doi:10.1186/s40001-023-01193-5 · Cited by 6 · see citing works
“Among them, ADAMTS9 belongs to the hub enzyme of proteoglycan degradation [43–45], and its harmful role in osteoarthritis, rheumatoid arthritis, and intervertebral disc degeneration have been widely described [46].”
Background
Secretome analysis of oligodendrocytes and precursors reveals their roles as contributors to the extracellular matrix and potential regulators of inflammationPreprint
Godoy, M. I., Pandey, V., Wohlschlegel, J. A., & Zhang, Y. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.07.22.604699 · Cited by 6 · see citing works
Identifying hub genes of sepsis-associated and hepatic encephalopathies based on bioinformatic analysis—focus on the two common encephalopathies of septic cirrhotic patients in ICU
Li, J., Dong, Y., Ge, S., Liu, L., Huo, Y., & Hu, Z. (2024) · BMC Medical Genomics · doi:10.1186/s12920-023-01774-7 · Cited by 5 · see citing works
Immune Cell Proteins and Parkinson's Disease: A Mendelian Randomization Analysis of Causal Associations
Li, H., He, J., Xuan, T., Gu, S., Niu, X., Ren, Y., Zhan, X., & Cheng, J. (2025) · Brain and Behavior · doi:10.1002/brb3.70596 · Cited by 4 · see citing works
Single‐nucleotide polymorphisms in the coding region of a disintegrin and metalloproteinase with thrombospondin motifs 4 and hepatocellular carcinoma: A retrospective case‐control study
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Expression and Preparation of Recombinant Reelin and ADAMTS-3 Proteins
Kohno, T., Ogino, H., Yamakage, Y., & Hattori, M. (2019) · Methods in molecular biology · doi:10.1007/978-1-4939-9698-8_8 · Cited by 3 · see citing works
Inhibition of the BET family of epigenetic reader proteins: A novel principle for modulating gene expression in IgE-activated mast cells
García‐Faroldi, G., Rönnberg, E., Grujić, M., & Pejler, G. (2017) · Immunity Inflammation and Disease · doi:10.1002/iid3.150 · Cited by 3 · see citing works
“As ADAMTS9 is implicated in connective tissue remodeling events [31], BET inhibition could thus counteract such processes orchestrated by mast cells.”
Evidence for Link Between Mental Disorders and in Utero Exposure to Synthetic Hormones: A Long and Crucial History
Soyer‐Gobillard, M., Gaspari, L., & Sultan, C. (2019) · IntechOpen eBooks · doi:10.5772/intechopen.80969 · Cited by 2 · see citing works
“The ADAM TS9 gene is implicated in the control of organ shape, especially in the development and function of the uterus and reproductive organs [32] which are often abnormal after in utero DES exposure as well as in the control of the CNS development [33] and in several kinds of cancers [34].”
Background
In utero exposure to synthetic sex hormones and their multigenerational impact on neurodevelopmental disorders: endocrine disruptors as neuroendocrine disruptors
Soyer-Gobillard, M.-O., Gaspari, L., & Sultan, C. (2025) · Journal of the Neurological Sciences · doi:10.1016/j.jns.2025.123471 · Cited by 2 · see citing works
Dopamine modulates the integrity of the perisynaptic extracellular matrix at excitatory synapsesPreprint
Mitlöhner, J., Kaushik, R., Niekisch, H., Blondiaux, A., Gee, C. E., Happel, M. F. K., Gundelfinger, E. D., Dityatev, A. E., Frischknecht, R., & Seidenbecher, C. I. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/722454 · Cited by 2 · see citing works
“Enzymes of the ADAMTS family are synthesized as pro-enzymes, which are cleaved at their C- or N-termini by furin or furin-like PPCs, such as PACE4, resulting in mature and potentially active enzymes (Flannery et al., 2002; Lemarchant et al., 2013).”
Background
Loss of function variants in ADAMTS6 : Connective tissue, Heart defect, thoracic Aortic aneurysm and Neuro developmental Syndrome (CHANS)Preprint
Herrero, J. H., Arnaud, P., Bibimbou, A., Seifert, D. E., Mougin, Z., Benarroch, L., Michot, C., Capri, Y., Ruaud, L., Dupuis‐Girod, S., et al. (2025) · medRxiv · doi:10.1101/2025.05.02.25326573 · Cited by 2 · see citing works
“The ADAMTS family is known to play a crucial role in neuroplasticity and neurological disorders 31 .”
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Wu, X., Tsuchiya, I., Aung, K. Z., Qiao, Q., Fardo, D. W., Nelson, P. T., Abner, E. L., James, B. D., Norris, C. M., & Katsumata, Y. (2025) · Journal of Alzheimer s Disease · doi:10.1177/13872877251385220 · Cited by 1 · see citing works
“58 The observed association of ADAMTS1 -rs2830489(T) with better global cognitive function among Asian participants with dementia may indicate a potential role in cognitive resilience mechanisms.”
