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Proteolysis of the low density lipoprotein receptor by bone morphogenetic protein-1 regulates cellular cholesterol uptake
Abstract
The development of cardiovascular disease is intimately linked to elevated levels of low-density lipoprotein (LDL) cholesterol in the blood. Hepatic LDL receptor (LDLR) levels regulate the amount of plasma LDL. We identified the secreted zinc metalloproteinase, bone morphogenetic protein 1 (BMP1), as responsible for the cleavage of human LDLR within its extracellular ligand-binding repeats at Gly 171↓Asp 172. The resulting 120 kDa membrane-bound C-terminal fragment (CTF) of LDLR had reduced capacity to bind LDL and when expressed in LDLR null cells had compromised LDL uptake as compared to the full length receptor. Pharmacological inhibition of BMP1 or siRNA-mediated knockdown prevented the generation of the 120 kDa CTF and resulted in an increase in LDL uptake into cells. The 120 kDa CTF was detected in the livers from humans and mice expressing human LDLR. Collectively, these results identify that BMP1 regulates cellular LDL uptake and may provide a target to modulate plasma LDL cholesterol.
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Two zinc metalloproteases, MT1-MMP and BMP1, also cleave the LDLR.
“In addition to the proteolytic cleavage of the LDLR by γ-secretase, two zinc metalloproteases also cleave the receptor, MT1-MMP and BMP1.”
From Post-translational regulation of the low-density lipoprotein receptor provides new targets for cholesterol regulation (2024) · cites this paper as [37]
The Results section, “The zinc metalloprotease BMP1 cleaves the LDLR in its ligand binding domain” (page unavailable), confirms that BMP1 cleaves human LDLR. The Introduction also mentions γ-secretase-mediated cleavage, but the passages found in our copy do not identify MT1-MMP as an LDLR-cleaving protease (searched: MT1-MMP and membrane type 1 matrix metalloproteinase). (LLM, conf=0.88)
Experimental — accuracy not yet measuredBMP1 is involved in cleaving the LDLR in human primary hepatocytes and in human liver and adrenal samples.
“However, there is evidence that BMP1 is involved in cleaving the LDLR in human primary hepatocytes and in human liver and adrenal samples [37,61,63], and the 36–40 kDa N-terminal fragment is present in human urine, likely due to clearance from the blood plasma by the kidneys [61].”
From Post-translational regulation of the low-density lipoprotein receptor provides new targets for cholesterol regulation (2024) · cites this paper as [37]
The Results (no page given) report a cleaved LDLR fragment in human liver samples, and the Discussion says human LDLR is likely cleaved there by BMP1. But the Methods identify the studied liver-derived and adrenal cells as HepG2 and SW13 carcinoma cell lines, not primary human hepatocytes or human adrenal tissue samples. (LLM, conf=0.89)
Experimental — accuracy not yet measuredBMP1 cleavage within the ligand binding domain of LDLR significantly reduces the affinity of the receptor for LDL, decreasing the ability of the LDLR to bind and internalise LDL.
“BMP1 cleavage within the ligand binding domain of the LDLR significantly reduces the affinity of the receptor for LDL, decreasing the ability of the LDLR to bind and internalise LDL [37].”
From Post-translational regulation of the low-density lipoprotein receptor provides new targets for cholesterol regulation (2024) · cites this paper as [37]
The Results sections report that BMP1 cleaves LDLR in its ligand-binding domain and that the resulting fragment shows significantly reduced LDL binding and cellular uptake. The paper does not report a direct measurement of receptor–LDL affinity, so that more specific part of the claim is not established. (LLM, conf=0.82)
Experimental — accuracy not yet measuredThe site of cleavage in human LDLR by BMP1 is highly specific, between residues Gly192 and Asp193, with the Asp residue being crucial for cleavage.
“The site of cleavage in human LDLR by BMP1 is highly specific, between residues Gly192 and Asp193, with the Asp residue being crucial for cleavage [37,61,63].”
