Binding and uptake of ligands by scavenger receptors (Homo sapiens)

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21, 46, 56, 101, 1317, 22, 34, 57, 89...20, 74, 88, 94, 107...16, 27, 47, 65, 68...11, 13-15, 28...4813, 28, 29, 38, 71...5, 64, 104, 12736, 103, 111, 112, 114...19, 37, 86, 136, 150...31, 55, 9748, 1223, 37, 42, 44, 50...67, 10220, 74, 107, 12169, 1486, 8, 30, 31, 70...12, 32, 49, 77, 80...37, 39, 66, 82, 158...115, 12883, 98, 14425, 26, 43, 69, 87...61, 128, 135, 14137, 66, 159106, 12448, 58, 12214110, 63, 1291, 35, 52, 78, 1262, 4, 17, 18, 23...10, 109, 134cytosolendocytic vesicleSCARA5:LigandIg lambda chain V-VI region SUT ferriheme b 1,3-beta-D-glucan TAGs 3x4Hyp-3Hyp-COL3A1 SCARA5:LigandIg kappa chain V-II region GM607 IGHV7-81(1-?) IgA:Alpha-1-MicroglobulinCHEST TAGs Ig lambda chain V-IV region MOL 7-ketocholesterol HPX Ig kappa chain V-I region CAR 10xdHF-10xglutamyl semialdehyde (Pro)-6xL-tyrosine residue-3xOxoH-2xmodified L-lysine residue-N'-formyl-L-kynurenine-APOB(28-4563) Peptide N-epsilon-(1-(1-carboxy)ethyl)lysine AcK-APOB(28-4563) Ig kappa chain V-I region Wes Ig kappa chain V-I region Rei COLEC12 IGKC LRP1 Ig kappa chain V-I region Kue 3x4Hyp-3Hyp-GlcGalHyl-COL1A2 Ligands of SCARB1SCARA5 trimerHBB Ig heavy chain V-I region EU 3x4Hyp-3Hyp-GalHyl-COL1A1 3x4Hyp-3Hyp-5Hyl-COL1A2 Ig kappa chain V region EV15 NECML hematite nanoparticle Ig kappa chain V-I region WAT IGLV2-23(1-?) Ig heavy chain V-III region WEA PL 5xHC-HP(162-406) LCFAs COLEC11 CHOL Ig kappa chain V-I region Ka Ig kappa chain V-IV region Len 3x4Hyp-GlcGalHyl-COL1A2 GlcGalHyl-COL1A1 Phosphatidylserine Ig kappa chain V-I region WAT hydroxy fatty acid ferroheme b hydroperoxy fatty acid Ig kappa chain V-I region Walker Ig lambda chain V-I region MEM SPARC Ig kappa chain V-III region WOL Ig kappa chain V-III region B6 Ig lambda chain V-III region LOI NECML 4xPalmC-CD36PL PI CHEST 3x4Hyp-5Hyl-COL3A1 HSPH1 Ligands of STAB2AcK-APOB(28-4563) Ig heavy chain V-I region SIE CHEST Ig heavy chain V-III region BUT MASP1(20-699) Ig kappa chain V-I region EU Ig kappa chain V-I region Kue hydroxy fatty acid CHOL IGHV7-81(1-?) PL SCARB1-2 3x4Hyp-3Hyp-COL1A1 TAGs Ig kappa chain V-I region OU Hemoglobin:Haptoglobinhydroperoxy fatty acid Ig kappa chain V-I region Bi ferroheme b Phosphatidylserine TAGs SAA1(19-122) Ig heavy chain V-II region HE Alpha1-Microglobulin:heme trimerLPS PL AcK-APOB(28-4563) Ig kappa chain V-III region Ti Ig heavy chain V-III region CAM Ig kappa chain V-III region POM 10xdHF-10xglutamyl semialdehyde (Pro)-6xL-tyrosine residue-3xOxoH-2xmodified L-lysine residue-N'-formyl-L-kynurenine-APOB(28-4563) Ig kappa chain V-II region MIL Lipoteichoic acid LPS Ig lambda chain V-II region NIG-58 Ig lambda chain V-II region BUR CHEST CHS O2 GlcGalHyl-COL1A2 CHEST Ig lambda chain V-I region EPS COLEC11:LigandGlcNAc oxidized phospholipids dextran sulfate SCARF1:LigandCHEST Phosphatidylserine Ig lambda chain V-VI region AR Lipoteichoic acid 7xHC-HP(19-160) Ig kappa chain V region EV15 Ig heavy chain V-III region WAS Ig heavy chain V-III region GAL GalHyl-COL1A2 TAGs Ig lambda chain V-VI region WLT APOB(28-4563) IGLV4-60(1-?) HBA1 6xHC-MARCO ALB 3x4Hyp-3Hyp-GlcGalHyl-COL3A1 3x4Hyp-COL3A1 LCFAs 3x4Hyp-3Hyp-COL1A2 HBB HBB 5Hyl-COL1A2 10xdHF-10xglutamyl semialdehyde (Pro)-6xL-tyrosine residue-3xOxoH-2xmodified L-lysine residue-N'-formyl-L-kynurenine-APOB(28-4563) Ig heavy chain V-III region POM O2 4xPalmC-CD36 Ig kappa chain V-III region SIE HPX:heme bCALR ferroheme b 3x4Hyp-COL1A1 Peptide SCARF1:LigandIg lambda chain V-II region MGC SCGB3A2 Ig kappa chain V-I region Ka Ig heavy chain V-III region JON Ig kappa chain V-I region Wes 3x4Hyp-COL1A2 3x4Hyp-GalHyl-COL1A1 HBA1 APOB(28-4563) IGLV11-55(1-?) Ig heavy chain V-III region KOL ferroheme b SCGB3A2 cholesterol esters Ig heavy chain V-II region MCE Ligands of STAB1HPXIGLC1 IGLC1 Fe3+ hydroperoxy fatty acid Ig kappa chain V-II region GM607 Ig kappa chain V-I region Hau lysophosphatidylcholine CHOL Phosphatidylserine 3x4Hyp-3Hyp-5Hyl-COL3A1 LPS Ig kappa chain V-II region TEW CHOL 7-ketocholesterol MARCO trimerIg lambda chain V-I region EPS Ig lambda chain V-II region VIL 10xdHF-10xglutamyl semialdehyde (Pro)-6xL-tyrosine residue-3xOxoH-2xmodified L-lysine residue-N'-formyl-L-kynurenine-APOB(28-4563) Ig kappa chain V-III region VG 7xHC-HP(19-160) CHOL IGLV5-45(1-?) ferriheme b FTH1 Ig heavy chain V-II region OU CHS Ig kappa chain V-I region HK101 SCARA5 Ig kappa chain V-III region WOL TAGs PL APOA1(25-266) Ig lambda chain V-II region NIG-58 Ig lambda chain V-I region BL2 3x4Hyp-3Hyp-GalHyl-COL1A2 hydroxy fatty acid TAGs Peptide SCARF15Hyl-COL1A1 HUA 3x4Hyp-COL1A2 CALR SAA1(19-122) carrageenan lysophosphatidylcholine IGLV5-37(1-?) COLEC12 trimer5xHC-HP(162-406) AcK-APOB(28-4563) lysophosphatidylcholine HUA Unmethylated CpG DNA 3x4Hyp-5Hyl-COL1A1 IGHA2 3x4Hyp-GalHyl-COL1A1 CALR Ig heavy chain V-III region LAY DNA GlcNAc CALR Ig lambda chain V-V region DEL CHOL ferroheme b cholesterol PL ferroheme b Ig lambda chain V-I region NEW 7-ketocholesterol IGLV2-23(1-?) hematite nanoparticle APOA1(25-266) TAGs AcK-APOB(28-4563) Ig heavy chain V-I region WOL IGLV2-11(1-?) HPX PL 7-ketocholesterol Ig lambda chain V-IV region Hil 7-ketocholesterol poly(G) Ig kappa chain V-IV region B17 Ig heavy chain V-II region WAH Ig kappa chain V-III region Ti lysophosphatidylcholine Ig lambda chain V-VI region WLT 7-ketocholesterol Albumin:ferrihemeMan COLEC12 1,3-beta-D-glucan Ig kappa chain V-III region GOL IGKVA18(21-?) Ig lambda chain V-II region NEI Phosphatidylserine Ig heavy chain V-II region HE TAGs Ig heavy chain V-II region NEWM Ig lambda chain V-I region NIG-64 Ig heavy chain V-II region COR 6xHC-MARCO HBB COLEC11:MASP1Ig kappa chain V-IV region JI PL MethemoglobinDouble-stranded RNA CHEST IGLV2-18(1-?) Phosphatidylserine Ig kappa chain V-III region CLL HSP90AA1 1,3-beta-D-glucan Ig kappa chain V-III region IARC/BL41 Ligands of SCARA5GalHyl-COL1A1 AcK-APOB(28-4563) Ig heavy chain V-III region HIL IGKV4-1(21-?) COLEC11 HSP90AA1 poly(I) Ig heavy chain V-III region ZAP lysophosphatidylcholine CHEST TAGs hydroxy fatty acid SCARF1 Ig lambda chain V-II region VIL Ig kappa chain V-II region FR DNA Ig lambda chain V-I region VOR Lipoteichoic acid IGLV2-18(1-?) 