Machine learning-based approach for efficient prediction of diagnosis, prognosis and lymph node metastasis of papillary thyroid carcinoma using adhesion signature selection
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“Long-term reduction of OTX2 in the PCx results in increased expression of Adamts9 and Mmp9 , which proteolyze proteoglycans (Huntley, 2012; Lemarchant et al., 2013) and would account for lower PNN levels through matrix reorganization in P400 mice.”
Background
Emerging roles of ADAMTS metalloproteinases in regenerativemedicine and restorative biology
Armutçu, F., & Demircan, K. (2016) · TURKISH JOURNAL OF BIOLOGY · doi:10.3906/biy-1505-32
“…of ECM macromolecules, have been extensively investigated for understanding their involvement in inflammation-induced osteoarthritis (OA), and an increasing amount of evidence indicates that they could have a crucial role physiologically and pathologically in the CNS (Lemarchant et al., 2013).”
BackgroundInfluential
The Metalloproteinase-Dependent Role of TIMPs in Regulation of Pulmonary Microvascular Endothelial Cell Barrier Function During Sepsis
Masciantonio, M. G. (2017) · Scholarship@Western (Western University)
THE THEORY AND PRACTICE OF RELAY TYPE INSTRUMENTS BASED ON RADIOACTIVE ISOTOPES
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Investigation of extracellular matrix genes associated with Alzheimer’s disease in the hippocampus of experimental diabetic model rats
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“During embryonic development, ECM directly affects neuronal and glial migration and differentiation, neurogenesis, and axonal growth, and it guides synaptogenesis [13, 25].”
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Retracted: Evaluation of ADAMTS-9 Expression in Post-Mortem Brain Tissue
Esadawi, A., Maamar, I., Woodroof, N., & Soosay, A. E. R. (2021) · Journal of Alasmarya University for Applied Sciences · doi:10.59743/aujas.v6i2.889
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Proteinlerin Posttranslasyonel Modifikasyonları
Gül, N. (2023) · Akademisyen Kitabevi eBooks · doi:10.37609/akya.2621
Additional file 1 of Identifying hub genes of sepsis-associated and hepatic encephalopathies based on bioinformatic analysis—focus on the two common encephalopathies of septic cirrhotic patients in ICU
Li, J., Dong, Y., Ge, S., Liu, L., Huo, Y., & Hu, Z. (2024) · Figshare · doi:10.6084/m9.figshare.24987710
Microglia: Key Players in Perineuronal Net Dynamics
Garmendia-Berges, M., & Puerta, E. (2025) · IntechOpen eBooks · doi:10.5772/intechopen.1012413
Additional file 3 of Identifying hub genes of sepsis-associated and hepatic encephalopathies based on bioinformatic analysis—focus on the two common encephalopathies of septic cirrhotic patients in ICU
Li, J., Yang, D., Ge, S., Liu, L., Huo, Y., & Hu, Z. (2024) · Figshare · doi:10.6084/m9.figshare.26666632
Additional file 1 of Screening of hub inflammatory bowel disease biomarkers and identification of immune-related functions based on basement membrane genes
Lin, P., Hua, J., Teng, Z., Lin, C., Liu, S., He, R., Chen, H., Yao, H., Ye, J., & Zhu, G. (2024) · Figshare · doi:10.6084/m9.figshare.26605882
Additional file 2 of Screening of hub inflammatory bowel disease biomarkers and identification of immune-related functions based on basement membrane genes
Lin, P., Hua, J., Teng, Z., Lin, C., Liu, S., He, R., Chen, H., Yao, H., Ye, J., & Zhu, G. (2024) · Figshare · doi:10.6084/m9.figshare.26605885
Additional file 2 of Identifying hub genes of sepsis-associated and hepatic encephalopathies based on bioinformatic analysis—focus on the two common encephalopathies of septic cirrhotic patients in ICU
Li, J., Yang, D., Ge, S., Liu, L., Huo, Y., & Hu, Z. (2024) · Figshare · doi:10.6084/m9.figshare.24987955
Contrôle du réseau périneuronal par l’activité des interneurones à décharge rapide exprimant la parvalbumine
Devienne, G. F. (2019) · theses.fr (ABES) · doi:10.70675/453418efzc908z49e0zba6fz71fefaa50691
“Les ADAMTS sont produits par les neurones, la glie et la microglie (Lemarchant et al., 2013).”
