Matrix Metalloproteinases as New Targets in Alzheimer’s Disease: Opportunities and Challenges

Zipfel, Pauline; Rochais, Christophe; Baranger, Kévin; Rivera, Santiago; Dallemagne, Patrick

doi:10.1021/acs.jmedchem.0c00352

Cited by 97Protease and Inhibitor MechanismsAlzheimer's disease research and treatmentsCholinesterase and Neurodegenerative Diseases

Matrix Metalloproteinases as New Targets in Alzheimer’s Disease: Opportunities and Challenges

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Zipfel, Pauline, Rochais, Christophe, Baranger, Kévin, Rivera, Santiago, Dallemagne, Patrick·2020·Journal of Medicinal Chemistry

DOI 10.1021/acs.jmedchem.0c00352

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Abstract

Although matrix metalloproteinases (MMPs) are implicated in the regulation of numerous physiological processes, evidence of their pathological roles have also been obtained in the last decades, making MMPs attractive therapeutic targets for several diseases. Recent discoveries of their involvement in central nervous system (CNS) disorders, and in particular in Alzheimer's disease (AD), have paved the way to consider MMP modulators as promising therapeutic strategies. Over the past few decades, diverse approaches have been undertaken in the design of therapeutic agents targeting MMPs for various purposes, leading, more recently, to encouraging developments. In this article, we will present recent examples of inhibitors ranging from small molecules and peptidomimetics to biologics. We will also discuss the scientific knowledge that has led to the development of emerging tools and techniques to overcome the challenges of selective MMP inhibition.

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MMPs are known to be linked to extracellular protein degradation including Aβ, whereas MMPs upregulated in AD may also confer neuroinflammation, synaptic dysfunction, and neuronal death.
“MMPs are known to be linked to extracellular protein degradation including Aβ (72), whereas MMPs upregulated in AD may also confer neuroinflammation, synaptic dysfunction, and neuronal death (73, 74).”
From Modeling late-onset Alzheimer’s disease neuropathology via direct neuronal reprogramming (2024) · cites this paper as [74]
The 'General implication of MMPs in AD' section identifies MMPs as Aβ-degrading enzymes and discusses AD-associated MMPs in relation to neuroinflammation and neuronal death. It attributes synaptic deficits to Aβ accumulation, however, rather than stating that upregulated MMPs cause synaptic dysfunction. No page numbers are available in our copy. (LLM, conf=0.84)
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Novel Processing of β-Amyloid Precursor Protein Catalyzed by Membrane Type 1 Matrix Metalloproteinase Releases a Fragment Lacking the Inhibitor Domain against Gelatinase A
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Role of Matrix Metalloproteinases in Migration and Neurotrophic Properties of Nasal Olfactory Stem and Ensheathing Cells
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Self-citation
Selective Inhibition of Membrane Type 1 Matrix Metalloproteinase Abrogates Progression of Experimental Inflammatory Arthritis: Synergy With Tumor Necrosis Factor Blockade
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MT5-MMP Promotes Alzheimer’s Pathogenesis in the Frontal Cortex of 5xFAD Mice and APP Trafficking in vitro
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Sugar‐Based Arylsulfonamide Carboxylates as Selective and Water‐Soluble Matrix Metalloproteinase‐12 Inhibitors
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MMP-9 Inhibitor SB-3CT Attenuates Behavioral Impairments and Hippocampal Loss after Traumatic Brain Injury in Rat
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Abnormal Expression and Distribution of MMP2 at Initial Stages of Alzheimer’s Disease-Related Pathology
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Structure-based design and optimization of pyrimidine- and 1,2,4-triazolo[4,3-a]pyrimidine-based matrix metalloproteinase-10/13 inhibitors via Dimroth rearrangement towards targeted polypharmacology
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Endogenous and synthetic MMP inhibitors in CNS physiopathology.
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Regional and age-related expression of gelatinases in the brains of young and old rats after treatment with kainic acid
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Simple Pseudo-dipeptides with a P2′ Glutamate
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Selective Gelatinase Inhibitor Neuroprotective Agents Cross the Blood-Brain Barrier
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Proamyloidogenic effects of membrane type 1 matrix metalloproteinase involve MMP‐2 and BACE‐1 activities, and the modulation of APP trafficking
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Self-citation
O-Phenyl Carbamate and Phenyl Urea Thiiranes as Selective Matrix Metalloproteinase-2 Inhibitors that Cross the Blood–Brain Barrier
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Matrix metalloproteinase-14 triggers an anti-inflammatory proteolytic cascade in endotoxemia
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Molecular Design of a Highly Selective and Strong Protein Inhibitor against Matrix Metalloproteinase-2 (MMP-2)
Higashi, S., Hirose, T., Takeuchi, T., & Miyazaki, K. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.441758 · Cited by 36 · see citing works
Matrix metalloproteinase-9 regulates neuronal circuit development and excitability
Murase, S., Lantz, C. L., Kim, E., Gupta, N., Higgins, R., Stopfer, M., Hoffman, D. A., & Quinlan, E. M. (2016) · Molecular Neurobiology · doi:10.1007/s12035-015-9295-y · Cited by 35 · see citing works
Identification of novel, exosite-binding matrix metalloproteinase-13 inhibitor scaffolds
Roth, J., Minond, D., Darout, E., Liu, Q., Lauer, J. L., Hodder, P., Fields, G. B., & Roush, W. R. (2011) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2011.09.077 · Cited by 35 · see citing works