1,3-beta-D-glucan CHOL IGKV1-5(23-?) SCARB1:EndocytosedLigand1,3-beta-D-glucan cholesterol 10xdHF-10xglutamyl semialdehyde (Pro)-6xL-tyrosine residue-3xOxoH-2xmodified L-lysine residue-N'-formyl-L-kynurenine-APOB(28-4563) Ig lambda chain V-I region NEWM O2 Ig kappa chain V-II region Cum Ig kappa chain V-I region OU IGLC3 hematite nanoparticle 7-ketocholesterol STAB2(1136-2551)6xHC-MSR1 IGLV11-55(1-?) AcK-APOB(28-4563) Peptide LPS PL Lipoteichoic acid Peptide IGLV4-3(1-?) COL4A2(184-1712) APOE SAA1(19-122) HPR:APOL1:APOA1:HDL3heme bhydroperoxy fatty acid IGLC2 HBB PI 7-ketocholesterol poly(G) ferriheme b Heparins TAGs hydroperoxy fatty acid Lipoteichoic acid TAGs CHOL N-epsilon-(1-(1-carboxy)ethyl)lysine Ig kappa chain V-I region Daudi N-epsilon-(1-(1-carboxy)ethyl)lysine 3x4Hyp-3Hyp-GalHyl-COL3A1 APOL1 porB CHOL PL Ig lambda chain V-I region MEM 3x4Hyp-5Hyl-COL1A1 hydroperoxy fatty acid 10xdHF-10xglutamyl semialdehyde (Pro)-6xL-tyrosine residue-3xOxoH-2xmodified L-lysine residue-N'-formyl-L-kynurenine-APOB(28-4563) Ig lambda chain V-II region MGC Ig kappa chain V-III region NG9 3x4Hyp-GlcGalHyl-COL3A1 ferriheme b 3x4Hyp-GalHyl-COL3A1 APOB(28-4563) IGLC3 lysophosphatidylcholine cholesterol PL HPX Ig kappa chain V-I region Lay Ig kappa chain V-I region Roy HYOU1 10xdHF-10xglutamyl semialdehyde (Pro)-6xL-tyrosine residue-3xOxoH-2xmodified L-lysine residue-N'-formyl-L-kynurenine-APOB(28-4563) PI cholesterol IGLV3-12(1-?) IGLV4-69(1-?) Ig lambda chain V-I region NIG-64 Ig heavy chain V-III region TUR IGHV(1-?) Double-stranded RNA ApohemoglobinHBA1 CHEST HBA1 PL hydroperoxy fatty acid GlcGalHyl-COL3A1(154-1241) Ig kappa chain V-I region Bi LPS IGLV3-12(1-?) hydroperoxy fatty acid IGLV2-11(1-?) HPR N-epsilon-(1-(1-carboxy)ethyl)lysine CALR STAB1 Ig kappa chain V-II region Cum IGKC APOL1 Ig kappa chain V-II region MIL hydroperoxy fatty acid Ig lambda chain V-VII region MOT Ig kappa chain V-I region BAN Ig heavy chain V-I region WOL CHOL Double-stranded RNA STAB2(1136-2551) Ig kappa chain V-I region DEE Ig heavy chain V-III region GA PL poly(I) Ig lambda chain V-I region VOR MSR1:LigandIg kappa chain V-I region Roy Ig kappa chain V-I region WEA 1,3-beta-D-glucan LPS ferroheme b HBA1 APOB(28-4563) IGLV7-46(1-?) Ig lambda chain V-V region DEL Ig heavy chain V-II region COR Ig lambda chain V-VI region NIG-48 Ligands of COLEC116xHC-MSR1 TAGs ferriheme b lysophosphatidylcholine LRP1:Hemopexin:hemeAMBP(20-198) CHOL Ligands of COLEC12Ig lambda chain V-VI region AR Ig lambda chain V-II region TRO Ig heavy chain V-III region TEI HYOU1 Ig heavy chain V-III region WEA Ig kappa chain V-II region TEW Ig heavy chain V-III region POM PL PL Ig heavy chain V-III region BUR STAB1Ig heavy chain V-III region GA IgAhydroxy fatty acid IGLV5-37(1-?) Ligands of CD36Ig kappa chain V-I region Scw Ig lambda chain V-III region SH Ig lambda chain V-IV region Hil PL Ig heavy chain V-III region TUR cholesterol esters IGLV3-25(1-?) Ig kappa chain V-I region Daudi Ligands of MSR1lysophosphatidylcholine CHEST Ig kappa chain V-I region Rei 6xHC-MSR1 HBB Ig lambda chain V region 4A APOA1(25-266) IGKV4-1(21-?) Ig lambda chain V-I region NEW AcK-APOB(28-4563) APOA1(25-266) cholesterol esters STAB2:LigandIg heavy chain V-I region Mot LRP1 IGLV3-27(1-?) NECML IGLV3-25(1-?) 3x4Hyp-GlcGalHyl-COL1A2 Ig kappa chain V-I region AG TAGs CHOL Ig kappa chain V-IV region Len Double-stranded RNA Ig lambda chain V-I region NEWM IGLV(23-?) Ig kappa chain V-I region Gal IGLV1-44(1-?) CHEST 3x4Hyp-GlcGalHyl-COL1A1 Ig heavy chain V-III region HIL STAB2:LigandIg heavy chain V-II region DAW 3x4Hyp-COL3A1 IGLV3-22(1-?) 3x4Hyp-3Hyp-COL1A2 lysophosphatidylcholine SAA1(19-122) poly(I) 7-ketocholesterol CHEST 7-ketocholesterol TAGs IgH heavy chain V-III region VH26 precursor 3x4Hyp-3Hyp-GalHyl-COL1A1 Double-stranded RNA Ig lambda chain V-II region BOH Ig lambda chain V-IV region X Ig heavy chain V-II region MCE 1,3-beta-D-glucan PL IGLV10-54(1-?) SPARC Ig lambda chain V-I region WAH GlcGalHyl-COL1A2 LPS Ig heavy chain V-III region JON Ig heavy chain V-II region DAW SCARB1-2 CHS 3x4Hyp-5Hyl-COL3A1 Phosphatidylserine lysophosphatidylcholine IGLV3-16(1-?) CHOL Ig heavy chain V-III region TRO LCFAs hydroxy fatty acid Ig lambda chain V-II region NIG-84 Ig lambda chain V-I region HA CD163cholesterol IGLV1-36(1-?) 5,6beta-epoxy-cholesterol COLEC12:LigandIGLV8-61(1-?) COL1A1 IGLC7 TAGs Ig heavy chain V-III region TIL IGLV2-33(1-?) APOE 10xdHF-10xglutamyl semialdehyde (Pro)-6xL-tyrosine residue-3xOxoH-2xmodified L-lysine residue-N'-formyl-L-kynurenine-APOB(28-4563) 10xdHF-10xglutamyl semialdehyde (Pro)-6xL-tyrosine residue-3xOxoH-2xmodified L-lysine residue-N'-formyl-L-kynurenine-APOB(28-4563) Ig kappa chain V-I region Ni 10xdHF-10xglutamyl semialdehyde (Pro)-6xL-tyrosine residue-3xOxoH-2xmodified L-lysine residue-N'-formyl-L-kynurenine-APOB(28-4563) N-epsilon-(1-(1-carboxy)ethyl)lysine PL IGLV(23-?) hydroperoxy fatty acid HSP90B1 Ig kappa chain V-I region CAR Ig lambda chain V-IV region Bau Lipoteichoic acid Double-stranded RNA GlcGalHyl-COL1A1 STAB1 Ig lambda chain V-II region BO 3x4Hyp-GlcGalHyl-COL1A1 Ig heavy chain V-III region NIE hydroxy fatty acid Hemoglobin:HPR:APOL1:APOA1:HDL37-ketocholesterol MSR1:CollagenI,III,IVO2 MSR1 (SCARA1) trimerSTAB1:Liganddextran sulfate silicon dioxide nanoparticle Ig heavy chain V-III region BRO hydroperoxy fatty acid IGHA1 titanium dioxide nanoparticle LRP1TruncatedAlpha1-Microglobulin:heme trimerCOL4A1(173-1669) HBB HSP90AA1 3x4Hyp-3Hyp-GlcGalHyl-COL1A2 Lipoteichoic acid 5Hyl-COL3A1 AcK-APOB(28-4563) GalHyl-COL3A1 GalHyl-COL1A1 hydroxy fatty acid APOA1(25-266) Ig lambda chain V-VII region MOT CHEST TAGs titanium dioxide nanoparticle 1,3-beta-D-glucan Ig kappa chain V-III region HIC TAGs dextran sulfate IGLV7-43(1-?) COLEC12 lysophosphatidylcholine Ig heavy chain V-I region SIE GalNAc Ig lambda chain V-IV region X silicon dioxide nanoparticle 7-ketocholesterol Ig lambda chain V-III region SH CHOL IGLV1-36(1-?) Ig kappa chain V-III region NG9 5,6beta-epoxy-cholesterol 5xHC-HP(162-406) TAGs IGLC6 Ig lambda chain V-III region LOI Ig kappa chain V-III region POM Ig lambda chain V-II region TOG 3x4Hyp-3Hyp-GalHyl-COL1A2 Ig heavy chain V-III region LAY Ig heavy chain V-II region ARH-77 Ig lambda chain V-IV region Kern STAB2(1136-2551) LPS Ig kappa chain V-I region AG IGLC6 APOA1(25-266) hydroxy fatty acid PL IGLV2-33(1-?) COL4A2(184-1712) Ig heavy chain V-III region ZAP 3x4Hyp-3Hyp-COL3A1 GalNAc IgH heavy chain V-III region VH26 precursor ferroheme b 3x4Hyp-GalHyl-COL3A1 Ig lambda chain V-IV region Bau Ig kappa chain V-I region DEE SCARB1:EndocytosedLigandGlcGalHyl-COL3A1(154-1241) 1,3-beta-D-glucan SCARA5 Heparins 3x4Hyp-5Hyl-COL1A2 CHEST Ig kappa chain V-I region Scw poly(G) IGLC2 lysophosphatidylcholine Double-stranded RNA hydroxy fatty acid 3x4Hyp-3Hyp-GlcGalHyl-COL1A1 