Expression, purification and charaterization of recombinant mouse MT5‐MMP protein products
Open accessAbstract
We have recently identified the fifth member of the membrane-type matrix metalloproteinase subfamily, MT5-MMP/MMP24, which is expressed in a brain specific manner (Duanqing Pei (1999) J. Biol. Chem. 274, 8925-8932). To further characterize its enzymic properties, an expression construct was engineered to produce MT5-MMP as a soluble and active form by truncating its transmembrane domain. Stable expression cell lines were subsequently established from MDCK cells transfected with this construct. Unfortunately, purification of MT5-MMP from the culture media in large quantity proves to be difficult initially due to its rapid turnover via a mechanism which can be inhibited by a broad spectrum metalloproteinase inhibitor, BB94. Thus, BB94 was included in the cell culture medium and throughout the purification process except the final step of chromatography to protect MT5-MMP from destruction. Purified to homogeneity and free of the synthetic inhibitor, MT5-MMP can activate progelatinase A efficiently in a TIMP2 sensitive fashion. A preliminary screen for its potential substrates among extracellular matrix components identified the proteoglycans as the preferred substrates for MT5-MMP. Furthermore, it is determined that the stability of purified MT5-MMP is temperature dependent with rapid destruction at 37 degrees C, but being relatively stable at temperatures 4 degrees C or lower. These observations establish MT5-MMP as a proteoglycanase with a short half-life at body temperature, which may be critical for tightly controlled turnover of ECM components such as those in the brain.
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MMP-2 and MMP-24 directly degrade CSPGs in the brain.
“Two members of this large group of ECM-degrading enzymes have been shown to have direct CSPG-degrading properties in the brain: MMP-2 and MMP-24 (Wang et al., 1999; Zuo et al., 1998)”
From Perineuronal nets and schizophrenia: The importance of neuronal coatings (2014) · cites this paper as Wang et al., 1999
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- Authors
- Wang, X., Yi, J., Lei, J., & Pei, D.
- Affiliations
- University of Minnesota (US)
- Corresponding author
- Pei, Duanqing
- Venue
- FEBS Letters
- Publisher
- Wiley
- Published
- 1999-11-30
- Volume
- 462
- Issue
- 3
- Pages
- 261-266
- ISSN
- 0014-5793 (ISSN-L)
- 1873-3468
- OpenAlex
- W1972486361
- Cited by
- 64
- References
- 26
- Citations by year
- 2026: 2 · 2025: 2 · 2024: 2 · 2021: 2 · 2020: 1 · 2019: 2 · 2018: 2 · 2017: 2 · 2015: 1 · 2014: 2 · 2013: 1 · 2012: 3
- FWCI
- 2.10
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- FEBS Letters (publishedVersion)
- PubMed (publishedVersion)
- Funders
- American Heart Association (9750197N)
- Elsa U. Pardee Foundation
- Wayne State University
- University of Minnesota
- National Cancer Institute (CA 76308)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Protease and Inhibitor Mechanisms
- Health Sciences › Medicine › Rheumatology › Bone and Dental Protein Studies
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biotechnology › Enzyme Production and Characterization
- Keywords
- MMP-24, membrane-type matrix metalloproteinases, proteoglycanase, proteoglycan degradation, TIMP-2, protein stability, brain extracellular matrix, recombinant protein purification, MDCK cells
- MeSH terms
- Animals, Cell Line, Chromatography, Affinity, Dogs, Enzyme Stability, Metalloendopeptidases, Recombinant Proteins, Temperature, Time Factors, Extracellular Matrix Proteins, Mice, Matrix Metalloproteinases, Membrane-Associated
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