From Post-translational regulation of the low-density lipoprotein receptor provides new targets for cholesterol regulation (2024) · cites this paper as [37]
The Results section, “The zinc metalloprotease BMP1 cleaves the LDLR in its ligand binding domain” (page unavailable), identifies the human LDLR cleavage bond as Gly171–Asp172, not Gly192–Asp193. The Results section, “Human but not murine LDLR is proteolytically cleaved by BMP1 in vivo” (page unavailable), supports the Asp-residue claim: replacing Asp172 with Val prevented cleavage. (LLM, conf=0.90)
Experimental — accuracy not yet measuredsiRNA-mediated silencing or ablation of BMP1 in HepG2 and CHO cells increased the levels of full-length LDLR and dramatically decreased the appearance of the truncated LDLR.
“Second, siRNA-mediated silencing or ablation of BPM1 in HepG2 and CHO cells increased the levels of full-length LDLR and dramatically decreased the appearance of the truncated LDLR [56,57].”
From The low-density lipoprotein receptor: Emerging post-transcriptional regulatory mechanisms (2025) · cites this paper as [56]
The Results section (Fig. 3; page unavailable) reports that BMP1 siRNA knockdown in HepG2 cells almost completely abolished production of the truncated LDLR fragments. Its rescue experiment also links BMP1 activity to a decrease in full-length LDLR. The Methods section describes CHO-A7 cells transfected with LDLR constructs, not BMP1 silencing or ablation in those cells; the claim’s CHO-cell and ablation portions are unsupported. (LLM, conf=0.87)
Experimental — accuracy not yet measured
BMP1 does not cleave murine LDLR because the cleavage-essential Asp193 is replaced with valine in mice.
“Intriguingly, BMP1 does not cleave murine LDLR [56,108] since the cleavage-essential Asp193 is replaced with valine in mice.”
From The low-density lipoprotein receptor: Emerging post-transcriptional regulatory mechanisms (2025) · cites this paper as [56]
The Results section reports that BMP1 did not cleave murine LDLR and that replacing the critical aspartate with valine prevented cleavage of human LDLR. However, it identifies the residue as Asp172, not Asp193, so the claim's residue number is not supported. (LLM, conf=0.90)
Experimental — accuracy not yet measuredThe cleaved N-terminal fragment of LDLR is detected in human urine, providing evidence that LDLR is cleaved by BMP1 in humans.
“The cleaved N-terminal fragment of LDLR is detected in human urine, providing evidence that LDLR is cleaved by BMP1 in humans110,111.”
From Pathways and Molecular Mechanisms Governing LDL Receptor Regulation (2025) · cites this paper as [110]
The Results section reports a cleaved LDLR fragment in human liver samples and shows that BMP1 cleaves human LDLR experimentally; the Discussion describes BMP1 as the likely protease in vivo. The paper detects the soluble N-terminal fragment in HepG2 cell culture medium, not human urine. The urine-specific evidence attributed to this source is therefore unsupported. (LLM, conf=0.88)
Experimental — accuracy not yet measuredBinding of RAP to the LDLR can block LDLR proteolytic cleavage by BMP1.
“In addition, the binding of RAP to the LDLR can influence the activity of other processing mechanisms that regulate the LDLR, such as blocking LDLR proteolytic cleavage by bone morphogenetic protein-1 (BMP1) [37] (see below).”
From Post-translational regulation of the low-density lipoprotein receptor provides new targets for cholesterol regulation (2024) · cites this paper as [37]
Murine LDLR is not cleaved by BMP1.
“In murine LDLR, this Asp residue is replaced with a Val and murine LDLR is not cleaved by BMP1 [37], so studies in mice expressing wild-type LDLR would not reveal whether cleavage of the receptor by BMP1 has any impact on LDL-cholesterol metabolism.”
From Post-translational regulation of the low-density lipoprotein receptor provides new targets for cholesterol regulation (2024) · cites this paper as [37]
In murine LDLR, the Asp residue is replaced with a Val.
“In murine LDLR, this Asp residue is replaced with a Val and murine LDLR is not cleaved by BMP1 [37], so studies in mice expressing wild-type LDLR would not reveal whether cleavage of the receptor by BMP1 has any impact on LDL-cholesterol metabolism.”