Unmethylated CpG DNA N-epsilon-(1-(1-carboxy)ethyl)lysine 5xHC-HP(162-406) N-epsilon-(1-(1-carboxy)ethyl)lysine Ig lambda chain V-IV region MOL Ig heavy chain V-III region TEI Ig heavy chain V-III region WAS Ig heavy chain V-II region SESS L-fucose AcK-APOB(28-4563) NECML MARCO:LigandIg heavy chain V-III region DOB IGLV4-3(1-?) Ig kappa chain V-III region HAH TAGs 7-ketocholesterol Ig kappa chain V-I region WEA IGLV4-60(1-?) APOE Ig kappa chain V-III region HAH Ig kappa chain V-IV region STH Ig heavy chain V-III region BUT cholesterol esters IGHV(1-?) Ig kappa chain V-I region Gal Ligands of MARCOIg lambda chain V-II region WIN COL4A1(173-1669) 3x4Hyp-3Hyp-GlcGalHyl-COL1A1 COL3A1 10xdHF-10xglutamyl semialdehyde (Pro)-6xL-tyrosine residue-3xOxoH-2xmodified L-lysine residue-N'-formyl-L-kynurenine-APOB(28-4563) IGLV7-46(1-?) AcK-APOB(28-4563) oxidized phospholipids hydroxy fatty acid AcK-APOB(28-4563) 6xHC-MSR1 GalHyl-COL1A2 thioether crosslinked C53-AMBP(20-202) IGLV1-44(1-?) Ig heavy chain V-III region NIE hydroperoxy fatty acid CHEST Denatured CollagenI,III, Collagen IVIGLV10-54(1-?) Ig heavy chain V-II region NEWM COL3A1 Ig heavy chain V-I region EU IGLV3-22(1-?) Haptoglobin DimerLRP1:Hemopexin:hemeSPARC PL Phosphatidylserine Ig lambda chain V-IV region Kern 7xHC-HP(19-160) CHOL Hemoglobin:Haptoglobin:CD163AcK-APOB(28-4563) 5Hyl-COL1A2 Ig heavy chain V-III region TIL LPS IGLV3-16(1-?) Ig lambda chain V-II region BO PI Phosphatidylserine LPS hydroxy fatty acid hydroperoxy fatty acid MSR1:LigandIg heavy chain V-II region OU N-epsilon-(1-(1-carboxy)ethyl)lysine PlateletglycoproteinIV:LigandIg kappa chain V-II region RPMI 6410 Ig heavy chain V-III region CAM 10xdHF-10xglutamyl semialdehyde (Pro)-6xL-tyrosine residue-3xOxoH-2xmodified L-lysine residue-N'-formyl-L-kynurenine-APOB(28-4563) LPS IGKV1-5(23-?) NECML Ig lambda chain V-II region TRO Ig kappa chain V-III region B6 Ig lambda chain V-I region BL2 5Hyl-COL3A1 Ig heavy chain V-II region SESS AMBP(20-202)Double-stranded RNA Ig kappa chain V-I region Mev 3x4Hyp-GlcGalHyl-COL3A1 Ig kappa chain V-III region IARC/BL41 PL IGLV4-69(1-?) 3x4Hyp-5Hyl-COL1A2 5,6beta-epoxy-cholesterol Ig lambda chain V region 4A Ig lambda chain V-II region TOG Ig heavy chain V-I region Mot Fe3+ 7xHC-HP(19-160) Ig heavy chain V-III region BUR 3x4Hyp-3Hyp-5Hyl-COL1A1 CHEST O2 STAB1:LigandHUA 3x4Hyp-3Hyp-5Hyl-COL1A1 Ig heavy chain V-III region GAL GalNAc Ig heavy chain V-I region HG3 HPX Peptide COL1A2 carrageenan 10xdHF-10xglutamyl semialdehyde (Pro)-6xL-tyrosine residue-3xOxoH-2xmodified L-lysine residue-N'-formyl-L-kynurenine-APOB(28-4563) SCARB1-2 IGLC7 3x4Hyp-3Hyp-COL1A1 TAGs hydroxy fatty acid Peptide Ig heavy chain V-III region TRO Double-stranded RNA IGHA2 Ig kappa chain V-I region AU lysophosphatidylcholine 3x4Hyp-GalHyl-COL1A2 Ig kappa chain V-I region HK101 hydroxy fatty acid IGKVA18(21-?) Fe3+ Ig kappa chain V-I region BAN Ig lambda chain V-II region NEI hydroperoxy fatty acid IGLV5-45(1-?) Ig heavy chain V-II region WAH Unmethylated CpG DNA Ig heavy chain V-III region KOL 10xdHF-10xglutamyl semialdehyde (Pro)-6xL-tyrosine residue-3xOxoH-2xmodified L-lysine residue-N'-formyl-L-kynurenine-APOB(28-4563) oxidized phospholipids ALB7-ketocholesterol PI HSP90B1 N-epsilon-(1-(1-carboxy)ethyl)lysine 10xdHF-10xglutamyl semialdehyde (Pro)-6xL-tyrosine residue-3xOxoH-2xmodified L-lysine residue-N'-formyl-L-kynurenine-APOB(28-4563) Ig kappa chain V-I region AU Ig lambda chain V-I region WAH CHEST cholesterol LPS CHOL 3x4Hyp-3Hyp-5Hyl-COL3A1 COL1A1 LPS Phosphatidylserine SCARB1-2Ig kappa chain V-III region GOL cholesterol hydroperoxy fatty acid carrageenan Ig kappa chain V-II region FR APOA1(25-266) AcK-APOB(28-4563) FTL cholesterol esters 3x4Hyp-3Hyp-5Hyl-COL1A2 hydroperoxy fatty acid lysophosphatidylcholine heme b Phosphatidylserine COLEC12:LigandHSPH1 HPX:ferriheme blysophosphatidylcholine SCGB3A2 Peptide Ig kappa chain V-III region VG 3x4Hyp-3Hyp-GalHyl-COL3A1 Ig lambda chain V-I region HA silicon dioxide nanoparticle ferriheme b NECML Lipoteichoic acid HBA1 IGLV7-43(1-?) MARCO:LigandAPOA1(25-266) Ig heavy chain V-III region BRO Ig lambda chain V-II region NIG-84 10xdHF-10xglutamyl semialdehyde (Pro)-6xL-tyrosine residue-3xOxoH-2xmodified L-lysine residue-N'-formyl-L-kynurenine-APOB(28-4563) APOA1(25-266) CALR 3x4Hyp-GalHyl-COL1A2 Heparins LPS FTL PL Ig heavy chain V-II region ARH-77 MASP1(20-699) APOB(28-4563) IGLV1-40(1-?) AMBP(20-202) Ligands of SCARF1Ig kappa chain V-I region Lay Ig kappa chain V-I region Walker Ig kappa chain V-IV region STH GalHyl-COL3A1 Ig heavy chain V-III region DOB PlateletglycoproteinIV:LigandTAGs 3x4Hyp-3Hyp-GlcGalHyl-COL3A1 lysophosphatidylcholine AMBP(20-198)Ig lambda chain V-VI region SUT 4xPalmC-CD36 Man IGLV3-27(1-?) PI FTH1 Lipoteichoic acid CHOL Ig kappa chain V-III region CLL ferroheme b Ig heavy chain V-I region HG3 titanium dioxide nanoparticle Ig kappa chain V-I region EU Lipoteichoic acid Hemoglobin DimerHPR AcK-APOB(28-4563) Ig lambda chain V-II region BOH 5Hyl-COL1A1 Ig lambda chain V-VI region EB4 IGLV8-61(1-?) Phosphatidylserine Ig heavy chain V-I region ND Ig heavy chain V-I region ND 7-ketocholesterol Ig kappa chain V-III region VH HYOU1 7-ketocholesterol Ig lambda chain V-II region BUR heme bIg kappa chain V-III region HIC ferriheme b FTL SCARB1:Ligandhydroxy fatty acid Ig lambda chain V-VI region NIG-48 Peptide PL Ig kappa chain V-I region Ni NECML IGLV1-40(1-?) 6xHC-MARCO FTH1 hydroxy fatty acid HBA1 3x4Hyp-COL1A1 Ig kappa chain V-IV region B17 CD163 Ig kappa chain V-IV region JI cholesterol esters Ig kappa chain V-II region RPMI 6410 Hemoglobin:Haptoglobin:CD163Ig lambda chain V-VI region EB4 NECML PL Lipoteichoic acid SCARA5 SCARF1 Ig kappa chain V-III region VH Ig lambda chain V-II region WIN HSP90B1 cholesterol esters Ig kappa chain V-III region SIE Ig kappa chain V-I region Mev LPS heme b Ig kappa chain V-I region Hau HSPH1 L-fucose COL1A2 AcK-APOB(28-4563) CD163 NECML IGHA1 13, 28, 38, 71, 845967, 1026, 30, 1244822, 341454882724820, 881453, 37, 42, 44, 50...61, 128, 135, 1416, 30, 12459454519, 37, 86, 136, 150...12514531, 55, 97, 123, 1495, 53, 64, 104, 127725982606020, 74, 881456314559125145955913, 28, 38, 71, 846019, 37, 86, 136, 150...5961, 115, 128, 135, 1415913, 28, 38, 71, 843, 37, 42, 44, 50...61, 128, 135, 14114559483, 37, 42, 44, 50...8319, 37, 86, 136, 150...601455914514548, 122125, 1525914514149, 77, 88, 132, 151...5920, 8859679, 10259125, 152591451451257248, 13324, 76, 105, 112, 141...458267, 1025948145675912214583125, 152104, 127145


