ECM in brain aging and dementia

Morawski, Markus; Filippov, Mikhail; Tzinia, Athina; Tsilibary, Effie; Vargova, Lydia

doi:10.1016/b978-0-444-63486-3.00010-4

Cited by 84Proteoglycans and glycosaminoglycans researchAlzheimer's disease research and treatmentsNeuroscience and Neuropharmacology Research

ECM in brain aging and dementia

Morawski, Markus, Filippov, Mikhail, Tzinia, Athina, Tsilibary, Effie, Vargova, Lydia·2014·Progress in Brain Research

DOI 10.1016/b978-0-444-63486-3.00010-4

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Abstract

An essential component of the brain extracellular space is the extracellular matrix contributing to the spatial assembly of cells by binding cell-surface adhesion molecules, supporting cell migration, differentiation, and tissue development. The most interesting and complex functions of the central nervous system are the abilities to encode new information (learning) and to store this information (memory). The creation of perineuronal nets, consisting mostly of chondroitin sulfate proteoglycans, stabilizes the synapses and memory trails and forms protective shields against neurodegenerative processes but terminates plasticity and the potential for recovery of the tissue. Age-related changes in the extracellular matrix composition and the extracellular space volume and permissivity are major determinants of the onset and development of the most common neurodegenerative disorder, Alzheimer's disease. In this regard, heparan sulfate proteoglycans, involved in amyloid clearance from the brain, play an important role in Alzheimer's disease and other types of neurodegeneration. Additional key players in the modification of the extracellular matrix are matrix metalloproteinases. Recent studies show that the extracellular matrix and matrix metalloproteinases are important regulators of plasticity, learning, and memory and might be involved in different neurological disorders like epilepsy, schizophrenia, addiction, and dementia. The identification of molecules and mechanisms that modulate these processes is crucial for the understanding of brain function and dysfunction and for the design of new therapeutic approaches targeting the molecular mechanism underlying these neurological disorders.