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[107](107) Larsen, P. H.; DaSilva, A. G.; Conant, K.; Yong, V. W. Myelin Formation during Development of the CNS Is Delayed in Matrix Metalloproteinase-9 and -12 Null Mice. J. Neurosci. 2006 , 26 (8), 2207-2214. https://doi.org/10.1523/JNEUROSCI.1880-05.2006. - · DOI

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Authors: Zipfel, P., Rochais, C., Baranger, K., Rivera, S., & Dallemagne, P.
Affiliations: Centre d'Etudes et de Recherche sur le Médicament de Normandie (FR)
Centre National de la Recherche Scientifique (FR)
Corresponding author: Dallemagne, Patrick
ORCID: Rochais, Christophe
Baranger, Kévin
Rivera, Santiago
Dallemagne, Patrick
Venue: Journal of Medicinal Chemistry
Publisher: American Chemical Society (ACS)
Published: 2020-05-27
Volume: 63
Issue: 19
Pages: 10705-10725
ISSN: 0022-2623 (ISSN-L)
1520-4804
DOI: 10.1021/acs.jmedchem.0c00352
OpenAlex: W3029030457
Cited by: 94
References: 224
Citations by year: 2026: 11 · 2025: 23 · 2024: 20 · 2023: 15 · 2022: 13 · 2021: 10 · 2020: 2
FWCI: 1.07
Type: journal article
Language: en
Open access: green
arxiv.org
Licence: doi.org/10.15223/policy-029 (stm-asf)
doi.org/10.15223/policy-037 (stm-asf)
doi.org/10.15223/policy-045 (stm-asf)
Locations: Journal of Medicinal Chemistry (publishedVersion)
PubMed (publishedVersion)
arXiv (Cornell University) (submittedVersion)
HAL (submittedVersion, other-oa)
arXiv (Cornell University)
Funders: Agence Nationale de la Recherche
European Regional Development Fund
Aix-Marseille Universit?
Centre National de la Recherche Scientifique
Association France Alzheimer
R?gion Normandie
Excellence Initiative of Aix-Marseille Universit?
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Protease and Inhibitor Mechanisms
Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
Health Sciences › Medicine › Pharmacology › Cholinesterase and Neurodegenerative Diseases
Keywords: matrix metalloproteinases, Alzheimer's disease, matrix metalloproteinase inhibitors, therapeutic target, peptidomimetics, small molecule inhibitors, central nervous system disorders
MeSH terms: Alzheimer Disease, Central Nervous System, Humans, Drug Delivery Systems, Matrix Metalloproteinases, Peptidomimetics, Matrix Metalloproteinase Inhibitors

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Matrix Metalloproteinases as New Targets in Alzheimer’s Disease: Opportunities and Challenges

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