Description

Scavenger receptors bind free extracellular ligands as the initial step in clearance of the ligands from the body (reviewed in Ascenzi et al. 2005, Areschoug and Gordon 2009, Nielsen et al. 2010). Some scavenger receptors, such as the CD163-haptoglobin system, are specific for only one ligand. Others, such as the SCARA receptors (SR-A receptors) are less specific, binding several ligands which share a common property, such as polyanionic charges.
Brown and Goldstein originated the idea of receptors dedicated to scavenging aberrant molecules such as modified low density lipoprotein particles (Goldstein et al. 1979) and such receptors have been shown to participate in pathological processes such as atherosclerosis. Based on homology, scavenger receptors have been categorized into classes A-H (reviewed in Murphy et al. 2005). View original pathway at:Reactome.

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Bibliography

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  133. Apostolov EO, Shah SV, Ray D, Basnakian AG.; ''Scavenger receptors of endothelial cells mediate the uptake and cellular proatherogenic effects of carbamylated LDL.''; PubMed Europe PMC Scholia
  134. Facciponte JG, Wang XY, Subjeck JR.; ''Hsp110 and Grp170, members of the Hsp70 superfamily, bind to scavenger receptor-A and scavenger receptor expressed by endothelial cells-I.''; PubMed Europe PMC Scholia
  135. Sakai M, Miyazaki A, Hakamata H, Kobori S, Shichiri M, Horiuchi S.; ''Endocytic uptake of lysophosphatidylcholine mediated by macrophage scavenger receptor plays a major role in oxidized low density lipoprotein-induced macrophage growth.''; PubMed Europe PMC Scholia
  136. Adams PA, Berman MC.; ''Kinetics and mechanism of the interaction between human serum albumin and monomeric haemin.''; PubMed Europe PMC Scholia
  137. Smith A, Farooqui SM, Morgan WT.; ''The murine haemopexin receptor. Evidence that the haemopexin-binding site resides on a 20 kDa subunit and that receptor recycling is regulated by protein kinase C.''; PubMed Europe PMC Scholia
  138. Morgan WT, Liem HH, Sutor RP, Muller-Ebergard U.; ''Transfer of heme from heme-albumin to hemopexin.''; PubMed Europe PMC Scholia
  139. Santiago-García J, Kodama T, Pitas RE.; ''The class A scavenger receptor binds to proteoglycans and mediates adhesion of macrophages to the extracellular matrix.''; PubMed Europe PMC Scholia
  140. Widener J, Nielsen MJ, Shiflett A, Moestrup SK, Hajduk S.; ''Hemoglobin is a co-factor of human trypanosome lytic factor.''; PubMed Europe PMC Scholia
  141. Resnick D, Chatterton JE, Schwartz K, Slayter H, Krieger M.; ''Structures of class A macrophage scavenger receptors. Electron microscopic study of flexible, multidomain, fibrous proteins and determination of the disulfide bond pattern of the scavenger receptor cysteine-rich domain.''; PubMed Europe PMC Scholia
  142. Dunne DW, Resnick D, Greenberg J, Krieger M, Joiner KA.; ''The type I macrophage scavenger receptor binds to gram-positive bacteria and recognizes lipoteichoic acid.''; PubMed Europe PMC Scholia
  143. Shiflett AM, Bishop JR, Pahwa A, Hajduk SL.; ''Human high density lipoproteins are platforms for the assembly of multi-component innate immune complexes.''; PubMed Europe PMC Scholia
  144. Keshi H, Sakamoto T, Kawai T, Ohtani K, Katoh T, Jang SJ, Motomura W, Yoshizaki T, Fukuda M, Koyama S, Fukuzawa J, Fukuoh A, Yoshida I, Suzuki Y, Wakamiya N.; ''Identification and characterization of a novel human collectin CL-K1.''; PubMed Europe PMC Scholia
  145. Berwin B, Hart JP, Rice S, Gass C, Pizzo SV, Post SR, Nicchitta CV.; ''Scavenger receptor-A mediates gp96/GRP94 and calreticulin internalization by antigen-presenting cells.''; PubMed Europe PMC Scholia
  146. Dahl M, Bauer AK, Arredouani M, Soininen R, Tryggvason K, Kleeberger SR, Kobzik L.; ''Protection against inhaled oxidants through scavenging of oxidized lipids by macrophage receptors MARCO and SR-AI/II.''; PubMed Europe PMC Scholia
  147. Janabi M, Yamashita S, Hirano K, Sakai N, Hiraoka H, Matsumoto K, Zhang Z, Nozaki S, Matsuzawa Y.; ''Oxidized LDL-induced NF-kappa B activation and subsequent expression of proinflammatory genes are defective in monocyte-derived macrophages from CD36-deficient patients.''; PubMed Europe PMC Scholia
  148. Podrez EA, Poliakov E, Shen Z, Zhang R, Deng Y, Sun M, Finton PJ, Shan L, Gugiu B, Fox PL, Hoff HF, Salomon RG, Hazen SL.; ''Identification of a novel family of oxidized phospholipids that serve as ligands for the macrophage scavenger receptor CD36.''; PubMed Europe PMC Scholia
  149. Park SY, Jung MY, Lee SJ, Kang KB, Gratchev A, Riabov V, Kzhyshkowska J, Kim IS.; ''Stabilin-1 mediates phosphatidylserine-dependent clearance of cell corpses in alternatively activated macrophages.''; PubMed Europe PMC Scholia
  150. Yokota T, Ehlin-Henriksson B, Hansson GK.; ''Scavenger receptors mediate adhesion of activated B lymphocytes.''; PubMed Europe PMC Scholia
  151. Tao N, Wagner SJ, Lublin DM.; ''CD36 is palmitoylated on both N- and C-terminal cytoplasmic tails.''; PubMed Europe PMC Scholia
  152. Arredouani MS, Palecanda A, Koziel H, Huang YC, Imrich A, Sulahian TH, Ning YY, Yang Z, Pikkarainen T, Sankala M, Vargas SO, Takeya M, Tryggvason K, Kobzik L.; ''MARCO is the major binding receptor for unopsonized particles and bacteria on human alveolar macrophages.''; PubMed Europe PMC Scholia
  153. Nielsen MJ, Petersen SV, Jacobsen C, Thirup S, Enghild JJ, Graversen JH, Graversen JH, Moestrup SK.; ''A unique loop extension in the serine protease domain of haptoglobin is essential for CD163 recognition of the haptoglobin-hemoglobin complex.''; PubMed Europe PMC Scholia
  154. Hansen B, Longati P, Elvevold K, Nedredal GI, Schledzewski K, Olsen R, Falkowski M, Kzhyshkowska J, Carlsson F, Johansson S, Smedsrød B, Goerdt S, Johansson S, McCourt P.; ''Stabilin-1 and stabilin-2 are both directed into the early endocytic pathway in hepatic sinusoidal endothelium via interactions with clathrin/AP-2, independent of ligand binding.''; PubMed Europe PMC Scholia
  155. Vishnyakova TG, Bocharov AV, Baranova IN, Chen Z, Remaley AT, Csako G, Eggerman TL, Patterson AP.; ''Binding and internalization of lipopolysaccharide by Cla-1, a human orthologue of rodent scavenger receptor B1.''; PubMed Europe PMC Scholia
  156. Smith A, Morgan WT.; ''Haem transport to the liver by haemopexin. Receptor-mediated uptake with recycling of the protein.''; PubMed Europe PMC Scholia
  157. Gowen BB, Borg TK, Ghaffar A, Mayer EP.; ''Selective adhesion of macrophages to denatured forms of type I collagen is mediated by scavenger receptors.''; PubMed Europe PMC Scholia
  158. Morgan WT.; ''The binding and transport of heme by hemopexin.''; PubMed Europe PMC Scholia
  159. Palani S, Maksimow M, Miiluniemi M, Auvinen K, Jalkanen S, Salmi M.; ''Stabilin-1/CLEVER-1, a type 2 macrophage marker, is an adhesion and scavenging molecule on human placental macrophages.''; PubMed Europe PMC Scholia
  160. Endemann G, Stanton LW, Madden KS, Bryant CM, White RT, Protter AA.; ''CD36 is a receptor for oxidized low density lipoprotein.''; PubMed Europe PMC Scholia

History

View all...
CompareRevisionActionTimeUserComment
117864view10:15, 23 May 2021EweitzModified title
114786view16:28, 25 January 2021ReactomeTeamReactome version 75
113231view11:29, 2 November 2020ReactomeTeamReactome version 74
112452view15:40, 9 October 2020ReactomeTeamReactome version 73
101359view11:25, 1 November 2018ReactomeTeamreactome version 66
100897view20:59, 31 October 2018ReactomeTeamreactome version 65
100438view19:34, 31 October 2018ReactomeTeamreactome version 64
99987view16:18, 31 October 2018ReactomeTeamreactome version 63
99541view14:52, 31 October 2018ReactomeTeamreactome version 62 (2nd attempt)
99175view12:42, 31 October 2018ReactomeTeamreactome version 62
93792view13:36, 16 August 2017ReactomeTeamreactome version 61
93328view11:20, 9 August 2017ReactomeTeamreactome version 61
87094view14:28, 18 July 2016MkutmonOntology Term : 'transport pathway' added !
86413view09:17, 11 July 2016ReactomeTeamreactome version 56
83217view10:25, 18 November 2015ReactomeTeamVersion54
81607view13:09, 21 August 2015ReactomeTeamVersion53
77068view08:36, 17 July 2014ReactomeTeamFixed remaining interactions
76773view12:13, 16 July 2014ReactomeTeamFixed remaining interactions
76096view10:16, 11 June 2014ReactomeTeamRe-fixing comment source
75808view11:35, 10 June 2014ReactomeTeamReactome 48 Update
75158view14:10, 8 May 2014AnweshaFixing comment source for displaying WikiPathways description
74805view08:54, 30 April 2014ReactomeTeamNew pathway

