The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.
The Angiopoietin-Like Protein 3 and 8 Complex Interacts with Lipoprotein Lipase and Induces LPL Cleavage
Abstract
Lipoprotein lipase (LPL) is the key enzyme that hydrolyzes triglycerides from triglyceride-rich lipoproteins. Angiopoietin-like proteins (ANGPTL) 3, 4, and 8 are well-characterized protein inhibitors of LPL. ANGPTL8 forms a complex with ANGPTL3, and the complex is a potent endogenous inhibitor of LPL. However, the nature of the structural interaction between ANGPTL3/8 and LPL is unknown. To probe the conformational changes in LPL induced by ANGPTL3/8, we found that HDX-MS detected significantly altered deuteration in the lid region, ApoC2 binding site, and furin cleavage region of LPL in the presence of ANGPTL3/8. Supporting this HDX structural evidence, we found that ANGPTL3/8 inhibits LPL enzymatic activities and increases LPL cleavage. ANGPTL3/8-induced effects on LPL activity and LPL cleavage are much stronger than those of ANGPTL3 or ANGPTL8 alone. ANGPTL3/8-mediated LPL cleavage is blocked by both an ANGPTL3 antibody and a furin inhibitor. Knock-down of furin expression by siRNA significantly reduced ANGPT3/8-induced cleavage of LPL. Our data suggest ANGPTL3/8 promotes furin-mediated LPL cleavage.
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In the citing paper
“One recent study suggested that ANGPTL3-ANGPTL8 complexes promote furin-mediated cleavage of LPL, but the levels of cleavage observed were not sufficient to explain the level of LPL inhibition (179).”
From Regulation of lipoprotein metabolism by ANGPTL3, ANGPTL4, and ANGPTL8 (2021) · cites this paper as [179]
In the citing paper
“As the ANGPTL3-ANGPTL8 complex is the functional unit of LPL inhibition, Evinacumab likely acts to lower plasma triglycerides by binding the ANGPTL3 of ANGPTL3-ANGPTL8 complexes.”
From Regulation of lipoprotein metabolism by ANGPTL3, ANGPTL4, and ANGPTL8 (2021) · cites this paper as [179]
In the citing paper
“Indeed, Jin et al. (179) showed that Evinacumab could robustly block inhibition by ANGPTL3-ANGPTL8 complexes.”
From Regulation of lipoprotein metabolism by ANGPTL3, ANGPTL4, and ANGPTL8 (2021) · cites this paper as [179]
Citations
Cites
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Sorted by citations
Regulation of lipoprotein metabolism by ANGPTL3, ANGPTL4, and ANGPTL8
Sylvers-Davie, K. L., & Davies, B. S. J. (2021) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00195.2021 · Cited by 154
Metadata
- Authors
- Jin, N., Matter, W. F., Michael, L. F., Qian, Y., Gheyi, T., Cano, L., Perez, C., Lafuente, C., Broughton, H. B., & Espada, A.
- Affiliations
- Diabetes and Complications Therapeutic Area, Lilly Research Laboratories, Eli Lilly and Company, Indianapolis, Indiana 46285, United States
- Laboratory for Experimental Medicine, Lilly Research Laboratories, Eli Lilly and Company, Indianapolis, Indiana 46285, United States
- Lilly Biotechnology Center, Eli Lilly and Company, San Diego, California 92121, United States
- Centro de Investigación Lilly S.A., 28108 Alcobendas, Spain
- ORCID
- Espada, Alfonso
- Venue
- ACS Chemical Biology
- Publisher
- American Chemical Society (ACS)
- Published
- 2021-03-03
- Volume
- 16
- Issue
- 3
- Pages
- 457-462
- ISSN
- 1554-8929
- 1554-8937
- Cited by
- 36
- References
- 3
- Language
- en
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Cite CoChat for the checks on this page, and the paper for its own findings.
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- CoChat. (2026). Citation check: The Angiopoietin-Like Protein 3 and 8 Complex Interacts with Lipoprotein Lipase and Induces LPL Cleavage. https://app.cochat.ai/papers/10.1021/acschembio.0c00954
- The paper
- Jin, N., Matter, W. F., Michael, L. F., Qian, Y., Gheyi, T., Cano, L., Perez, C., Lafuente, C., Broughton, H. B., & Espada, A. (2021). The Angiopoietin-Like Protein 3 and 8 Complex Interacts with Lipoprotein Lipase and Induces LPL Cleavage. ACS Chemical Biology. https://doi.org/10.1021/acschembio.0c00954
