Part-Time α-Secretases: The Functional Biology of ADAM 9, 10 and 17
Abstract
Disintegrin metalloproteases of the ADAM family form a large (at present > 40 members in mammals) family of multidomain membrane proteins that in their ectodomain combine a cystein-rich, disintegrin and a zinc metalloprotease domain. Via their metalloprotease domain, ADAMs are often implicated in ectodomain shedding, either to release e.g. growth factors or to initiate further intracellular signalling via regulated intramembrane proteolysis. Mainly based upon overexpression studies in vehicle cells, three of them, ADAMs 9, 10 and 17, have been proposed to act as alpha-secretases for amyloid precursor protein (APP). It is striking thereby that this role has since then remained somewhat ill-defined, as APP processing in ADAM9 deficient neurons is unaltered, and also ADAM10 deficient murine embryonic fibroblasts exhibit at best a highly variable reduction in alpha-secretase activity. However, during the past years, numerous other substrates have been linked to all three sheddases, the cleavage of which in some cases appears to be strikingly more important for the organism than APP processing. Most notably, the perinatally lethal phenotype of ADAM17 knockout mice is dominated by a loss of growth factor shedding, while the even earlier fatal effects of ADAM10 deficiency exhibit key features of disabled Notch signalling and possibly also cadherin processing defects. In this review, we will summarize the published data on the "non-APP" functions of all three ADAMs, the further evaluation of which may be crucial when attempting to treat Alzheimer s Disease by increasing their expression and/or activity. As the knockouts of ADAM10 and ADAM17 are only informative for their roles in (early) development, while a number of recently assigned new substrates play crucial roles in the normal and/or diseased adult organism as well, work on conditional knockout models will be crucial to fully characterize both the full functional portfolio of (candidate) alpha-secretases as well as their clinical relevance, which may go way beyond Alzheimer s Disease.
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ADAM17 is implicated in AD, and its protein product is known to carry α-secretase activity as ADAM10.
“However, we implicate ADAM17, a gene whose protein product is known to carry α-secretase activity as ADAM10 (ref. 24).”
From New insights into the genetic etiology of Alzheimer’s disease and related dementias (2022) · cites this paper as [24]
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- Authors
- Deuss, M., Reiss, K., & Hartmann, D.
- Affiliations
- University of Bonn (DE)
- Corresponding author
- Hartmann, Dieter
- Venue
- Current Alzheimer Research
- Publisher
- Bentham Science Publishers Ltd.
- Published
- 2008-04-01
- Volume
- 5
- Issue
- 2
- Pages
- 187-201
- ISSN
- 1567-2050 (ISSN-L)
- OpenAlex
- W2011690803
- Cited by
- 98
- References
- 0
- Citations by year
- 2025: 4 · 2024: 1 · 2023: 2 · 2022: 2 · 2021: 4 · 2020: 6 · 2019: 6 · 2018: 2 · 2017: 5 · 2016: 6 · 2015: 6 · 2014: 6 · 2013: 6 · 2012: 5
- FWCI
- 8.13
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Current Alzheimer Research (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Protease and Inhibitor Mechanisms
- Health Sciences › Medicine › Oncology › Peptidase Inhibition and Analysis
- Keywords
- ADAM9, ADAM10, ADAM17, alpha-secretase, APP processing, regulated intramembrane proteolysis, ectodomain shedding, Notch signaling, Alzheimer's disease
- MeSH terms
- ADAM10 Protein, ADAM17 Protein, Alzheimer Disease, Animals, Humans, Membrane Proteins, Protein Conformation, Ephrins, ADAM Proteins, Amyloid Precursor Protein Secretases
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
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