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The Metalloprotease Disintegrin ADAM8
Open accessAbstract
ADAMs (a disintegrin and metalloprotease domains) are metalloprotease and disintegrin domain-containing transmembrane glycoproteins with proteolytic, cell adhesion, cell fusion, and cell signaling properties. ADAM8 was originally cloned from monocytic cells, and its distinct expression pattern indicates possible roles in both immunology and neuropathology. Here we describe our analysis of its biochemical properties. In transfected COS-7 cells, ADAM8 is localized to the plasma membrane and processed into two forms derived either by prodomain removal or as remnant protein comprising the extracellular region with the disintegrin domain at the N terminus. Proteolytic removal of the ADAM8 propeptide was completely blocked in mutant ADAM8 with a Glu(330) to Gln exchange (EQ-A8) in the Zn(2+) binding motif (HE(330)LGHNLGMSHD), arguing for autocatalytic prodomain removal. In co-transfection experiments, the ectodomain but not the entire MP domain of ADAM8 was able to remove the prodomain from EQ-ADAM8. With cells expressing ADAM8, cell adhesion to a substrate-bound recombinant ADAM8 disintegrin/Cys-rich domain was observed in the absence of serum, blocked by an antibody directed against the ADAM8 disintegrin domain. Soluble ADAM8 protease, consisting of either the metalloprotease domain or the complete ectodomain, cleaved myelin basic protein and a fluorogenic peptide substrate, and was inhibited by batimastat (BB-94, IC(50) approximately 50 nm) but not by recombinant tissue inhibitor of matrix metalloproteinases 1, 2, 3, and 4. Our findings demonstrate that ADAM8 processing by autocatalysis leads to a potential sheddase and to a form of ADAM8 with a function in cell adhesion.
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“However, loss of its proteolytic activity is predicted in eutherians 42 owing to a single point mutation within its active site (E to Q).”
From Genome analysis of the platypus reveals unique signatures of evolution (2008) · cites this paper as [42]
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Metadata
- Authors
- Schlomann, U., Wildeboer, D., Webster, A., Antropova, O., Zeuschner, D., Knight, C. G., Docherty, A. J. P., Lambert, M., Skelton, L., Jockusch, H., & Bartsch, J. W.
- Affiliations
- Bielefeld University (DE)
- University of Münster (DE)
- University of Cambridge (GB)
- Corresponding author
- Bartsch, Jörg W.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2002-12
- Volume
- 277
- Issue
- 50
- Pages
- 48210-48219
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2121652791
- Cited by
- 171
- References
- 39
- Citations by year
- 2026: 5 · 2025: 6 · 2024: 5 · 2023: 8 · 2022: 2 · 2021: 9 · 2020: 5 · 2019: 9 · 2018: 5 · 2017: 5 · 2016: 5 · 2015: 5 · 2014: 4 · 2013: 5 · 2012: 10
- FWCI
- 3.16
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Middlesex University Research Repository (Middlesex University Of London) (submittedVersion)
- Research Portal (King's College London) (submittedVersion)
- PUB – Publications at Bielefeld University (Bielefeld University) (submittedVersion)
- Publikationen an der Universität Bielefeld (Universität Bielefeld) (submittedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Protease and Inhibitor Mechanisms
- Health Sciences › Medicine › Hematology › Blood Coagulation and Thrombosis Mechanisms
- Health Sciences › Medicine › Immunology and Allergy › Cell Adhesion Molecules Research
- Keywords
- ADAM8, ADAM metalloproteinases, disintegrin domain, autocatalytic cleavage, zinc-binding motif, cell adhesion, batimastat, tissue inhibitors of metalloproteinases, sheddases, plasma membrane localization, monocytic cells
- MeSH terms
- Amino Acid Sequence, Animals, Base Sequence, Catalysis, Cell Adhesion, Hydrolysis, Membrane Proteins, Metalloendopeptidases, Tumor Cells, Cultured, Antigens, CD, DNA Primers, COS Cells, Mice, ADAM Proteins
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