From Post-translational regulation of the low-density lipoprotein receptor provides new targets for cholesterol regulation (2024) · cites this paper as [37]
BMP1-mediated cleavage of LDLR releases a small N-terminal fragment of 36-40 kDa and retains a C-terminal fragment of 120 kDa in the plasma membrane.
“The BMP1-mediated cleavage of LDLR releases a small N-terminal fragment of 36–40 kDa and retains a C-terminal fragment of 120 kDa in the plasma membrane (Figure 1I) [37,61].”
From Post-translational regulation of the low-density lipoprotein receptor provides new targets for cholesterol regulation (2024) · cites this paper as [37]
Two independent research groups identified BMP1 as the enzyme responsible for cleavage of LDLR in the linker region between LA4 and LA5.
“Two independent research groups have identified Bone morphogenetic protein 1 (BMP1), a secreted zinc-dependent metalloprotease, as the enzyme responsible for this event [56,57].”
From The low-density lipoprotein receptor: Emerging post-transcriptional regulatory mechanisms (2025) · cites this paper as [56]
The LDLR is cleaved in the linker region between LA repeat 4 and 5, with Asp193 being crucial for this cleavage.
“Multiple studies have shown that the LDLR is cleaved in the linker region between LA repeat 4 and 5 [107], with Asp193 being crucial for this cleavage [56,106].”
From The low-density lipoprotein receptor: Emerging post-transcriptional regulatory mechanisms (2025) · cites this paper as [56]
BMP1 cleaves LDLR within its ligand binding domain, releasing a small N-terminal fragment and retaining a 120kDa membrane-bound C-terminal fragment.
“In contrast to MT1-MMP, BMP cleaves LDLR within its ligand binding domain, releasing a small N-terminal fragment, and retaining a 120kDa membrane-bound C-terminal fragment (Fig. 7C)110,111.”
From Pathways and Molecular Mechanisms Governing LDL Receptor Regulation (2025) · cites this paper as [110]
miR-1908-5p targets TGF-β mRNA, an activator of BMP1, which promotes cleavage and functional inactivation of the LDLR.
“miR-1908-5p targets TGF-β mRNA, an activator of the metalloprotease BMP1, which, as discussed below, promotes cleavage and functional inactivation of the LDLR [56,57].”
From The low-density lipoprotein receptor: Emerging post-transcriptional regulatory mechanisms (2025) · cites this paper as [56]
BMP1 promotes ectodomain shedding of LDLR, decreasing LDLR.
“BMP1 Promotes ectodomain shedding of LDLR ↓ [56,57]”
From The low-density lipoprotein receptor: Emerging post-transcriptional regulatory mechanisms (2025) · cites this paper as [56]
Disruption of the LDLR ligand binding domain reduces the receptor's affinity for LDL, thereby reducing its ability to bind and internalize LDL.
“The disruption of the ligand binding domain reduces affinity of the receptor for LDL, thereby reducing the ability to bind and internalize LDL110.”
From Pathways and Molecular Mechanisms Governing LDL Receptor Regulation (2025) · cites this paper as [110]
The BMP1 cleavage site in human LDLR is between Gly192 and Asp193, and the aspartate residue is critical for cleavage.
“Importantly, the BMP1 cleavage site in human LDLR is between Gly192 and Asp193, with the aspartate residue being critical for cleavage to occur110,”
From Pathways and Molecular Mechanisms Governing LDL Receptor Regulation (2025) · cites this paper as [110]
In mice, Asp193 is replaced with a valine residue and mouse LDLR is not cleaved by BMP1.
“although in mice, Asp193 is replaced with a valine residue and mouse LDLR is not cleaved by BMP1110.”
From Pathways and Molecular Mechanisms Governing LDL Receptor Regulation (2025) · cites this paper as [110]
Cleavage of the LDLR in its LDL-binding domain by BMP1 reduces the ability of the LDLR to bind and internalise LDL-cholesterol at the cell surface.
“Shedding of the extracellular domain of the receptor by membrane-type 1 matrix metalloprotease and cleavage of the receptor in its LDL-binding domain by bone morphogenetic protein-1 reduces the ability of the LDLR to bind and internalise LDL-cholesterol at the cell surface.”