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Neurotrypsin cleaves agrin locally at the synapse
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Extracellular matrix molecules and synaptic plasticity: immunomapping of intracellular and secreted Reelin in the adult rat brain
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Nonsynaptic communication in the central nervous system
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Selective distribution of matrix metalloproteinase-3 (MMP-3) in Alzheimer’s disease brain
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α3Na+/K+-ATPase Is a Neuronal Receptor for Agrin
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Extracellular matrix glycoproteins and diffusion barriers in human astrocytic tumours
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Bral1: its role in diffusion barrier formation and conduction velocity in the CNS
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Changes in extracellular space size and geometry in APP23 transgenic mice: A model of Alzheimer's disease
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Synapse Loss in Cortex of Agrin-Deficient Mice after Genetic Rescue of Perinatal Death
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Calcium diffusion enhanced after cleavage of negatively charged components of brain extracellular matrix by chondroitinase ABC
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Loss of perineuronal net N-acetylgalactosamine in Alzheimer’s disease
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Matrix metalloproteinases in peripheral blood and cerebrospinal fluid in patients with Alzheimer's disease
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Alterations of matrix metalloproteinases in the healthy elderly with increased risk of prodromal Alzheimer's disease
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Coincident Pre- and Postsynaptic Activation Induces Dendritic Filopodia via Neurotrypsin-Dependent Agrin Cleavage
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Decomposition and long-lasting downregulation of extracellular matrix in perineuronal nets induced by focal cerebral ischemia in rats.
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Learning deficits in aged rats related to decrease in extracellular volume and loss of diffusion anisotropy in hippocampus
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High resolution in situ zymography reveals matrix metalloproteinase activity at glutamatergic synapses
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Perineuronal nets protect against amyloid β-protein neurotoxicity in cultured cortical neurons
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CHEMICAL STUDIES ON ALZHEIMERʼS DISEASE
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Cognitive Decline Is Associated with Reduced Reelin Expression in the Entorhinal Cortex of Aged Rats
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Effects of matrix metalloproteinase inhibition on short‐ and long‐term plasticity of schaffer collateral/CA1 synapses
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Age-related accumulation of Reelin in amyloid-like deposits
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Neurochemical mapping of the human hippocampus reveals perisynaptic matrix around functional synapses in Alzheimer’s disease.
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Reelin depletion is an early phenomenon of Alzheimer's pathology
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Degradation of Soluble and Fibrillar Amyloid β-Protein by Matrix Metalloproteinase (MT1-MMP) in-Vitro
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Reelin signaling in development, maintenance, and plasticity of neural networks
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Aggrecan-based extracellular matrix is an integral part of the human basal ganglia circuit
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Induction of matrix metalloproteinases (MMP3, MMP12 and MMP13) expression in the microglia by amyloid-β stimulation via the PI3K/Akt pathway
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Perilesional Treatment with Chondroitinase ABC and Motor Training Promote Functional Recovery After Stroke in Rats
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Collagen XVIII: a Novel Heparan Sulfate Proteoglycan Associated with Vascular Amyloid Depositions and Senile Plaques in Alzheimer's Disease Brains
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Primary structure and high expression of human agrin in basement membranes of adult lung and kidney
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Early Destruction of the Extracellular Matrix around Parvalbumin-Immunoreactive Interneurons in Creutzfeldt-Jakob Disease
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Heparan Sulfate Accumulation with Aβ Deposits in Alzheimer's Disease and Tg2576 Mice is Contributed by Glial Cells
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Chondroitin sulfate proteoglycans are a common component of neuronal inclusions and astrocytic reaction in neurodegenerative diseases
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Neuroprotective role of MMP-9 overexpression in the brain of Alzheimer's 5xFAD mice.
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Immunohistochemical localization of hyaluronic acid in rat and human brain
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Reduced extracellular space in the brain of tenascin‐R‐ and HNK‐1‐sulphotransferase deficient mice
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“It seems that accumulation of Ab or increased production of the ECM molecules evoked by AD pathogenesis prevents normal decrease in the ECS volume fraction during aging (Sykova et al., 2005a).”
The Collagen Type XVIII Endostatin Domain Is Co-localized with Perlecan in Basement Membranes in Vivo
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Syndecan-2 Induces Filopodia by Active cdc42Hs
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Heparanase overexpression impairs inflammatory response and macrophage-mediated clearance of amyloid-β in murine brain
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Enhanced neuronal plasticity and elevated endogenous sAPPα levels in mice over‐expressing MMP9
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REGULATION OF MATRIX METALLOPROTEINASE 2 BY OLIGOMERIC AMYLOID β PROTEIN
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Unique features of extracellular matrix in the mouse medial nucleus of trapezoid body – Implications for physiological functions
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Concentrations of Matrix Metalloproteinases and their Tissue Inhibitors in the Cerebrospinal Fluid of Patients with Alzheimer's Disease
Mroczko, B., Groblewska, M., Zboch, M., Kulczyńska‐Przybik, A., Koper‐Lenkiewicz, O. M., Szmitkowski, M., Kornhuber, J., & Lewczuk, P. (2014) · Journal of Alzheimer s Disease · doi:10.3233/jad-131634 · Cited by 58 · see citing works
The inhibitory and facilitatory actions of amyloid-β peptides on nicotinic ACh receptors and AMPA receptors
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Abeta(1–40)-induced secretion of matrix metalloproteinase-9 results in sAPPα release by association with cell surface APP
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Matrix metalloproteinases-2 and -3 are reduced in cerebrospinal fluid with low beta-amyloid1–42 levels
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Rostral truncation of a cyclostome,Lampetra japonica, induced by all-trans retinoic acid defines the head/trunk interface of the vertebrate body
