Pathophysiological function of ADAMTS enzymes on molecular mechanism of Alzheimer’s disease
Open accessAbstract
The extracellular matrix (ECM) is an environment that has various enzymes attended in regeneration and restoration processes which is very important to sustain physiological and biological functions of central nervous system (CNS). One of the participating enzyme systems in ECM turnover is matrix metalloproteinases. A disintegrin-like and metalloproteinase with thrombospondin type 1 motifs (ADAMTS) is a unique family of ECM proteases found in mammals. Components of this family may be distinguished from the ADAM (A Disintegrin and Metalloproteinase) family based on the multiple copies of thrombospondin 1-like repeats. The considerable role of the ADAMTS in the CNS continues to develop. Evidences indicate that ADAMTS play an important role in neuroplasticity as well as nervous system pathologies such as Alzheimer's disease (AD). It is hopeful and possible that ADAMTS family members may be utilized to develop therapies for CNS pathologies, ischemic injuries, neurodegenerative and neurological diseases. To understand and provide definitive data on ADAMTS to improve structural and functional recovery in CNS injury and diseases, this review aimed to enlighten the subject extensively to reach certain information on metalloproteinases and related molecules/enzymes. It will be interesting to examine how ADAMTS expression and action would affect the initiation/progression of above-mentioned clinical situations, especially AD.
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ADAMTS1 has been implicated in AD both biochemically and genetically.
“ADAMTS1 has been implicated in AD both biochemically88 and genetically.6”
From Single nucleus multiomics identifies ZEB1 and MAFB as candidate regulators of Alzheimer’s disease-specific cis-regulatory elements (2023) · cites this paper as [88]
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- Authors
- Gurses, M. S., Ural, M. N., Gulec, M. A., Akyol, O., & Akyol, S.
- Affiliations
- Bursa Uludağ Üni̇versi̇tesi̇ (TR)
- Turgut Özal University (TR)
- Venue
- Aging and disease
- Publisher
- Aging and Disease
- Published
- 2016
- Volume
- 7
- Issue
- 4
- Pages
- 479
- ISSN
- 2152-5250 (ISSN-L)
- PMC
- PMC4963191
- OpenAlex
- W2493883729
- Cited by
- 35
- References
- 88
- Citations by year
- 2026: 3 · 2025: 6 · 2024: 8 · 2023: 7 · 2022: 1 · 2021: 3 · 2020: 3 · 2019: 2 · 2018: 1 · 2017: 1
- FWCI
- 0.12
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- cc-by
- Locations
- Aging and Disease (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, other-oa)
- PubMed Central (publishedVersion, other-oa)
- PubMed (publishedVersion)
- Bursa Uludag University - AVESIS (submittedVersion)
- Malatya Turgut Özal University Institutional Repository (submittedVersion, other-oa)
- Hacettepe University Institutional Repository (hacettepe.edu.tr) (submittedVersion, other-oa)
- 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 › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Keywords
- Alzheimer's disease, extracellular matrix, matrix metalloproteinases, ADAM family, neuroplasticity, neurodegenerative diseases, central nervous system injury, pathogenesis
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