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 Ischemia/reperfusion-induced myosin light chain 1 phosphorylation increases its degradation by matrix metalloproteinase 2. Ischemia/reperfusion-induced myosin light chain 1 phosphorylation increases its degradation by matrix metalloproteinase 2. FEBS J. (1742-464X) 2012 Cadete VJ., Sawicka J., Jaswal JS., Lopaschuk GD., Schulz R., Szczesna-Cordary D., Sawicki G. in vitro In vitro comig non denat gel comigration in non denaturing gel electrophoresis comig non denat gel immunostaining immunostaining Cadete VJ., Sawicka J., Jaswal JS., Lopaschuk GD., Schulz R., Szczesna-Cordary D., Sawicki G. FEBS J. (1742-464X) 2012 mylk2_rat Myosin light chain kinase 2, skeletal/cardiac muscle Mylk2 protein protein rat Rattus norvegicus (Rat) Rat MATENGAVELGTQSLSTDHPPTDAAGDGSPASEKEPSLPDTEKDLGPTNTKKDPGAPDPKKNPDPPSLKKTPEAPGPEKKGDSAPASASNQGPSGEGDGGGGPAEGGTGPPAVLPQPTATADASIQKLDATQAPSGNQESGEAKAGKKAAECREAGRRGSPAFLHSPSCPAIISCSEKTLAMKPLSETTELIFAGVSETPDPQDPGPAKDEGGTNTLADGKEEAEAGQAEQAKVQGDTSQRIGFQAVPSERAEVGQALCLTAKEEDCFQILDDCPPPPAPFPHRIVELRTGNVSSEFSMNSKEALGGGKFGAVCTCTERSTGLKLAAKVIKKQTPKDKEMVLLEIEVMNQLNHRNLIQLYSAIETSHEIILFMEYIEGGELFERIVDEDYQLTEVDTMVFVRQICDGILFMHKMRVLHLDLKPENILCVNTTGHLVKIIDFGLARRYNPNEKLKVNFGTPEFLSPEVVNYDQISDKTDMWSLGVITYMLLSGLSPFLGDDDTETLNNVLSANWYFDEETFEAVSDEAKDFVSNLITKDQSARMSAEQCLAHPWLNNLAEKAKRCNRRLKSQILLKKYLMKRRWKKNFIAVSAANRFKKISSSGALMALGV mint Implicated in the level of global muscle contraction and cardiac function (By similarity). Phosphorylates a specific serine in the N-terminus of a myosin light chain E26BF76EFF88701F p02600-1 Myosin light chain 1/3, skeletal muscle isoform Myl1 Myosin light chain alkali 1/2 protein protein rat Rattus norvegicus (Rat) Rat MAPKKDVKKPAAAAPAPAPAPAPAPAKPKEEKIDLSAIKIEFSKEQQEEFKEAFLLFDRTGECKITLSQVGDVLRALGTNPTNAEVKKVLGNPSNEEMNAKKIEFEQFLPMMQAISNNKDQGGYEDFVEGLRVFDKEGNGTVMGAELRHVLATLGEKMKEEEVEALLAGQEDSNGCINYEAFVKHIMSV mint C8FC83CA793220B4 myl1-mylk2 1 MLC1 3 immunostaining immunostaining predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component cell lysate cell lysate physiological level physiological level endogenous level endogenous endogenous endogenous level MLCK 2 immunostaining immunostaining predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component cell lysate cell lysate physiological level physiological level endogenous level endogenous endogenous endogenous level association association f7 mint Potential co-localization of MLC1 with MLCK was evaluated by separating protein complexes from heart homogenates under non reducing and non-denaturing conditions (using native gels), followed by dual-immunoblotting (Fig. 7). Under nonreducing conditions, two distinct bands of MLC1 (red) were seen in aerobic control, I/R and I/R+ML-7 heart homogenates (Fig. 7a, middle panel). Blotting for MLCK revealed only one band (green) (Fig.7a, top panel). Overlap of both blots revealed co-localization of MLCK with MLC1 (yellow) (Fig. 7a, bottom panel). Quantitative analysis of the blots showed a slightly increased co-localization of MLC1 with MLCK in I/R hearts compared to aerobic controls, but the difference was not statistically significant (p=0.0661, Fig. 7b). Administration of ML-7 significantly reduced the co-localization of MLC1 with MLCK in comparison to non-treated hearts subjected to I/R (Fig. 7b).