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Statements

OLR1 binds LRP6. 9 / 9
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"Indicating LRP6 preferentially bound to ox-LDL rather DKK1."
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"In a previous study [ 32 ], we identified ox-LDL, a hallmark for hyperlipidaemia and atherosclerosis, as one of the key molecular mediating high-fat diet-induced impaired bone formation and identified[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"Taken together, these results validate that LRP6 on cell surface preferentially binds to ox-LDL rather than DKK1, mediating the uptake of ox-LDL."
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"Moreover, ox-LDL decreased RUNX2 expression much more than DKK1, and ox-LDL and DKK1 co-treatment decreased the expression of RUNX2 much more than their individual treatment, demonstrating that ox-LDL[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"The direct binding of oxPLs to LRP6 was also detected by a protein lipid overlay (PLO) assay, xref , xref in which the in vitro binding of the same amount of nLDL and oxLDL to full length LRP6 or the extracellular domain of LRP6 (LRP6N) was detected."
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"These results indicate that ox-LDL binds to LRP6, inhibiting Wnt signaling, and the uptake of ox-LDL induces oxidative stress-related BMSC senescence, which together impair bone formation."
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"We substantiated that the bone loss induced by HFD is resulting from obesity-induced BMSCs senescence, primarily mediated by the uptake of ox-LDL bound to LRP6."
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"MESD inhibits the uptake of the LRP6-ox-LDL complex by antagonizing the binding of LRP6 to ox-LDL, consequently alleviating cellular senescence."
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"After various effects caused by LRP6 binding to ox-LDL in BMSCs were explored, we found that LRP6 uptake of ox-LDL led to an increase of intracellular ROS in BMSCs, resulting in cellular senescence an[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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