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 Lactoferrin and its hydrolysate bind directly to the oleate-activated form of the lipolysis stimulated lipoprotein receptor. Lactoferrin and its hydrolysate bind directly to the oleate-activated form of the lipolysis stimulated lipoprotein receptor. FEBS J. (1742-464X) 2012 Ahmad N., Girardet JM., Akbar S., Lanhers MC., Paris C., Yen FT., Corbier C. mouse-hepa1-6 Mus musculus hepa1-6 hepa1-6 fluorescence imaging fluorescence microscopy fluorescence imaging predetermined predetermined participant predetermined Ahmad N., Girardet JM., Akbar S., Lanhers MC., Paris C., Yen FT., Corbier C. FEBS J. (1742-464X) 2012 Lactoferrin and its hydrolysate bind directly to the oleate-activated form of the lipolysis stimulated lipoprotein receptor. Lactoferrin and its hydrolysate bind directly to the oleate-activated form of the lipolysis stimulated lipoprotein receptor. FEBS J. (1742-464X) 2012 Ahmad N., Girardet JM., Akbar S., Lanhers MC., Paris C., Yen FT., Corbier C. in vitro In vitro filter binding filter binding Filter overlay assay Filter overlay assay predetermined predetermined participant predetermined Ahmad N., Girardet JM., Akbar S., Lanhers MC., Paris C., Yen FT., Corbier C. FEBS J. (1742-464X) 2012 lsr_rat Lipolysis-stimulated lipoprotein receptor Lsr Lisch7 Lipolysis-stimulated remnant receptor protein protein rat Rattus norvegicus (Rat) Rat MAPAAGACAGAPDSHPATVVFVCLFLIIFCPDPASAIQVTVSDPYHVVILFQPVTLPCTYQMSNTLTVPIVIWKYKSFCRDRIADAFSPASVDNQLNAQLAAGNPGYNPYVECQDSVRTVRVVATKQGNAVTLGDYYQGRRITITGNADLTFEQTAWGDSGVYYCSVVSAQDLDGNNEAYAELIVLGRTSEAPELLPGFRAGPLEDWLFVVVVCLASLLLFLLLGICWCQCCPHTCCCYVRCPCCPDKCCCPEALYAAGKAATSGVPSIYAPSIYTHLSPAKTPPPPPAMIPMGPPYGYPGDFDRHSSVGGHSSQVPLLRDVDGSVSSEVRSGYRIQANQQDDSMRVLYYMEKELANFDPSRPGPPNGRVERAMSEVTSLHEDDWRSRPSRAPALTPIRDEEWNRHSPQSPRTWEQEPLQEQPRGGWGSGRPRARSVDALDDINRPGSTESGRSSPPSSGRRGRAYAPPRSRSRDDLYDPDDPRDLPHSRDPHYYDDIRSRDPRADPRSRQRSRDPRDAGFRSRDPQYDGRLLEEALKKKGSGERRRVYREEEEEEEGQYPPAPPPYSETDSQASRERRLKKNLALSRESLVV mint homomint Probable role in the clearance of triglyceride-rich lipoprotein from plasma. Binds chylomicrons, LDL and VLDL in presence of free fatty acids and allows their subsequent uptake in the cells 7C0288823492C87F trfl_bovin Lactotransferrin LTF protein protein bovin Bos taurus (Bovine) Bovine MKLFVPALLSLGALGLCLAAPRKNVRWCTISQPEWFKCRRWQWRMKKLGAPSITCVRRAFALECIRAIAEKKADAVTLDGGMVFEAGRDPYKLRPVAAEIYGTKESPQTHYYAVAVVKKGSNFQLDQLQGRKSCHTGLGRSAGWIIPMGILRPYLSWTESLEPLQGAVAKFFSASCVPCIDRQAYPNLCQLCKGEGENQCACSSREPYFGYSGAFKCLQDGAGDVAFVKETTVFENLPEKADRDQYELLCLNNSRAPVDAFKECHLAQVPSHAVVARSVDGKEDLIWKLLSKAQEKFGKNKSRSFQLFGSPPGQRDLLFKDSALGFLRIPSKVDSALYLGSRYLTTLKNLRETAEEVKARYTRVVWCAVGPEEQKKCQQWSQQSGQNVTCATASTTDDCIVLVLKGEADALNLDGGYIYTAGKCGLVPVLAENRKSSKHSSLDCVLRPTEGYLAVAVVKKANEGLTWNSLKDKKSCHTAVDRTAGWNIPMGLIVNQTGSCAFDEFFSQSCAPGADPKSRLCALCAGDDQGLDKCVPNSKEKYYGYTGAFRCLAEDVGDVAFVKNDTVWENTNGESTADWAKNLNREDFRLLCLDGTRKPVTEAQSCHLAVAPNHAVVSRSDRAAHVKQVLLHQQALFGKNGKNCPDKFCLFKSETKNLLFNDNTECLAKLGGRPTYEEYLGTEYVTAIANLKKCSTSPLLEACAFLTR mint Transferrins are iron binding transport proteins which can bind two Fe(3+) ions in association with the binding of an anion, usually bicarbonate The lactotransferrin peptidase S60 domain 1 functions as a serine protease