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MMP‐2 inhibits PCSK9‐induced degradation of the LDL receptor in Hepa1‐c1c7 cells
Abstract
Low‐density lipoprotein receptor (LDLR) catalyzes the uptake of LDL‐cholesterol by liver and peripheral organs. The function of the LDLR is antagonized by pro‐protein convertase subtilisin/kexin type 9 (PCSK9), which binds to LDLR at the plasma membrane inducing LDLR degradation. Here, we report that matrix metalloproteinase‐2 (MMP‐2) interacts with and cleaves PCSK9, as evidenced by proteomic, chemical cross‐linkage, blue native‐PAGE and domain‐specific antibodies Western blot analyses. Furthermore, MMP‐2 overexpression renders Hepa1‐c1c7 cells resistant to PCSK9‐induced LDLR degradation. The data suggest that pathological MMP‐2 overexpression may protect the LDLR from PCSK‐9‐induced degradation.
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Active MMP2 can cleave PCSK9.
“We have previously reported that active MMP2 can cleave PCSK923.”
From Membrane type 1 matrix metalloproteinase promotes LDL receptor shedding and accelerates the development of atherosclerosis (2021) · cites this paper as [23]
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Research works printed but not linked: 10
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- 10.1016/j.jacc.2013.07.056 · DOI
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- Fernandez-Patron C., 1992, Reverse staining of sodium dodecyl sulfate polyacrylamide gels by imidazole‐zinc salts: sensitive detection of unmodified proteins, Biotechniques, 12, 564
- 10.1021/ac402802a · DOI
Cited by
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Alabi, A., Xia, X.-D., Gu, H.-M., Wang, F., Deng, S.-J., Yang, N., Adijiang, A., Douglas, D. N., Kneteman, N. M., Xue, Y., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-22167-3 · Cited by 63
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Metadata
- Authors
- Wang, X., Berry, E., Hernandez-Anzaldo, S., Sun, D., Adijiang, A., Li, L., Zhang, D., & Fernandez-Patron, C.
- Venue
- FEBS Letters
- Publisher
- Wiley
- Published
- 2015-01-19
- Volume
- 589
- Issue
- 4
- Pages
- 490-496
- ISSN
- 0014-5793
- 1873-3468
- Cited by
- 15
- References
- 0
- Language
- en
- Funders
- Canadian Institutes of Health Research (RES0011328)
- Natural Sciences and Engineering Research Council of Canada (RES0004433)
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