{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Albrechtsen R"],"funding":["The Danish Cancer Society","Danish Cancer Society","Novo Nordisk Fonden"],"pagination":["E1957"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC6514901"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["20(8)"],"pubmed_abstract":["The transmembrane glycoprotein basigin, a member of the immunoglobulin superfamily, stimulates matrix metalloproteinase (MMP)-mediated extracellular matrix (ECM) degradation and thereby drives cancer cell invasion. Basigin is proteolytically shed from the cell surface and high concentrations of soluble basigin in the blood dictates poor prognosis in cancer patients. A positive correlation between basigin and a disintegrin and metalloproteinase (ADAM)-12 in serum from prostate cancer patients has been reported. Yet, the functional relevance of this correlation is unknown. Here, we show that ADAM12 interacts with basigin and cleaves it in the juxtamembrane region. Specifically, overexpression of ADAM12 increases ectodomain shedding of an alkaline phosphatase-tagged basigin reporter protein f"],"journal":["International journal of molecular sciences"],"pubmed_title":["Identification of ADAM12 as a Novel Basigin Sheddase."],"pmcid":["PMC6514901"],"funding_grant_id":["R72-A4591","R146-A9211-16-S2","NNF17OC0024464","R204-A12270","R146-A9211","R124-A7508"],"pubmed_authors":["Albrechtsen R","Wewer Albrechtsen NJ","Gnosa S","Dyrskjot L","Schwarz J","Kveiborg M"],"additional_accession":[]},"is_claimable":false,"name":"Identification of ADAM12 as a Novel Basigin Sheddase.","description":"The transmembrane glycoprotein basigin, a member of the immunoglobulin superfamily, stimulates matrix metalloproteinase (MMP)-mediated extracellular matrix (ECM) degradation and thereby drives cancer cell invasion. Basigin is proteolytically shed from the cell surface and high concentrations of soluble basigin in the blood dictates poor prognosis in cancer patients. A positive correlation between basigin and a disintegrin and metalloproteinase (ADAM)-12 in serum from prostate cancer patients has been reported. Yet, the functional relevance of this correlation is unknown. Here, we show that ADAM12 interacts with basigin and cleaves it in the juxtamembrane region. Specifically, overexpression of ADAM12 increases ectodomain shedding of an alkaline phosphatase-tagged basigin reporter protein f","dates":{"release":"2019-01-01T00:00:00Z","publication":"2019 Apr","modification":"2025-04-21T13:59:22.721Z","creation":"2019-07-01T13:51:20Z"},"accession":"S-EPMC6514901","cross_references":{"pubmed":["31013576"],"doi":["10.3390/ijms20081957"]}}