External references

DataNodes

View all...
NameTypeDatabase referenceComment
1,3-beta-D-glucan MetaboliteCHEBI:37671 (ChEBI)
10xdHF-10xglutamyl semialdehyde (Pro)-6xL-tyrosine residue-3xOxoH-2xmodified L-lysine residue-N'-formyl-L-kynurenine-APOB(28-4563) ProteinP04114 (Uniprot-TrEMBL)
3x4Hyp-3Hyp-5Hyl-COL1A1 ProteinP02452 (Uniprot-TrEMBL)
3x4Hyp-3Hyp-5Hyl-COL1A2 ProteinP08123 (Uniprot-TrEMBL)
3x4Hyp-3Hyp-5Hyl-COL3A1 ProteinP02461 (Uniprot-TrEMBL)
3x4Hyp-3Hyp-COL1A1 ProteinP02452 (Uniprot-TrEMBL)
3x4Hyp-3Hyp-COL1A2 ProteinP08123 (Uniprot-TrEMBL)
3x4Hyp-3Hyp-COL3A1 ProteinP02461 (Uniprot-TrEMBL)
3x4Hyp-3Hyp-GalHyl-COL1A1 ProteinP02452 (Uniprot-TrEMBL)
3x4Hyp-3Hyp-GalHyl-COL1A2 ProteinP08123 (Uniprot-TrEMBL)
3x4Hyp-3Hyp-GalHyl-COL3A1 ProteinP02461 (Uniprot-TrEMBL)
3x4Hyp-3Hyp-GlcGalHyl-COL1A1 ProteinP02452 (Uniprot-TrEMBL)
3x4Hyp-3Hyp-GlcGalHyl-COL1A2 ProteinP08123 (Uniprot-TrEMBL)
3x4Hyp-3Hyp-GlcGalHyl-COL3A1 ProteinP02461 (Uniprot-TrEMBL)
3x4Hyp-5Hyl-COL1A1 ProteinP02452 (Uniprot-TrEMBL)
3x4Hyp-5Hyl-COL1A2 ProteinP08123 (Uniprot-TrEMBL)
3x4Hyp-5Hyl-COL3A1 ProteinP02461 (Uniprot-TrEMBL)
3x4Hyp-COL1A1 ProteinP02452 (Uniprot-TrEMBL)
3x4Hyp-COL1A2 ProteinP08123 (Uniprot-TrEMBL)
3x4Hyp-COL3A1 ProteinP02461 (Uniprot-TrEMBL)
3x4Hyp-GalHyl-COL1A1 ProteinP02452 (Uniprot-TrEMBL)
3x4Hyp-GalHyl-COL1A2 ProteinP08123 (Uniprot-TrEMBL)
3x4Hyp-GalHyl-COL3A1 ProteinP02461 (Uniprot-TrEMBL)
3x4Hyp-GlcGalHyl-COL1A1 ProteinP02452 (Uniprot-TrEMBL)
3x4Hyp-GlcGalHyl-COL1A2 ProteinP08123 (Uniprot-TrEMBL)
3x4Hyp-GlcGalHyl-COL3A1 ProteinP02461 (Uniprot-TrEMBL)
4xPalmC-CD36 ProteinP16671 (Uniprot-TrEMBL)
4xPalmC-CD36ProteinP16671 (Uniprot-TrEMBL)
5,6beta-epoxy-cholesterol MetaboliteCHEBI:28164 (ChEBI)
5Hyl-COL1A1 ProteinP02452 (Uniprot-TrEMBL)
5Hyl-COL1A2 ProteinP08123 (Uniprot-TrEMBL)
5Hyl-COL3A1 ProteinP02461 (Uniprot-TrEMBL)
5xHC-HP(162-406) ProteinP00738 (Uniprot-TrEMBL)
6xHC-MARCO ProteinQ9UEW3 (Uniprot-TrEMBL)
6xHC-MSR1 ProteinP21757 (Uniprot-TrEMBL)
7-ketocholesterol MetaboliteCHEBI:64294 (ChEBI)
7xHC-HP(19-160) ProteinP00738 (Uniprot-TrEMBL)
ALB ProteinP02768 (Uniprot-TrEMBL)
ALBProteinP02768 (Uniprot-TrEMBL)
AMBP(20-198) ProteinP02760 (Uniprot-TrEMBL)
AMBP(20-198)ProteinP02760 (Uniprot-TrEMBL)
AMBP(20-202) ProteinP02760 (Uniprot-TrEMBL)
AMBP(20-202)ProteinP02760 (Uniprot-TrEMBL)
APOA1(25-266) ProteinP02647 (Uniprot-TrEMBL)
APOB(28-4563) ProteinP04114 (Uniprot-TrEMBL)
APOE ProteinP02649 (Uniprot-TrEMBL)
APOL1 ProteinO14791 (Uniprot-TrEMBL)
AcK-APOB(28-4563) ProteinP04114 (Uniprot-TrEMBL)
Albumin:ferrihemeComplexR-HSA-2168871 (Reactome)
Alpha1-Microglobulin:heme trimerComplexR-HSA-2512834 (Reactome)
ApohemoglobinComplexR-HSA-2168856 (Reactome)
CALR ProteinP27797 (Uniprot-TrEMBL)
CD163 ProteinQ86VB7 (Uniprot-TrEMBL)
CD163ProteinQ86VB7 (Uniprot-TrEMBL)
CHEST MetaboliteCHEBI:17002 (ChEBI)
CHOL MetaboliteCHEBI:16113 (ChEBI)
CHS MetaboliteCHEBI:37397 (ChEBI)
COL1A1 ProteinP02452 (Uniprot-TrEMBL)
COL1A2 ProteinP08123 (Uniprot-TrEMBL)
COL3A1 ProteinP02461 (Uniprot-TrEMBL)
COL4A1(173-1669) ProteinP02462 (Uniprot-TrEMBL)
COL4A2(184-1712) ProteinP08572 (Uniprot-TrEMBL)
COLEC11 ProteinQ9BWP8 (Uniprot-TrEMBL)
COLEC11:LigandComplexR-HSA-2203468 (Reactome)
COLEC11:MASP1ComplexR-HSA-2981041 (Reactome)
COLEC12 ProteinQ5KU26 (Uniprot-TrEMBL)
COLEC12 trimerComplexR-HSA-2187243 (Reactome)
COLEC12:LigandComplexR-HSA-2187245 (Reactome)
COLEC12:LigandComplexR-HSA-2981043 (Reactome)
DNA R-NUL-2203467 (Reactome)
Denatured Collagen I,III, Collagen IVComplexR-HSA-3221907 (Reactome)
Double-stranded RNA R-NUL-2173769 (Reactome)
Double-stranded RNA R-NUL-2507849 (Reactome)
FTH1 ProteinP02794 (Uniprot-TrEMBL)
FTL ProteinP02792 (Uniprot-TrEMBL)
Fe3+ MetaboliteCHEBI:29034 (ChEBI)
GalHyl-COL1A1 ProteinP02452 (Uniprot-TrEMBL)
GalHyl-COL1A2 ProteinP08123 (Uniprot-TrEMBL)
GalHyl-COL3A1 ProteinP02461 (Uniprot-TrEMBL)
GalNAc MetaboliteCHEBI:28037 (ChEBI)
GlcGalHyl-COL1A1 ProteinP02452 (Uniprot-TrEMBL)
GlcGalHyl-COL1A2 ProteinP08123 (Uniprot-TrEMBL)
GlcGalHyl-COL3A1(154-1241) ProteinP02461 (Uniprot-TrEMBL)
GlcNAc MetaboliteCHEBI:17411 (ChEBI)
HBA1 ProteinP69905 (Uniprot-TrEMBL)
HBB ProteinP68871 (Uniprot-TrEMBL)
HPR ProteinP00739 (Uniprot-TrEMBL)
HPR:APOL1:APOA1:HDL3ComplexR-HSA-2168878 (Reactome)
HPX ProteinP02790 (Uniprot-TrEMBL)
HPX:ferriheme bComplexR-HSA-2203498 (Reactome)
HPX:heme bComplexR-HSA-2168851 (Reactome)
HPXProteinP02790 (Uniprot-TrEMBL)
HSP90AA1 ProteinP07900 (Uniprot-TrEMBL)
HSP90B1 ProteinP14625 (Uniprot-TrEMBL)
HSPH1 ProteinQ92598 (Uniprot-TrEMBL)
HUA MetaboliteCHEBI:16336 (ChEBI)
HYOU1 ProteinQ9Y4L1 (Uniprot-TrEMBL)
Haptoglobin DimerComplexR-HSA-2168859 (Reactome)
Hemoglobin DimerComplexR-HSA-2168876 (Reactome)
Hemoglobin:HPR:APOL1:APOA1:HDL3ComplexR-HSA-2168857 (Reactome)
Hemoglobin:Haptoglobin:CD163ComplexR-HSA-2168879 (Reactome)
Hemoglobin:Haptoglobin:CD163ComplexR-HSA-2230960 (Reactome)
Hemoglobin:HaptoglobinComplexR-HSA-2168869 (Reactome)
Heparins MetaboliteCHEBI:24505 (ChEBI)
IGHA1 ProteinP01876 (Uniprot-TrEMBL)
IGHA2 ProteinP01877 (Uniprot-TrEMBL)
IGHV(1-?) ProteinA2KUC3 (Uniprot-TrEMBL)
IGHV7-81(1-?) ProteinQ6PIL0 (Uniprot-TrEMBL)
IGKC ProteinP01834 (Uniprot-TrEMBL)
IGKV1-5(23-?) ProteinP01602 (Uniprot-TrEMBL)
IGKV4-1(21-?) ProteinP06312 (Uniprot-TrEMBL)
IGKVA18(21-?) ProteinA2NJV5 (Uniprot-TrEMBL)
IGLC1 ProteinP0CG04 (Uniprot-TrEMBL)
IGLC2 ProteinP0CG05 (Uniprot-TrEMBL)
IGLC3 ProteinP0CG06 (Uniprot-TrEMBL)
IGLC6 ProteinP0CF74 (Uniprot-TrEMBL)
IGLC7 ProteinA0M8Q6 (Uniprot-TrEMBL)
IGLV(23-?) ProteinA2NXD2 (Uniprot-TrEMBL)
IGLV1-36(1-?) ProteinQ5NV67 (Uniprot-TrEMBL)
IGLV1-40(1-?) ProteinQ5NV69 (Uniprot-TrEMBL)
IGLV1-44(1-?) ProteinQ5NV81 (Uniprot-TrEMBL)
IGLV10-54(1-?) ProteinQ5NV86 (Uniprot-TrEMBL)
IGLV11-55(1-?) ProteinQ5NV87 (Uniprot-TrEMBL)
IGLV2-11(1-?) ProteinQ5NV84 (Uniprot-TrEMBL)
IGLV2-18(1-?) ProteinQ5NV65 (Uniprot-TrEMBL)
IGLV2-23(1-?) ProteinQ5NV89 (Uniprot-TrEMBL)
IGLV2-33(1-?) ProteinQ5NV66 (Uniprot-TrEMBL)
IGLV3-12(1-?) ProteinQ5NV85 (Uniprot-TrEMBL)
IGLV3-16(1-?) ProteinQ5NV64 (Uniprot-TrEMBL)
IGLV3-22(1-?) ProteinQ5NV75 (Uniprot-TrEMBL)
IGLV3-25(1-?) ProteinQ5NV90 (Uniprot-TrEMBL)
IGLV3-27(1-?) ProteinQ5NV91 (Uniprot-TrEMBL)
IGLV4-3(1-?) ProteinQ5NV61 (Uniprot-TrEMBL)
IGLV4-60(1-?) ProteinQ5NV79 (Uniprot-TrEMBL)
IGLV4-69(1-?) ProteinQ5NV92 (Uniprot-TrEMBL)
IGLV5-37(1-?) ProteinQ5NV68 (Uniprot-TrEMBL)
IGLV5-45(1-?) ProteinQ5NV82 (Uniprot-TrEMBL)
IGLV7-43(1-?) ProteinQ5NV80 (Uniprot-TrEMBL)
IGLV7-46(1-?) ProteinQ5NV83 (Uniprot-TrEMBL)
IGLV8-61(1-?) ProteinQ5NV62 (Uniprot-TrEMBL)
Ig heavy chain V-I region EU ProteinP01742 (Uniprot-TrEMBL)
Ig heavy chain V-I region HG3 ProteinP01743 (Uniprot-TrEMBL)
Ig heavy chain V-I region Mot ProteinP06326 (Uniprot-TrEMBL)
Ig heavy chain V-I region ND ProteinP01744 (Uniprot-TrEMBL)
Ig heavy chain V-I region SIE ProteinP01761 (Uniprot-TrEMBL)
Ig heavy chain V-I region WOL ProteinP01760 (Uniprot-TrEMBL)
Ig heavy chain V-II region ARH-77 ProteinP06331 (Uniprot-TrEMBL)
Ig heavy chain V-II region COR ProteinP01815 (Uniprot-TrEMBL)
Ig heavy chain V-II region DAW ProteinP01816 (Uniprot-TrEMBL)
Ig heavy chain V-II region HE ProteinP01818 (Uniprot-TrEMBL)
Ig heavy chain V-II region MCE ProteinP01817 (Uniprot-TrEMBL)
Ig heavy chain V-II region NEWM ProteinP01825 (Uniprot-TrEMBL)
Ig heavy chain V-II region OU ProteinP01814 (Uniprot-TrEMBL)
Ig heavy chain V-II region SESS ProteinP04438 (Uniprot-TrEMBL)
Ig heavy chain V-II region WAH ProteinP01824 (Uniprot-TrEMBL)
Ig heavy chain V-III region BRO ProteinP01766 (Uniprot-TrEMBL)
Ig heavy chain V-III region BUR ProteinP01773 (Uniprot-TrEMBL)
Ig heavy chain V-III region BUT ProteinP01767 (Uniprot-TrEMBL)
Ig heavy chain V-III region CAM ProteinP01768 (Uniprot-TrEMBL)
Ig heavy chain V-III region DOB ProteinP01782 (Uniprot-TrEMBL)
Ig heavy chain V-III region GA ProteinP01769 (Uniprot-TrEMBL)