that cuts arginine rich regions. This function contributes to the antimicrobial activity homomint Lactotransferrin has antimicrobial activity. The most effective inhibitory activity was seen against E.coli and P.aeruginosa Lactoferricin B is an antimicrobial peptide. Inhibits the growth of Gram-negative and Gram-positive bacteria C6FD7FC15D68E93F lsr_mouse Lipolysis-stimulated lipoprotein receptor Lsr Lisch7 Liver-specific bHLH-Zip transcription factor Lipolysis-stimulated receptor Liver-specific gene on mouse chromosome 7 protein protein protein mouse Mus musculus Mouse MAPAASACAGAPGSHPATTIFVCLFLIIYCPDRASAIQVTVPDPYHVVILFQPVTLHCTYQMSNTLTAPIVIWKYKSFCRDRVADAFSPASVDNQLNAQLAAGNPGYNPYVECQDSVRTVRVVATKQGNAVTLGDYYQGRRITITGNADLTFEQTAWGDSGVYYCSVVSAQDLDGNNEAYAELIVLGRTSEAPELLPGFRAGPLEDWLFVVVVCLASLLFFLLLGICWCQCCPHTCCCYVRCPCCPDKCCCPEALYAAGKAATSGVPSIYAPSIYTHLSPAKTPPPPPAMIPMRPPYGYPGDFDRTSSVGGHSSQVPLLREVDGSVSSEVRSGYRIQANQQDDSMRVLYYMEKELANFDPSRPGPPNGRVERAMSEVTSLHEDDWRSRPSRAPALTPIRDEEWNRHSPRSPRTWEQEPLQEQPRGGWGSGRPRARSVDALDDINRPGSTESGRSSPPSSGRRGRAYAPPRSRSRDDLYDPDDPRDLPHSRDPHYYDDLRSRDPRADPRSRQRSHDPRDAGFRSRDPQYDGRLLEEALKKKGAGERRRVYREEEEEEEEGHYPPAPPPYSETDSQASRERRMKKNLALSRESLVV mint homomint Probable role in the clearance of triglyceride-rich lipoprotein from blood. Binds chylomicrons, LDL and VLDL in presence of free fatty acids and allows their subsequent uptake in the cells 2ADE28BB870A001D lsr-ltf 2 Lf 4 western blot western blot Immuno blot Immuno blot predetermined predetermined participant predetermined unspecified role unspecified role prey prey purified purified Lsr 3 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role bait bait purified purified direct interaction direct interaction f5a homomint mint As shown in Figure 5A (lanes 3-6), both lobes of Lf are able to bind to LSR, but again, only if oleate is present. This also suggests that there are structural motifs or sequences located not only the N-lobe, but also the C-lobe of Lf that are recognized by LSR. lsr-ltf-1 1 Lf 4 tag fluorescence tag visualisation by fluorescence tag fluorescence predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component physiological level physiological level endogenous level endogenous endogenous endogenous level fixed cell fixed cell tag tag tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined Lsr 5 immunostaining immunostaining predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component physiological level physiological level endogenous level endogenous endogenous endogenous level fixed cell fixed cell colocalization colocalization f3 homomint mint Intact cells were used, in which Alexafluor 488-labelled Lf was incubated with Hepa1-6 cells with or without oleate. Figure 3 shows strong labeling of permeabilized cells with both Lf and LSR, with little apparent co-localization in the merge picture in the absence of oleate (Fig. 3, top panels). However, when cells were incubated in the presence of oleate, co-localization of Lf and LSR labeling increased dramatically, as evidenced by the increased orange intensity in the merged picture (Fig. 3, lower right panel). This suggests that Lf interacts directly with LSR, but only in the presence of oleate, thus when LSR is in its active conformation.