{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Joe MK"],"funding":["NEI NIH HHS"],"pagination":["5308-5318"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC5644706"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["58(12)"],"pubmed_abstract":["<h4>Purpose</h4>To elucidate functions of wild-type myocilin, a secreted glycoprotein associated with glaucoma.<h4>Methods</h4>Lysates of mouse eyes were used for immunoprecipitation with affinity-purified antibodies against mouse myocilin. Shotgun proteomic analysis was used for the identification of proteins interacting with myocilin. Colocalization of myocilin and tissue inhibitor of metalloproteinases 3 (TIMP3) in different eye structures was investigated by a multiplex fluorescent in situ hybridization and immunofluorescent labeling with subsequent confocal microscopy. Matrix metalloproteinase 2 (MMP2) activity assay was used to test effects of myocilin on TIMP3 inhibitory action.<h4>Results</h4>TIMP3 was identified by a shotgun proteomic analysis as a protein that was coimmunoprecipi"],"journal":["Investigative ophthalmology & visual science"],"pubmed_title":["Myocilin Regulates Metalloprotease 2 Activity Through Interaction With TIMP3."],"pmcid":["PMC5644706"],"funding_grant_id":["R01 EY021205"],"pubmed_authors":["Nakaya N","Lieberman RL","Tomarev SI","Joe MK"],"additional_accession":[]},"is_claimable":false,"name":"Myocilin Regulates Metalloprotease 2 Activity Through Interaction With TIMP3.","description":"<h4>Purpose</h4>To elucidate functions of wild-type myocilin, a secreted glycoprotein associated with glaucoma.<h4>Methods</h4>Lysates of mouse eyes were used for immunoprecipitation with affinity-purified antibodies against mouse myocilin. Shotgun proteomic analysis was used for the identification of proteins interacting with myocilin. Colocalization of myocilin and tissue inhibitor of metalloproteinases 3 (TIMP3) in different eye structures was investigated by a multiplex fluorescent in situ hybridization and immunofluorescent labeling with subsequent confocal microscopy. Matrix metalloproteinase 2 (MMP2) activity assay was used to test effects of myocilin on TIMP3 inhibitory action.<h4>Results</h4>TIMP3 was identified by a shotgun proteomic analysis as a protein that was coimmunoprecipi","dates":{"release":"2017-01-01T00:00:00Z","publication":"2017 Oct","modification":"2025-04-22T09:10:36.075Z","creation":"2019-03-27T02:59:09Z"},"accession":"S-EPMC5644706","cross_references":{"pubmed":["29049729"],"doi":["10.1167/iovs.16-20336"]}}