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Perineuronal nets are largely unaffected in Alzheimer model Tg2576 mice
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Perineuronal and perisynaptic extracellular matrix in the human spinal cord
Jäger, C., Lendvai, D., Seeger, G., Brückner, G., Matthews, R. T., Arendt, T., Alpár, A., & Morawski, M. (2013) · Neuroscience · doi:10.1016/j.neuroscience.2013.02.014 · Cited by 48 · see citing works
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Vicia villosa lectin-positive neurones in human cerebral cortex. Loss in Alzheimer-type dementia
Kobayashi, K., Emson, P. C., & Mountjoy, C. Q. (1989) · Brain Research · doi:10.1016/0006-8993(89)90416-2 · Cited by 48 · see citing works
Isoforms of agrin are widely expressed in the developing rat and may function as protease inhibitors
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MMP‐2, ‐3 and ‐9 levels and activity are not related to Aβ load in the frontal cortex in Alzheimer's disease
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Transmembrane agrin regulates dendritic filopodia and synapse formation in mature hippocampal neuron cultures
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Clustering transmembrane-agrin induces filopodia-like processes on axons and dendrites
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HIV-I Induced Destruction of Neocortical Extracellular Matrix Components in AIDS Victims
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Glycosaminoglycans in Cortical Autopsy Samples from Alzheimer Brain
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Destruction of extracellular matrix proteoglycans is pervasive in simian retroviral neuroinfection
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The extracellular matrix and diffusion barriers in focal cortical dysplasias
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Reelin-immunoreactive Cajal-Retzius cells: the entorhinal cortex in normal aging and Alzheimer's disease
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Perlecan: The multidomain heparan sulphate proteoglycan of basement membrane and extracellular matrix
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Alzheimer's dementia by circulation disorders: when trees hide the forest
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Matrix Metalloproteinase-9 Participates in NGF-Induced α-Secretase Cleavage of Amyloid-β Protein Precursor in PC12 Cells
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β-amyloid and glutamate receptors
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Interaction between matrix metalloproteinase 3 and the ε4 allele of apolipoprotein E increases the risk of Alzheimer’s disease in Finns
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Assessment of calcium-binding proteins (Parvalbumin and Calbindin D-28K) and perineuronal nets in normal and scrapie-affected adult sheep brains
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Age-Related Changes in Brain Extracellular Space Affect Processing of Amyloid-β Peptides in Alzheimer's Disease
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The Binding of Iron to Perineuronal Nets: A Combined Nuclear Microscopy and Mössbauer Study
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Genetic meta-analysis of diagnosed Alzheimer’s disease identifies new risk loci and implicates Aβ, tau, immunity and lipid processing
Alzheimer Disease Genetics Consortium (ADGC), Kunkle, B. W., The European Alzheimer’s Disease Initiative (EADI), Cohorts for Heart and Aging Research in Genomic Epidemiology Consortium (CHARGE), Genetic and Environmental Risk in AD/Defining Genetic, P. A. E. R. F. A. D. C. (., Grenier-Boley, B., Sims, R., Bis, J. C., Damotte, V., Naj, A. C., et al. (2019) · Nature Genetics · doi:10.1038/s41588-019-0358-2 · Cited by 2,946 · see citing works
Early changes in extracellular matrix in Alzheimer's disease
Lepelletier, F.-X., Mann, D. M. A., Robinson, A., Pinteaux, E., & Boutin, H. (2015) · Neuropathology and Applied Neurobiology · doi:10.1111/nan.12295 · Cited by 192 · see citing works
Experimental evidence for the age dependence of tau protein spread in the brain
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Urinary proteome profiling for stratifying patients with familial Parkinson’s disease
Winter, S. V., Karayel, Ö., Strauss, M. T., Padmanabhan, S., Surface, M., Merchant, K., Alcalay, R. N., & Mann, M. (2021) · EMBO Molecular Medicine · doi:10.15252/emmm.202013257 · Cited by 149 · see citing works
Collagen XVIII in tissue homeostasis and dysregulation — Lessons learned from model organisms and human patients
Heljäsvaara, R., Aikio, M., Ruotsalainen, H. J., & Pihlajaniemi, T. A. (2016) · Matrix Biology · doi:10.1016/j.matbio.2016.10.002 · Cited by 142 · see citing works
The hyaluronan and proteoglycan link proteins: Organizers of the brain extracellular matrix and key molecules for neuronal function and plasticity
Oohashi, T., Edamatsu, M., Bekku, Y., & Carulli, D. (2015) · Experimental Neurology · doi:10.1016/j.expneurol.2015.09.010 · Cited by 131 · see citing works
Pathological changes within the cerebral vasculature in Alzheimer’s disease: New perspectives
Fisher, R. A., Miners, J. S., & Love, S. (2022) · Brain Pathology · doi:10.1111/bpa.13061 · Cited by 127 · see citing works
The Hyaluronidase, TMEM2, Promotes ER Homeostasis and Longevity Independent of the UPRER
Schinzel, R. T., Higuchi‐Sanabria, R., Shalem, O., Moehle, E. A., Webster, B. M., Joe, L. K., Bar‐Ziv, R., Frankino, P. A., Durieux, J., Pender, C. L., et al. (2019) · Cell · doi:10.1016/j.cell.2019.10.018 · Cited by 115 · see citing works
Artificial extracellular matrix scaffolds of mobile molecules enhance maturation of human stem cell-derived neurons
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Protective Properties of Neural Extracellular Matrix
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Authors: Morawski, M., Filippov, M., Tzinia, A., Tsilibary, E., & Vargova, L.
Affiliations: Leipzig University (DE)
German Center for Neurodegenerative Diseases (DE)
National Centre of Scientific Research "Demokritos" (GR)
Corresponding author: Morawski, Markus
ORCID: Morawski, Markus
Filippov, Mikhail
Venue: Progress in Brain Research
Publisher: Elsevier
Published: 2014
Volume: 214
Pages: 207-227
ISSN: 0079-6123 (ISSN-L)
DOI: 10.1016/b978-0-444-63486-3.00010-4
OpenAlex: W2463290683
Cited by: 84
References: 144
Citations by year: 2026: 3 · 2025: 6 · 2024: 3 · 2023: 8 · 2022: 11 · 2021: 7 · 2020: 8 · 2019: 9 · 2018: 7 · 2017: 9 · 2016: 6 · 2015: 4 · 2014: 2 · 2013: 1
FWCI: 10.06
Type: book chapter
Language: en
Open access: closed
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations: Progress in brain research (publishedVersion)
PubMed (publishedVersion)
ASEP (submittedVersion, public-domain)
DZNE Pub (submittedVersion)
Funders: European Commission
Deutsche Forschungsgemeinschaft
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Proteoglycans and glycosaminoglycans research
Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
Keywords: extracellular matrix, brain aging, dementia, Alzheimer's disease, perineuronal nets, chondroitin sulfate proteoglycans, heparan sulfate proteoglycans, amyloid clearance, matrix metalloproteinases, extracellular space, synaptic stability, memory, neuroplasticity, neurodegeneration, epilepsy, schizophrenia, addiction
MeSH terms: Aging, Animals, Brain, Dementia, Extracellular Matrix, Humans

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ECM in brain aging and dementia

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