Role of ADAMTS(L) family in thoracic aortic aneurysm
Herrero, J. H. (2025) · doi:10.70675/5037c26az4b33z47d1z8910z8937d504b9b9
The ADAMTS8 paradox: Context-dependent mechanisms linking tumor suppression and cardiovascular remodeling
Cai, Y., Wang, M., Qiu, R., Liu, S., Liu, T., & Wang, G. (2026) · Genes & Diseases · doi:10.1016/j.gendis.2026.102311
Convergent Lower Expression of Redox-Linked Stress-Adaptation and Synaptic-Plasticity Genes in Major Depressive Disorder Across Seven Postmortem dlPFC Cohorts
Klepacki, H., Ordak, M., Kowalczuk, K., Hermanowicz, J. M., & Waszkiewicz, N. (2026) · Antioxidants · doi:10.3390/antiox15070908
The translational paradox of ADAMTS-5 in osteoarthritis: mechanistic centrality but limited clinical efficacy
Li, Y., Chu, J., Qin, S., & Liu, S. (2026) · Frontiers in Medicine · doi:10.3389/fmed.2026.1877932

and pathological central nervous system
Lemarchant, S., Pruvost, M., Montaner, J., Emery, É., Vivien, D., Kanninen, K., & Koıstınaho, J. (2014)
Self-citation
ADAMTS‐4 in central nervous system pathologies
Lemarchant, S., Wojciechowski, S., Vivien, D., & Koıstınaho, J. (2017) · Journal of Neuroscience Research · doi:10.1002/jnr.24021 · Cited by 16 · see citing works
Self-citation
ADAMTS1, ADAMTS5, ADAMTS9 and aggrecanase-generated proteoglycan fragments are induced following spinal cord injury in mouse
Demircan, K., Yonezawa, T., Takigawa, T., Topçu, V., Erdoğan, S., Uçar, F., Armutçu, F., Yiǧitoǧlu, M. R., Ninomiya, Y., & Hirohata, S. (2013) · Neuroscience Letters · doi:10.1016/j.neulet.2013.02.064 · Cited by 48 · see citing works
Anti‐inflammatory effects of ADAMTS‐4 in a mouse model of ischemic stroke
Lemarchant, S., Dhungana, H., Pomeshchik, Y., Leinonen, H., Kołosowska, N., Korhonen, P., Kanninen, K. M., García‐Berrocoso, T., Montaner, J., Malm, T., et al. (2016) · Glia · doi:10.1002/glia.23017 · Cited by 45 · see citing works
Self-citation
The endogenous proteoglycan-degrading enzyme ADAMTS-4 promotes functional recovery after spinal cord injury
Tauchi, R., Imagama, S., Natori, T., Ohgomori, T., Muramoto, A., Shinjo, R., Matsuyama, Y., Ishiguro, N., & Kadomatsu, K. (2012) · Journal of Neuroinflammation · doi:10.1186/1742-2094-9-53 · Cited by 91 · see citing works

Authors: Lemarchant, S., Pruvost, M., Montaner, J., Emery, E., Vivien, D., Kanninen, K., & Koistinaho, J.
Affiliations: University of Eastern Finland (FI)
Inserm (FR)
Universitat Autònoma de Barcelona (ES)
Corresponding author: Lemarchant, Sighild
ORCID: Lemarchant, Sighild
Pruvost, Mathilde
Montaner, Joan
Vivien, Denis
Kanninen, Katja
Venue: Journal of Neuroinflammation
Publisher: Springer Science and Business Media LLC
Published: 2013-10-31
Volume: 10
Issue: 1
Pages: 133-133
ISSN: 1742-2094 (ISSN-L)
DOI: 10.1186/1742-2094-10-133
PMC: PMC4228433
OpenAlex: W2107027445
Cited by: 96
References: 65
Citations by year: 2026: 3 · 2025: 7 · 2024: 6 · 2023: 11 · 2022: 10 · 2021: 10 · 2020: 7 · 2019: 11 · 2018: 7 · 2017: 13 · 2016: 4 · 2015: 3 · 2014: 3
FWCI: 0.38
Type: journal article
Language: en
Open access: gold
doi.org
Licence: cc-by
creativecommons.org/licenses/by/2.0 (unspecified)
Locations: Journal of Neuroinflammation (publishedVersion, cc-by)
Europe PMC (PubMed Central) (publishedVersion, cc-by)
PubMed Central (publishedVersion, cc-by)
PubMed (publishedVersion)
HAL (submittedVersion, other-oa)
DIGITAL.CSIC (Spanish National Research Council (CSIC)) (submittedVersion, cc-by)
Funders: Itä-Suomen Yliopisto
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Proteoglycans and glycosaminoglycans research
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Protease and Inhibitor Mechanisms
Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
Keywords: ADAMTS1, ADAMTS-4, ADAMTS5, central nervous system injury, stroke, spinal cord injury, synaptic plasticity, neurorepair, angiogenesis, neuroinflammation, therapeutic target
MeSH terms: ADAMTS1 Protein, ADAMTS5 Protein, ADAMTS9 Protein, ADAMTS4 Protein, Animals, Central Nervous System, Humans, Procollagen N-Endopeptidase, ADAM Proteins

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ADAMTS proteoglycanases in the physiological and pathological central nervous system.

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