From Post-translational regulation of the low-density lipoprotein receptor provides new targets for cholesterol regulation (2024) · cites this paper as [37]
BMP1 cleaves the LDLR within the ligand binding domain, between LA repeats 4 and 5.
“BMP1 cleaves the LDLR within the ligand binding domain (Figure 2), between LA repeats 4 and 5 where the linker between the repeats is slightly larger, at 12 amino acids rather than 4–5 amino acids as in the linkers between the other LA repeats [37].”
From Post-translational regulation of the low-density lipoprotein receptor provides new targets for cholesterol regulation (2024) · cites this paper as [37]
The linker between LA repeats 4 and 5 is 12 amino acids, rather than 4-5 amino acids as in linkers between other LA repeats.
“BMP1 cleaves the LDLR within the ligand binding domain (Figure 2), between LA repeats 4 and 5 where the linker between the repeats is slightly larger, at 12 amino acids rather than 4–5 amino acids as in the linkers between the other LA repeats [37].”
From Post-translational regulation of the low-density lipoprotein receptor provides new targets for cholesterol regulation (2024) · cites this paper as [37]
In transgenic mice in which one allele of mouse Ldlr was replaced by human LDLR, cleavage of the human LDLR protein was observed in the liver, consistent with BMP1 acting on it in a physiologic setting.
“In this model cleavage of the human LDLR protein could be observed in the liver, consistent with BMP1 acting on it in a physiologic setting.”
From The low-density lipoprotein receptor: Emerging post-transcriptional regulatory mechanisms (2025) · cites this paper as [56]
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Cites
The LXR–Idol Axis Differentially Regulates Plasma LDL Levels in Primates and Mice
Hong, C., Marshall, S. M., McDaniel, A. L., Graham, M., Layne, J. D., Cai, L., Scotti, E., Boyadjian, R., Kim, J., Chamberlain, B. T., et al. (2014) · Cell Metabolism · doi:10.1016/j.cmet.2014.10.001 · Cited by 87
γ-secretase inhibition lowers plasma triglyceride-rich lipoproteins by stabilizing the LDL receptor
Kim, K., Goldberg, I. J., Graham, M. J., Sundaram, M., Bertaggia, E., Lee, S. X., Qiang, L., Haeusler, R. A., Metzger, D., Chambon, P., et al. (2018) · Cell Metabolism · doi:10.1016/j.cmet.2018.02.010 · Cited by 26
Flagged first, then by citations
Research works printed but not linked: 32
- Vincent, J. Reducing elevated plasma LDL cholesterol: the central role of the LDL receptor. Clin Pharmacol Ther 96, 3–7, https://doi.org/10.1038/clpt.2014.95 (2014). · DOI · Paper page
- Ference, B. A. et al. Low-density lipoproteins cause atherosclerotic cardiovascular disease. 1. Evidence from genetic, epidemiologic, and clinical studies. A consensus statement from the European Atherosclerosis Society Consensus Panel. Eur Heart J 38, 2459–2472, https://doi.org/10.1093/eurheartj/ehx144 (2017). · DOI · Paper page
- Rader, D. J. New Therapeutic Approaches to the Treatment of Dyslipidemia. Cell Metab 23, 405–412, https://doi.org/10.1016/j.cmet.2016.01.005 (2016). · DOI
- Laufs, U., Scharnagl, H. & Marz, W. Statin intolerance. Curr Opin Lipidol 26, 492–501, https://doi.org/10.1097/MOL.0000000000000236 (2015). · DOI
- Zelcer, N., Hong, C., Boyadjian, R. & Tontonoz, P. LXR regulates cholesterol uptake through Idol-dependent ubiquitination of the LDL receptor. Science 325, 100–104, https://doi.org/10.1126/science.1168974 (2009). · DOI · Paper page