Ig heavy chain V-III region GAL ProteinP01781 (Uniprot-TrEMBL)
Ig heavy chain V-III region HIL ProteinP01771 (Uniprot-TrEMBL)
Ig heavy chain V-III region JON ProteinP01780 (Uniprot-TrEMBL)
Ig heavy chain V-III region KOL ProteinP01772 (Uniprot-TrEMBL)
Ig heavy chain V-III region LAY ProteinP01775 (Uniprot-TrEMBL)
Ig heavy chain V-III region NIE ProteinP01770 (Uniprot-TrEMBL)
Ig heavy chain V-III region POM ProteinP01774 (Uniprot-TrEMBL)
Ig heavy chain V-III region TEI ProteinP01777 (Uniprot-TrEMBL)
Ig heavy chain V-III region TIL ProteinP01765 (Uniprot-TrEMBL)
Ig heavy chain V-III region TRO ProteinP01762 (Uniprot-TrEMBL)
Ig heavy chain V-III region TUR ProteinP01779 (Uniprot-TrEMBL)
Ig heavy chain V-III region WAS ProteinP01776 (Uniprot-TrEMBL)
Ig heavy chain V-III region WEA ProteinP01763 (Uniprot-TrEMBL)
Ig heavy chain V-III region ZAP ProteinP01778 (Uniprot-TrEMBL)
Ig kappa chain V region EV15 ProteinP06315 (Uniprot-TrEMBL)
Ig kappa chain V-I region AG ProteinP01593 (Uniprot-TrEMBL)
Ig kappa chain V-I region AU ProteinP01594 (Uniprot-TrEMBL)
Ig kappa chain V-I region BAN ProteinP04430 (Uniprot-TrEMBL)
Ig kappa chain V-I region Bi ProteinP01595 (Uniprot-TrEMBL)
Ig kappa chain V-I region CAR ProteinP01596 (Uniprot-TrEMBL)
Ig kappa chain V-I region DEE ProteinP01597 (Uniprot-TrEMBL)
Ig kappa chain V-I region Daudi ProteinP04432 (Uniprot-TrEMBL)
Ig kappa chain V-I region EU ProteinP01598 (Uniprot-TrEMBL)
Ig kappa chain V-I region Gal ProteinP01599 (Uniprot-TrEMBL)
Ig kappa chain V-I region HK101 ProteinP01601 (Uniprot-TrEMBL)
Ig kappa chain V-I region Hau ProteinP01600 (Uniprot-TrEMBL)
Ig kappa chain V-I region Ka ProteinP01603 (Uniprot-TrEMBL)
Ig kappa chain V-I region Kue ProteinP01604 (Uniprot-TrEMBL)
Ig kappa chain V-I region Lay ProteinP01605 (Uniprot-TrEMBL)
Ig kappa chain V-I region Mev ProteinP01612 (Uniprot-TrEMBL)
Ig kappa chain V-I region Ni ProteinP01613 (Uniprot-TrEMBL)
Ig kappa chain V-I region OU ProteinP01606 (Uniprot-TrEMBL)
Ig kappa chain V-I region Rei ProteinP01607 (Uniprot-TrEMBL)
Ig kappa chain V-I region Roy ProteinP01608 (Uniprot-TrEMBL)
Ig kappa chain V-I region Scw ProteinP01609 (Uniprot-TrEMBL)
Ig kappa chain V-I region WAT ProteinP80362 (Uniprot-TrEMBL)
Ig kappa chain V-I region WEA ProteinP01610 (Uniprot-TrEMBL)
Ig kappa chain V-I region Walker ProteinP04431 (Uniprot-TrEMBL)
Ig kappa chain V-I region Wes ProteinP01611 (Uniprot-TrEMBL)
Ig kappa chain V-II region Cum ProteinP01614 (Uniprot-TrEMBL)
Ig kappa chain V-II region FR ProteinP01615 (Uniprot-TrEMBL)
Ig kappa chain V-II region GM607 ProteinP06309 (Uniprot-TrEMBL)
Ig kappa chain V-II region MIL ProteinP01616 (Uniprot-TrEMBL)
Ig kappa chain V-II region RPMI 6410 ProteinP06310 (Uniprot-TrEMBL)
Ig kappa chain V-II region TEW ProteinP01617 (Uniprot-TrEMBL)
Ig kappa chain V-III region B6 ProteinP01619 (Uniprot-TrEMBL)
Ig kappa chain V-III region CLL ProteinP04207 (Uniprot-TrEMBL)
Ig kappa chain V-III region GOL ProteinP04206 (Uniprot-TrEMBL)
Ig kappa chain V-III region HAH ProteinP18135 (Uniprot-TrEMBL)
Ig kappa chain V-III region HIC ProteinP18136 (Uniprot-TrEMBL)
Ig kappa chain V-III region IARC/BL41 ProteinP06311 (Uniprot-TrEMBL)
Ig kappa chain V-III region NG9 ProteinP01621 (Uniprot-TrEMBL)
Ig kappa chain V-III region POM ProteinP01624 (Uniprot-TrEMBL)
Ig kappa chain V-III region SIE ProteinP01620 (Uniprot-TrEMBL)
Ig kappa chain V-III region Ti ProteinP01622 (Uniprot-TrEMBL)
Ig kappa chain V-III region VG ProteinP04433 (Uniprot-TrEMBL)
Ig kappa chain V-III region VH ProteinP04434 (Uniprot-TrEMBL)
Ig kappa chain V-III region WOL ProteinP01623 (Uniprot-TrEMBL)
Ig kappa chain V-IV region B17 ProteinP06314 (Uniprot-TrEMBL)
Ig kappa chain V-IV region JI ProteinP06313 (Uniprot-TrEMBL)
Ig kappa chain V-IV region Len ProteinP01625 (Uniprot-TrEMBL)
Ig kappa chain V-IV region STH ProteinP83593 (Uniprot-TrEMBL)
Ig lambda chain V region 4A ProteinP04211 (Uniprot-TrEMBL)
Ig lambda chain V-I region BL2 ProteinP06316 (Uniprot-TrEMBL)
Ig lambda chain V-I region EPS ProteinP06888 (Uniprot-TrEMBL)
Ig lambda chain V-I region HA ProteinP01700 (Uniprot-TrEMBL)
Ig lambda chain V-I region MEM ProteinP06887 (Uniprot-TrEMBL)
Ig lambda chain V-I region NEW ProteinP01701 (Uniprot-TrEMBL)
Ig lambda chain V-I region NEWM ProteinP01703 (Uniprot-TrEMBL)
Ig lambda chain V-I region NIG-64 ProteinP01702 (Uniprot-TrEMBL)
Ig lambda chain V-I region VOR ProteinP01699 (Uniprot-TrEMBL)
Ig lambda chain V-I region WAH ProteinP04208 (Uniprot-TrEMBL)
Ig lambda chain V-II region BO ProteinP01710 (Uniprot-TrEMBL)
Ig lambda chain V-II region BOH ProteinP01706 (Uniprot-TrEMBL)
Ig lambda chain V-II region BUR ProteinP01708 (Uniprot-TrEMBL)
Ig lambda chain V-II region MGC ProteinP01709 (Uniprot-TrEMBL)
Ig lambda chain V-II region NEI ProteinP01705 (Uniprot-TrEMBL)
Ig lambda chain V-II region NIG-58 ProteinP01713 (Uniprot-TrEMBL)
Ig lambda chain V-II region NIG-84 ProteinP04209 (Uniprot-TrEMBL)
Ig lambda chain V-II region TOG ProteinP01704 (Uniprot-TrEMBL)
Ig lambda chain V-II region TRO ProteinP01707 (Uniprot-TrEMBL)
Ig lambda chain V-II region VIL ProteinP01711 (Uniprot-TrEMBL)
Ig lambda chain V-II region WIN ProteinP01712 (Uniprot-TrEMBL)
Ig lambda chain V-III region LOI ProteinP80748 (Uniprot-TrEMBL)
Ig lambda chain V-III region SH ProteinP01714 (Uniprot-TrEMBL)
Ig lambda chain V-IV region Bau ProteinP01715 (Uniprot-TrEMBL)
Ig lambda chain V-IV region Hil ProteinP01717 (Uniprot-TrEMBL)
Ig lambda chain V-IV region Kern ProteinP01718 (Uniprot-TrEMBL)
Ig lambda chain V-IV region MOL ProteinP06889 (Uniprot-TrEMBL)
Ig lambda chain V-IV region X ProteinP01716 (Uniprot-TrEMBL)
Ig lambda chain V-V region DEL ProteinP01719 (Uniprot-TrEMBL)
Ig lambda chain V-VI region AR ProteinP01721 (Uniprot-TrEMBL)
Ig lambda chain V-VI region EB4 ProteinP06319 (Uniprot-TrEMBL)
Ig lambda chain V-VI region NIG-48 ProteinP01722 (Uniprot-TrEMBL)
Ig lambda chain V-VI region SUT ProteinP06317 (Uniprot-TrEMBL)
Ig lambda chain V-VI region WLT ProteinP06318 (Uniprot-TrEMBL)
Ig lambda chain V-VII region MOT ProteinP01720 (Uniprot-TrEMBL)
IgA:Alpha-1-MicroglobulinComplexR-HSA-2203510 (Reactome)
IgAComplexR-HSA-1479277 (Reactome)
IgH heavy chain V-III region VH26 precursor ProteinP01764 (Uniprot-TrEMBL)
L-fucose MetaboliteCHEBI:2181 (ChEBI)
LCFAs MetaboliteCHEBI:15904 (ChEBI)
LPS MetaboliteCHEBI:16412 (ChEBI)
LRP1 ProteinQ07954 (Uniprot-TrEMBL)
LRP1:Hemopexin:hemeComplexR-HSA-2168892 (Reactome)
LRP1:Hemopexin:hemeComplexR-HSA-2230986 (Reactome)
LRP1ProteinQ07954 (Uniprot-TrEMBL)
Ligands of CD36ComplexR-HSA-2187232 (Reactome)
Ligands of COLEC11ComplexR-HSA-R-ALL-2203469 (Reactome)
Ligands of COLEC12ComplexR-HSA-2187235 (Reactome)
Ligands of MARCOComplexR-HSA-2173758 (Reactome)
Ligands of MSR1ComplexR-HSA-2173760 (Reactome)
Ligands of SCARA5ComplexR-HSA-2187242 (Reactome)
Ligands of SCARB1ComplexR-HSA-2197637 (Reactome)
Ligands of SCARF1ComplexR-HSA-2197640 (Reactome)
Ligands of STAB1ComplexR-HSA-2197767 (Reactome)
Ligands of STAB2ComplexR-HSA-2197765 (Reactome)
Lipoteichoic acid MetaboliteCHEBI:28640 (ChEBI)
MARCO trimerComplexR-HSA-2173759 (Reactome)
MARCO:LigandComplexR-HSA-2173772 (Reactome)
MARCO:LigandComplexR-HSA-2239517 (Reactome)
MASP1(20-699) ProteinP48740 (Uniprot-TrEMBL)
MSR1 (SCARA1) trimerComplexR-HSA-2173771 (Reactome)
MSR1:Collagen I,III,IVComplexR-HSA-3221871 (Reactome)
MSR1:LigandComplexR-HSA-2173774 (Reactome)
MSR1:LigandComplexR-HSA-2507847 (Reactome)
Man MetaboliteCHEBI:4208 (ChEBI)
MethemoglobinComplexR-HSA-2168866 (Reactome)
N-epsilon-(1-(1-carboxy)ethyl)lysine MetaboliteCHEBI:60125 (ChEBI)
NECML MetaboliteCHEBI:53014 (ChEBI)
O2 MetaboliteCHEBI:15379 (ChEBI)
PI MetaboliteCHEBI:16749 (ChEBI)
PL MetaboliteCHEBI:16247 (ChEBI)
Peptide MetaboliteCHEBI:16670 (ChEBI)
Phosphatidylserine MetaboliteCHEBI:18303 (ChEBI)
Platelet

