MINT MINT, Dpt of Biology, University of Rome Tor Vergata MINT http://mint.bio.uniroma2.it/mint url>http://mint.bio.uniroma2.it/mint/ https://mint.bio.uniroma2.it MINT-[0-9]+ https://mint.bio.uniroma2.it/index.php/results-interactions/?id=${ac} The Molecular INTeraction database (MINT) is a relational database designed to store interactions between biological molecules. http://mint.bio.uniroma2.it http://mint.bio.uniroma2.it/mint niarakis-2013v-1 Detection of a latent soluble form of membrane–type 1 matrix metalloprotease bound with TIMP-2 in periprosthetic tissues and fluids from loose arthroplasty endoprostheses human Homo sapiens Human anti bait coip anti bait coimmunoprecipitation anti bait coip western blot western blot Immuno blot Immuno blot Niarakis A., Giannopoulou E., Ravazoula P., Panagiotopoulos E., Zarkadis I.K., Aletras A.J. aletras@chemistry.upatras.gr FEBS J. (1742-464X) 2013 Only protein-protein interactions imex curation mmp14_human Matrix metalloproteinase-14 Membrane-type matrix metalloproteinase 1 Membrane-type-1 matrix metalloproteinase MMP-X1 MMP14 protein protein human Homo sapiens Human MSPAPRPPRCLLLPLLTLGTALASLGSAQSSSFSPEAWLQQYGYLPPGDLRTHTQRSPQSLSAAIAAMQKFYGLQVTGKADADTMKAMRRPRCGVPDKFGAEIKANVRRKRYAIQGLKWQHNEITFCIQNYTPKVGEYATYEAIRKAFRVWESATPLRFREVPYAYIREGHEKQADIMIFFAEGFHGDSTPFDGEGGFLAHAYFPGPNIGGDTHFDSAEPWTVRNEDLNGNDIFLVAVHELGHALGLEHSSDPSAIMAPFYQWMDTENFVLPDDDRRGIQQLYGGESGFPTKMPPQPRTTSRPSVPDKPKNPTYGPNICDGNFDTVAMLRGEMFVFKERWFWRVRNNQVMDGYPMPIGQFWRGLPASINTAYERKDGKFVFFKGDKHWVFDEASLEPGYPKHIKELGRGLPTDKIDAALFWMPNGKTYFFRGNKYYRFNEELRAVDSEYPKNIKVWEGIPESPRGSFMGSDEVFTYFYKGNKYWKFNNQKLKVEPGYPKSALRDWMGCPSGGRPDEGTEEETEVIIIEVDEEGGGAVSAAAVVLPVLLLLLVLAVGLAVFFFRRHGTPRRLLYCQRSLLDKV timp2_human Metalloproteinase inhibitor 2 TIMP2 Tissue inhibitor of metalloproteinases 2 CSC-21K protein protein human Homo sapiens Human MGAAARTLRLALGLLLLATLLRPADACSCSPVHPQQAFCNADVVIRAKAVSEKEVDSGNDIYGNPIKRIQYEIKQIKMFKGPEKDIEFIYTAPSSAVCGVSLDVGGKKEYLIAGKAEGDGKMHITLCDFIVPWDTLSTTQKKSLNHRYQMGCECKITRCPMIPCYISSPDECLWMDWVTEKNINGHQAKFFACIKRSDGSCAWYRGAAPPKQEFLDIEDP mmp14-timp2-2 1440931 n/a MT1-MPP 1440932 predetermined predetermined participant predetermined unspecified role unspecified role bait bait living cell living cell physiological level physiological level endogenous level endogenous endogenous endogenous level n/a TIMP-2 1440933 western blot western blot Immuno blot Immuno blot unspecified role unspecified role prey prey living cell living cell physiological level physiological level endogenous level endogenous endogenous endogenous level physical association physical association false false false f5a However, upon immunoprecipitation of sMT1-MMP from tissue extracts and fluids with polyclonal antibodies against the hinge region of MT1-MMP and western blot analysis, using monoclonal antibodies against human TIMP-2, an immunoreactive band of ~ 21 kDa, migrating as the human recombinant TIMP-2, was observed in all samples (Fig. 5A). Since polyclonal antibodies against the hinge region of MT1-MMP used for immunoprecipitation, do not recognize TIMP-2 (Fig. 5B), and they did not show non specific reaction with monoclonal antibodies against TIMP-2 (Fig. 5A), these results suggest that TIMP-2 co-precipitated with sMT1-MMP because it was already in complex with it. Consequently, it appears that the sMT1- MMP in tissue extracts and fluids exists in a latent form and yet, bound to TIMP-2. These results were further confirmed by reverse immunoprecipitation with monoclonal antibodies against TIMP-2 and western blotting using polyclonal antibodies against the hinge region of MT1-MMP. Only one immunoreactive band of ~ 57 kDa, corresponding to sMT1- MMP, was observed in all samples (Fig. 5C). The same interaction has been detected in the following tissues: SF-OA, SF-RA, PSSF, POL, LUNG, PCT, IFT. timp2-mmp14 1440931 n/a MT1-MPP 1440932 western blot western blot Immuno blot Immuno blot unspecified role unspecified role prey prey living cell living cell physiological level physiological level endogenous level endogenous endogenous endogenous level n/a TIMP-2 1440933 predetermined predetermined participant predetermined unspecified role unspecified role bait bait living cell living cell physiological level physiological level endogenous level endogenous endogenous endogenous level physical association physical association false false false f5C However, upon immunoprecipitation of sMT1-MMP from tissue extracts and fluids with polyclonal antibodies against the hinge region of MT1-MMP and western blot analysis, using monoclonal antibodies against human TIMP-2, an immunoreactive band of ~ 21 kDa, migrating as the human recombinant TIMP-2, was observed in all samples (Fig. 5A). Since polyclonal antibodies against the hinge region of MT1-MMP used for immunoprecipitation, do not recognize TIMP-2 (Fig. 5B), and they did not show non specific reaction with monoclonal antibodies against TIMP-2 (Fig. 5A), these results suggest that TIMP-2 co-precipitated with sMT1-MMP because it was already in complex with it. Consequently, it appears that the sMT1- MMP in tissue extracts and fluids exists in a latent form and yet, bound to TIMP-2. These results were further confirmed by reverse immunoprecipitation with monoclonal antibodies against TIMP-2 and western blotting using polyclonal antibodies against the hinge region of MT1-MMP. Only one immunoreactive band of ~ 57 kDa, corresponding to sMT1- MMP, was observed in all samples (Fig. 5C). The same interaction has been detected in the following tissues: SF-OA, SF-RA, PSSF, POL, PCT, IFT.