{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Zhu L"],"funding":["Fundamental Research Funds for the Central Universities","Breast Cancer Research Foundation","NIDDK NIH HHS","Margolies Family Discovery Fund for Cancer Research","National Natural Science Foundation of China","NCI NIH HHS","National Institutes of Health","NIAMS NIH HHS","NIH HHS"],"pagination":["e202206121"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9998966"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["222(4)"],"pubmed_abstract":["Bone-resorbing osteoclasts mobilize proteolytic enzymes belonging to the matrix metalloproteinase (MMP) family to directly degrade type I collagen, the dominant extracellular matrix component of skeletal tissues. While searching for additional MMP substrates critical to bone resorption, Mmp9/Mmp14 double-knockout (DKO) osteoclasts-as well as MMP-inhibited human osteoclasts-unexpectedly display major changes in transcriptional programs in tandem with compromised RhoA activation, sealing zone formation and bone resorption. Further study revealed that osteoclast function is dependent on the ability of Mmp9 and Mmp14 to cooperatively proteolyze the β-galactoside-binding lectin, galectin-3, on the cell surface. Mass spectrometry identified the galectin-3 receptor as low-density lipoprotein-rela"],"journal":["The Journal of cell biology"],"pubmed_title":["Proteolytic regulation of a galectin-3/Lrp1 axis controls osteoclast-mediated bone resorption."],"pmcid":["PMC9998966"],"funding_grant_id":["R01-105068","R01-AR075168","2042022kf1207","P30 DK020572","R01 CA071699","R01 AR075168","81970919","R01-CA071699"],"pubmed_authors":["Zhu L","Ma J","Li XY","Sun X","Lyssiotis CA","Wang Z","Weiss SJ","Tang Y","Cho JS","Kerk SA"],"additional_accession":[]},"is_claimable":false,"name":"Proteolytic regulation of a galectin-3/Lrp1 axis controls osteoclast-mediated bone resorption.","description":"Bone-resorbing osteoclasts mobilize proteolytic enzymes belonging to the matrix metalloproteinase (MMP) family to directly degrade type I collagen, the dominant extracellular matrix component of skeletal tissues. While searching for additional MMP substrates critical to bone resorption, Mmp9/Mmp14 double-knockout (DKO) osteoclasts-as well as MMP-inhibited human osteoclasts-unexpectedly display major changes in transcriptional programs in tandem with compromised RhoA activation, sealing zone formation and bone resorption. Further study revealed that osteoclast function is dependent on the ability of Mmp9 and Mmp14 to cooperatively proteolyze the β-galactoside-binding lectin, galectin-3, on the cell surface. Mass spectrometry identified the galectin-3 receptor as low-density lipoprotein-rela","dates":{"release":"2023-01-01T00:00:00Z","publication":"2023 Apr","modification":"2025-04-04T20:04:56.365Z","creation":"2025-04-04T20:04:56.365Z"},"accession":"S-EPMC9998966","cross_references":{"pubmed":["36880731"],"doi":["10.1083/jcb.202206121"]}}