glycoprotein

IV:Ligand		ComplexR-HSA-2187250 (Reactome)
Platelet

glycoprotein

IV:Ligand		ComplexR-HSA-2247505 (Reactome)
SAA1(19-122) ProteinP0DJI8 (Uniprot-TrEMBL)
SCARA5 ProteinQ6ZMJ2 (Uniprot-TrEMBL)
SCARA5 trimerComplexR-HSA-2187252 (Reactome)
SCARA5:LigandComplexR-HSA-2187254 (Reactome)
SCARA5:LigandComplexR-HSA-2299667 (Reactome)
SCARB1-2 ProteinQ8WTV0-2 (Uniprot-TrEMBL)
SCARB1-2ProteinQ8WTV0-2 (Uniprot-TrEMBL)
SCARB1:Endocytosed LigandComplexR-HSA-2512792 (Reactome)
SCARB1:Endocytosed LigandComplexR-HSA-2512799 (Reactome)
SCARB1:LigandComplexR-HSA-2197639 (Reactome)
SCARF1 ProteinQ14162 (Uniprot-TrEMBL)
SCARF1:LigandComplexR-HSA-2197638 (Reactome)
SCARF1:LigandComplexR-HSA-2247507 (Reactome)
SCARF1ProteinQ14162 (Uniprot-TrEMBL)
SCGB3A2 ProteinQ96PL1 (Uniprot-TrEMBL)
SPARC ProteinP09486 (Uniprot-TrEMBL)
STAB1 ProteinQ9NY15 (Uniprot-TrEMBL)
STAB1:LigandComplexR-HSA-2197764 (Reactome)
STAB1:LigandComplexR-HSA-2247508 (Reactome)
STAB1ProteinQ9NY15 (Uniprot-TrEMBL)
STAB2(1136-2551) ProteinQ8WWQ8 (Uniprot-TrEMBL)
STAB2(1136-2551)ProteinQ8WWQ8 (Uniprot-TrEMBL)
STAB2:LigandComplexR-HSA-2203471 (Reactome)
STAB2:LigandComplexR-HSA-2247504 (Reactome)
TAGs MetaboliteCHEBI:17855 (ChEBI)
Truncated Alpha1-Microglobulin:heme trimerComplexR-HSA-2512859 (Reactome)
Unmethylated CpG DNA R-NUL-3221682 (Reactome)
Unmethylated CpG DNA R-NUL-3221685 (Reactome)
carrageenan MetaboliteCHEBI:3435 (ChEBI)
cholesterol MetaboliteCHEBI:16113 (ChEBI)
cholesterol esters MetaboliteCHEBI:17002 (ChEBI)
dextran sulfate MetaboliteCHEBI:34674 (ChEBI)
ferriheme b MetaboliteCHEBI:36144 (ChEBI)
ferroheme b MetaboliteCHEBI:17627 (ChEBI)
hematite nanoparticle MetaboliteCHEBI:50824 (ChEBI)
heme b MetaboliteCHEBI:26355 (ChEBI)
heme bMetaboliteCHEBI:26355 (ChEBI)
heme bComplexR-HSA-R-ALL-2203503 (Reactome)
hydroperoxy fatty acid MetaboliteCHEBI:64009 (ChEBI)
hydroxy fatty acid MetaboliteCHEBI:24654 (ChEBI)
lysophosphatidylcholine MetaboliteCHEBI:60479 (ChEBI)
oxidized phospholipids MetaboliteCHEBI:60156 (ChEBI)
poly(G) R-ALL-3221650 (Reactome)
poly(G) R-ALL-3221830 (Reactome)
poly(I) R-ALL-3221640 (Reactome)
poly(I) R-ALL-3221725 (Reactome)
porB ProteinP18195 (Uniprot-TrEMBL)
silicon dioxide nanoparticle MetaboliteCHEBI:50828 (ChEBI)
thioether crosslinked C53-AMBP(20-202) ProteinP02760 (Uniprot-TrEMBL)
titanium dioxide nanoparticle MetaboliteCHEBI:51050 (ChEBI)

Annotated Interactions

View all...
SourceTargetTypeDatabase referenceComment
4xPalmC-CD36R-HSA-2187264 (Reactome)
ALBArrowR-HSA-2168887 (Reactome)
AMBP(20-198)ArrowR-HSA-2203516 (Reactome)
AMBP(20-198)R-HSA-2168881 (Reactome)
AMBP(20-202)R-HSA-2168888 (Reactome)
Albumin:ferrihemeR-HSA-2168887 (Reactome)
Alpha1-Microglobulin:heme trimerArrowR-HSA-2168888 (Reactome)
ApohemoglobinArrowR-HSA-2168884 (Reactome)
CD163R-HSA-2168883 (Reactome)
COLEC11:LigandArrowR-HSA-2203480 (Reactome)
COLEC11:MASP1R-HSA-2203480 (Reactome)
COLEC12 trimerR-HSA-2187261 (Reactome)
COLEC12:LigandArrowR-HSA-2187261 (Reactome)
COLEC12:LigandArrowR-HSA-2981040 (Reactome)
COLEC12:LigandR-HSA-2981040 (Reactome)
Denatured Collagen I,III, Collagen IVR-HSA-3221843 (Reactome)
HPR:APOL1:APOA1:HDL3R-HSA-2168889 (Reactome)
HPX:ferriheme bArrowR-HSA-2168884 (Reactome)
HPX:ferriheme bArrowR-HSA-2168887 (Reactome)
HPX:heme bArrowR-HSA-2168886 (Reactome)
HPX:heme bR-HSA-2168897 (Reactome)
HPXR-HSA-2168884 (Reactome)
HPXR-HSA-2168886 (Reactome)
HPXR-HSA-2168887 (Reactome)
Haptoglobin DimerR-HSA-2168885 (Reactome)
Hemoglobin DimerR-HSA-2168885 (Reactome)
Hemoglobin DimerR-HSA-2168889 (Reactome)
Hemoglobin:HPR:APOL1:APOA1:HDL3ArrowR-HSA-2168889 (Reactome)
Hemoglobin:Haptoglobin:CD163ArrowR-HSA-2168883 (Reactome)
Hemoglobin:Haptoglobin:CD163ArrowR-HSA-2230938 (Reactome)
Hemoglobin:Haptoglobin:CD163R-HSA-2230938 (Reactome)
Hemoglobin:HaptoglobinArrowR-HSA-2168885 (Reactome)
Hemoglobin:HaptoglobinR-HSA-2168883 (Reactome)
IgA:Alpha-1-MicroglobulinR-HSA-2203516 (Reactome)
IgAArrowR-HSA-2203516 (Reactome)
LRP1:Hemopexin:hemeArrowR-HSA-2168897 (Reactome)
LRP1:Hemopexin:hemeArrowR-HSA-2230983 (Reactome)
LRP1:Hemopexin:hemeR-HSA-2230983 (Reactome)
LRP1R-HSA-2168897 (Reactome)
Ligands of CD36R-HSA-2187264 (Reactome)
Ligands of COLEC11R-HSA-2203480 (Reactome)
Ligands of COLEC12R-HSA-2187261 (Reactome)
Ligands of MARCOR-HSA-2173781 (Reactome)
Ligands of MSR1R-HSA-2173778 (Reactome)
Ligands of SCARA5R-HSA-2187266 (Reactome)
Ligands of SCARB1R-HSA-2197646 (Reactome)
Ligands of SCARF1R-HSA-2197645 (Reactome)
Ligands of STAB1R-HSA-2197770 (Reactome)
Ligands of STAB2R-HSA-2203479 (Reactome)
MARCO trimerR-HSA-2173781 (Reactome)
MARCO:LigandArrowR-HSA-2173781 (Reactome)
MARCO:LigandArrowR-HSA-2247510 (Reactome)
MARCO:LigandR-HSA-2247510 (Reactome)
MSR1 (SCARA1) trimerR-HSA-2173778 (Reactome)
MSR1 (SCARA1) trimerR-HSA-3221843 (Reactome)
MSR1:Collagen I,III,IVArrowR-HSA-3221843 (Reactome)
MSR1:LigandArrowR-HSA-2173778 (Reactome)
MSR1:LigandArrowR-HSA-2507854 (Reactome)
MSR1:LigandR-HSA-2507854 (Reactome)
MethemoglobinR-HSA-2168884 (Reactome)
Platelet