- Benjannet, S. et al. NARC-1/PCSK9 and its natural mutants: zymogen cleavage and effects on the low density lipoprotein (LDL) receptor and LDL cholesterol. J Biol Chem 279, 48865–48875, https://doi.org/10.1074/jbc.M409699200 (2004). · DOI · Paper page
- Park, S. W., Moon, Y. A. & Horton, J. D. Post-transcriptional regulation of low density lipoprotein receptor protein by proprotein convertase subtilisin/kexin type 9a in mouse liver. J Biol Chem 279, 50630–50638, https://doi.org/10.1074/jbc.M410077200 (2004). · DOI · Paper page
- McGettigan, P. & Ferner, R. E. PCSK9 inhibitors for hypercholesterolaemia. BMJ 356, j188, https://doi.org/10.1136/bmj.j188 (2017). · DOI
- Lo Surdo, P. et al. Mechanistic implications for LDL receptor degradation from the PCSK9/LDLR structure at neutral pH. EMBO Rep 12, 1300–1305, https://doi.org/10.1038/embor.2011.205 (2011). · DOI · Paper page
- Tveten, K. et al. Characterization of a naturally occurring degradation product of the LDL receptor. Mol Genet Metab 105, 149–154, https://doi.org/10.1016/j.ymgme.2011.10.008 (2012). · DOI · Paper page
- Fish, P. V. et al. Potent and Selective Nonpeptidic Inhibitors of Procollagen C-Proteinase. J. Med. Chem. 50, 3442–3456, https://doi.org/10.1021/jm061010z (2007). · DOI
- Krieger, M. Complementation of mutations in the LDL pathway of receptor-mediated endocytosis by cocultivation of LDL receptor-defective hamster cell mutants. Cell 33, 413–422 (1983). · DOI
- Garrigue-Antar, L., Barker, C. & Kadler, K. E. Identification of amino acid residues in bone morphogenetic protein-1 important for procollagen C-proteinase activity. J Biol Chem 276, 26237–26242, https://doi.org/10.1074/jbc.M010814200 (2001). · DOI
- Kessler, E. In Handbook of Proteolytic Enzymes Vol. 1 (eds Barrett, A. J., Rawlings, N. D. & Woessner, J. F.) 609–617 (Academic Press, 2004). · DOI
- Knouff, C., Malloy, S., Wilder, J., Altenburg, M. K. & Maeda, N. Doubling expression of the low density lipoprotein receptor by truncation of the 3′-untranslated region sequence ameliorates type iii hyperlipoproteinemia in mice expressing the human apoe2 isoform. J Biol Chem 276, 3856–3862, https://doi.org/10.1074/jbc.M009423200 (2001). · DOI · Paper page
- Maxwell, K. N., Fisher, E. A. & Breslow, J. L. Overexpression of PCSK9 accelerates the degradation of the LDLR in a post-endoplasmic reticulum compartment. Proc Natl Acad Sci USA 102, 2069–2074, https://doi.org/10.1073/pnas.0409736102 (2005). · DOI · Paper page
- Lehrman, M. A., Goldstein, J. L., Brown, M. S., Russell, D. W. & Schneider, W. J. Internalization-defective LDL receptors produced by genes with nonsense and frameshift mutations that truncate the cytoplasmic domain. Cell 41, 735–743 (1985). · DOI
- Rudenko, G. et al. Structure of the LDL receptor extracellular domain at endosomal pH. Science 298, 2353–2358, https://doi.org/10.1126/science.1078124 (2002). · DOI · Paper page
- Hopkins, D. R., Keles, S. & Greenspan, D. S. The bone morphogenetic protein 1/Tolloid-like metalloproteinases. Matrix Biol 26, 508–523, https://doi.org/10.1016/j.matbio.2007.05.004 (2007). · DOI
- Troilo, H. et al. Mammalian tolloid proteinases: role in growth factor signalling. FEBS Lett 590, 2398–2407, https://doi.org/10.1002/1873-3468.12287 (2016). · DOI
- Esser, V., Limbird, L. E., Brown, M. S., Goldstein, J. L. & Russell, D. W. Mutational analysis of the ligand binding domain of the low density lipoprotein receptor. J Biol Chem 263, 13282–13290 (1988). · DOI · Paper page
- Russell, D. W., Brown, M. S. & Goldstein, J. L. Different combinations of cysteine-rich repeats mediate binding of low density lipoprotein receptor to two different proteins. J Biol Chem 264, 21682–21688 (1989). · DOI · Paper page
- Bu, G., Geuze, H. J., Strous, G. J. & Schwartz, A. L. 39 kDa receptor-associated protein is an ER resident protein and molecular chaperone for LDL receptor-related protein. EMBO J 14, 2269–2280 (1995). · DOI · Paper page
- Tai, M. H. et al. Curcumin enhances cell-surface LDLR level and promotes LDL uptake through downregulation of PCSK9 gene expression in HepG2 cells. Molecular Nutrition & Food Research 58, 2133–2145, https://doi.org/10.1002/mnfr.201400366 (2014). · DOI
- Gu, L. et al. Lunasin functionally enhances LDL uptake via inhibiting PCSK9 and enhancing LDLR expression in vitro and in vivo. Oncotarget 8, 80826–80840, https://doi.org/10.18632/oncotarget.20590 (2017). · DOI
- Chau, P., Fielding, P. E. & Fielding, C. J. Bone Morphogenetic Protein-1 (BMP-1) Cleaves Human Proapolipoprotein A1 and Regulates Its Activation for Lipid Binding. Biochemistry 46, 8445–8450, https://doi.org/10.1021/bi700028u (2007). · DOI
- Zhu, J. et al. Regulation of apoAI processing by procollagen C-proteinase enhancer-2 and bone morphogenetic protein-1. J. Lipid Res. 50, 1330–1339, https://doi.org/10.1194/jlr.M900034-JLR200 (2009). · DOI
- Bourhis, J.-M. et al. Procollagen C-proteinase enhancer grasps the stalk of the C-propeptide trimer to boost collagen precursor maturation. Proc Natl Acad Sci USA 110, 6394–6399, https://doi.org/10.1073/pnas.1300480110 (2013). · DOI
- Bayley, C. P. et al. Diversity between mammalian tolloid proteinases: Oligomerisation and non-catalytic domains influence activity and specificity. Scientific reports 6, 21456, https://doi.org/10.1038/srep21456 (2016). · DOI
- Suzuki, N. et al. Failure of ventral body wall closure in mouse embryos lacking a procollagen C-proteinase encoded by Bmp1, a mammalian gene related to Drosophila tolloid. Development 122, 3587–3595 (1996). · DOI
- Allan, G. A. et al. Pharmacokinetics and metabolism of UK-383,367 in rats and dogs: a rationale for long-lived plasma radioactivity. Xenobiotica 36, 399–418, https://doi.org/10.1080/00498250600618177 (2006). · DOI
- Miller, C. L. et al. Integrative functional genomics identifies regulatory mechanisms at coronary artery disease loci. Nat Commun 7, 12092, https://doi.org/10.1038/ncomms12092 (2016). · DOI
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Pathways and Molecular Mechanisms Governing LDL Receptor Regulation
Schmidt, H. M., Jarrett, K. E., de Aguiar Vallim, T. Q., & Tarling, E. J. (2025) · Circulation Research · doi:10.1161/circresaha.124.323578 · Cited by 33
The low-density lipoprotein receptor: Emerging post-transcriptional regulatory mechanisms
Ndoj, K., Meurs, A., Papaioannou, D., Bjune, K., & Zelcer, N. (2025) · Atherosclerosis · doi:10.1016/j.atherosclerosis.2024.119082 · Cited by 17
Aldworth, H., & Hooper, N. M. (2024) · Biochemical Society Transactions · doi:10.1042/bst20230918 · Cited by 11
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Metadata
- Authors
- Banerjee, S., Andrew, R. J., Duff, C. J., Fisher, K., Jackson, C. D., Lawrence, C. B., Maeda, N., Greenspan, D. S., Kellett, K. A. B., & Hooper, N. M.
- Venue
- Scientific Reports
- Published
- 2019-08-06
- Volume
- 9
- Issue
- 1
- ISSN
- 2045-2322
- PMC
- PMC6684651
- Cited by
- 26
- References
- 2
- Language
- en
- Update notices
- correction (2020-02-11)
- Funders
- RCUK | Medical Research Council (MR/L009625/1)
- University of Manchester (.)
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