glycoprotein

IV:Ligand		ArrowR-HSA-2187264 (Reactome)
Platelet

glycoprotein

IV:Ligand		ArrowR-HSA-2247512 (Reactome)
Platelet

glycoprotein

IV:Ligand		R-HSA-2247512 (Reactome)
R-HSA-2168881 (Reactome) Truncated Alpha-1-Microglobulin binds heme b and then degrades heme b by an unknown mechanism (Allhorn et al. 2002). The crystal structure of the untruncated Alpha1-Microglobulin:heme complex indicates that each Alpha1-Microglobulin molecule binds 2 heme molecules and the Alpha1-Microglobulin molecules trimerize (Siebel et al. 2012).
R-HSA-2168883 (Reactome) The CD163 receptor binds the haptoglobin:hemoglobin complex (Kristiansen et al. 2001, Madsen et al. 2004, Nielsen et al. 2007). After binding, the CD163:haptoglobin:hemoglobin complex is internalized by endocytosis and is degraded in the lysosome. CD163 is found on the membranes of monocytes and macrophages.
R-HSA-2168884 (Reactome) When haptoglobin capacity to buffer hemoglobin is overwhelmed, hemoglobin undergoes a rapid conversion to methemoglobin. Ferriheme is transferred directly from methemoglobin to hemopexin (Miller et al. 1996, Mauk and Mauk 2010).
R-HSA-2168885 (Reactome) Haptoglobin is an acute phase protein. It is produced by the liver and secreted into the plasma where it binds alpha-beta dimers of hemoglobin (Hamaguchi et al. 1971, Nagel and Gibson 1971, Tsapis et al. 1978, reviewed in Chiabrando et al. 2011). Haptoglobin monomers contain alpha and beta chains cleaved from a single proprotein and bonded by cystine disulfide bonds. The monomers further associate into dimers by disulfide-bonding and beta strand swapping (Andersen et al. 2012). Each haptoglobin dimer can bind two hemoglobin dimers, each containing hemoglobin alpha and hemoglobin beta.
R-HSA-2168886 (Reactome) Hemopexin binds either ferriheme b or ferroheme b, however the stability of the complex containing ferriheme b is greater than the stability of the complex containing ferroheme b (Morgan 1976, Pasternack et al. 1983, Solar et al. 1989, Miller and Shaklai 1999, Rosell et al. 2005, Mauk and Mauk 2010).
R-HSA-2168887 (Reactome) Despite the lower affinity of ferriheme for albumin than for hemopexin, ferriheme initially associates with albumin, presumably because the molar concentration of albumin in plasma is considerably greater than that of hemopexin. Ferriheme is transferred directly from serum albumin to hemopexin (Morgan et al. 1976, Pasternack et al. 1983, Pasternack et al. 1985).
R-HSA-2168888 (Reactome) Alpha-1-Microglobulin binds heme b (Allhorn et al. 2002, Larsson et al. 2004). The crystal structure of the complex indicates that each microglobulin molecule binds 2 heme molecules and the microglobulin:heme complex trimerizes (Siebel et al. 2012).
R-HSA-2168889 (Reactome) Haptoglobin-related protein (HRP) is present in human serum in a complex known as trypanosome lytic factor-1 (TLF-1) that contains APOL1, APOA1, and HDL3. The HPR subunit of the complex binds hemoglobin with an unknown stoichiometry (Shiflett et al. 2005, Nielsen et al. 2006, Widener et al. 2007, Harrington et al. 2009).
R-HSA-2168897 (Reactome) Once formed in the plasma, the hemopexin:heme complex is rapidly cleared from circulation and it is taken up by the liver (Smith and Morgan 1984, Smith and Morgan 1985, Tolosano et al. 2010, Vinchi et al. 2008), where heme is degraded by heme oxygenases. In mouse, rat and rabbit several experimental evidences led to the postulation of a specific receptor on hepatocytes with high affinity for the hemopexin:heme complex (Smith and Morgan 1981, Smith and Morgan 1984, Smith et al, 1988, Smith et al., 1991), but such a receptor has not been identified to date. The only known hemopexin:heme receptor is LRP1 (CD91) that is ubiquitously expressed and has a low affinity for the complex. LRP1 is a multi-ligand scavenger receptor, involved in endocytosis in some cells types, for example macrophages, and in signaling in other cell types (reviewed in Boucher and Herz 2011). LRP1 is known to act in the metabolism of lipoprotein and it is expressed in several cell types including macrophages, hepatocytes and neurons. Among several ligands, LRP1 (CD91) can bind the hemopexin:heme complex (Hvidberg et al. 2005).
R-HSA-2173778 (Reactome) MSR1 (SCARA1, SR-A) binds oxidized and acetylated low density lipid (LDL) particles ((Brown et al. 1980), Haberland et al 1984, Gough et al. 1998, Yang et al. 2011), apolipoproteins A-I and E (human and mouse, Neyen et al. 2009), lysophosphatidylcholine from apoptotic cells (mouse, Sakai et al. 1996), phosphatidylinositol and phosphatidylserine (mouse, Nishikawa et al. 1990). MSR1 binds activated B-lymphocytes (human, Yokota et al. 1998), calreticulin and gp96 (mouse, Berwin et al. 2003). MSR1 binds bacterial products (E.coli, Neisseria meningitides, Staphylococcus aureus) (mouse, Peiser et al. 2006), Lipopolysaccharide (LPS) (mouse and bovine, Hampton et al. 1991), Lipoteichoic acid (LTA) and Gram-positive bacteria (bovine, Dunne et al. 1994), Adenovirus 5 (Haisma et al. 2009). MSR1 binds polysaccharides (carrageenan, dextran sulphate, fucoidan) (Brown et al. 1980, Krieger et al. 1992), extracellular matrix proteoglycans, biglycan and decorin (mouse, Santiago-Garcia et al. 2003). MSR1 binds extracellular matrix molecules, including denatured type I and III collagen, as well as glycated collagen IV (human and mouse and bovine, el Khoury et al. 1994, Gowen et al. 2000, Gowen et al. 2001), beta-amyloid fibrils (human and mouse, El Khoury et al. 1996), maleyl-BSA and advanced glycation end-product modified (AGE)-BSA (bovine, Brown et al. 1980, Araki et al. 1995). MSR1 binds polynucleotides (polyI, polyG) (bovine, Brown et al. 1980, Pearson et al. 1993, Mielewczyk et al. 1996), double-stranded RNA (Limmon et al. 2008, DeWitte-Orr et al. 2010). MSR1 interacts with the modified apoB-100 component of LDL (Parthasarathy et al. 1987) and with the lipid part of LDL (Terpstra et al. 1998). MSR1 is expressed most strongly on macrophages and can also be detected on endothelial cells and smooth muscle cells.
R-HSA-2173781 (Reactome) Unlike MSR1, MARCO uses the SRCR domain and more particularly the arginine-rich region within this domain for binding. (Brannstrom et al. 2002). MARCO binds lipopolysaccharide and lipoteichoic acid, both found on the surfaces of bacteria (Elomaa et al. 1998, Elshourbagy et al. 2000). MARCO binds and phagocytoses Streptococcus pneumoniae (mouse, Dorrington et al. 2013), Escherichia coli and Staphylococcus aureus (Elshourbagy, Li et al. 2000), Neisseria meningitidis (Mukhopadhyay et al. 2006), Clostridium sordellii (Thelen et al. 2010). MARCO binds proinflammatory oxidized lipids (mouse, Dahl et al. 2007). MARCO binds CpG oligonucleotide sequences (CpG-ODN) in microbial DNA (mouse, Jozefowski et al. 2006), uteroglobin-related protein 1 (Bin et al. 2003), unopsonized particles (TiO2, Fe2O3, and latex beads) (Palecanda et al. 1999) and silica particles (Hamilton et al. 2006). MARCO is most strongly expressed on subgroups of macrophages and can also be detected on splenic dendritic cells.
R-HSA-2187261 (Reactome) COLEC12 (SCARA4) binds beta-glucan (Jang et al. 2009), N-acetylgalactosamine (Yoshida et al. 2003), oxidized LDL (Ohtani et al. 2001), and double-stranded RNA (DeWitte-Orr et al. 2010). COLEC12 is expressed on endothelial cells
R-HSA-2187264 (Reactome) CD36 (Platelet glycoprotein IV) binds oxidized LDL (Janabi et al. 2000, Endemann et al. 1993) through both the lipid and the protein moieties of LDL (Boullier et al. 2000), oxidized phospholipids (Podrez et al. 2002), long-chain fatty acids (inferred from rat and mouse, Abumrad et al. 1993, Laugerette et al. 2005), hexarelin (a hexapeptide member of the growth hormone-releasing peptide family) (inferred from rat and mouse, Bodart et al. 2002), betaglucan (Means et al. 2009), oxidized and native phosphatidylserine (Greenberg et al. 2006) and apoptotic cells (Ren et al. 1995; Fadok et al. 1998), lipopeptide from Staphylococcus aureus as well as lipoteichoic acid from Gram-positive bacteria, both in cooperation with TLR2 (inferred from mouse, Hoebe et al. 2005). As inferred from mouse, CD36 also binds phosphatidylinositol, and HDL.
R-HSA-2187266 (Reactome) SCARA5 binds double-stranded RNA (DeWitte-Orr et al. 2010). As inferred from mouse SCARA5 also binds lipopolysaccharide and ferritin. SCARA5 is expressed on epithelial cells.
R-HSA-2197645 (Reactome) SCARF1 (SREC-I) binds low density lipoprotein (LDL), oxidized LDL, acetylated LDL (Adachi et al. 1997), carbamylated LDL (Apostolov et al. 2009), beta glucan (Means et al. 2009), and calreticulin (Berwin et al. 2004). SREC-I binds Hsp90 and Hsp90-chaperoned peptides (Murshid et al. 2010) as well as Heat shock protein 110 (hsp110) and glucose-regulated protein (grp170) (inferred from mouse, Facciponte, Wang et al. 2007). SREC-I interacts with PorB of Neisseria gonorrhoeae and mediates host cell entry (Rechner et al. 2007).
R-HSA-2197646 (Reactome) SCARB1 (SR-BI) binds low density lipoprotein (LDL), acetylated LDL, oxidized LDL, high density lipoprotein (HDL) (Calvo et al. 1997, Murao et al. 1997, Rhainds et al. 1999, inferred from hamster in Acton et al. 1994). SCARB1 binds HDL via its protein moiety, including apolipoproteins A-I, A-II, CII, CIII and E (Bultel-Brienne et al. 2002, inferred from mouse in Xu, Laccotripe et al. 1997, Li et al. 2002). SCARB1 also binds serum amyloid A protein (Baranova et al. 2005), and lipopolysaccharide (LPS) (Vishnyakova et al. 2003). SCARB1 is expressed on the extracellular face of the plasma membrane of several types of polarized epithelial cells.
R-HSA-2197770 (Reactome) STAB1 (FEEL-1) binds acetylated low density lipoprotein (LDL) (Adachi & Tsujimoto 2002, Palani et al. 2011), phosphatidylserine (exposed when cells are lysed) (Park et al. 2009), advanced glycation end products (AGE) (Tamura et al. 2003, Hansen et al. 2005), and Osteonectin (SPARC) (Kzhyshkowska et al. 2006).
R-HSA-2203479 (Reactome) STAB2 (FEEL-2) binds acetylated low density lipoprotein (LDL) (Adachi & Tsujimoto 2002, Harris & Weigel 2008), advanced glycation end products (AGE) (Tamura et al. 2003), chondroitin sulfate (Harris & Weigel 2008), hyaluronic acid (Zhou et al. 2003, Harris et al. 2004, Harris et al. 2007, Harris & Weigel 2008), heparin (Harris et al. 2008, Harris & Weigel 2008, Harris et al. 2009), and phosphatidylserne (Park et al. 2008).
R-HSA-2203480 (Reactome) COLEC11 (CL-K1) binds D-mannose, L-fucose, N-acetylglucosamine, DNA, lipopolysaccharide (LPS), and lipoteichoic acid (LTA) (Keshi et al. 2006, Hansen et al. 2010).
R-HSA-2203516 (Reactome) Both hemoglobin and the cytosolic face of erythrocytes are able to catalyze the cleavage of Alpha-1-Microglobulin in the IgA:Alpha-1-Microglobulin complex present in serum (Allhorn et al. 2002). The reaction produces truncated Alpha-1-Microglobulin, which is able to bind and degrade heme. About half of the circulating Alpha-1-Microglobulin is covalently bound to IgA.
R-HSA-2230938 (Reactome) The CD163:haptoglobin:hemoglobin complex is endocytosed (Schaer et al. 2006, Kristiansen et al. 2001) by monocytes or macrophages. CD163 is constitutively endocytosed by monocytes independently of ligand binding (Schaer et al. 2006). Upon endocytosis, the receptor–ligand complex enters early endosomes where haptoglobin:hemoglobin complexes are released from CD163. The receptor then recycles to the cell surface while haptoglobin:hemoglobin complexes continue through the endocytic pathway to end up in lysosomes where the protein moieties and the ligand are degraded.
R-HSA-2230983 (Reactome) The LRP1:hemopexin:heme complex is endocytosed and the complex is dissociated in lysosomes, leading to heme uptake. Heme is then degraded by heme oxygenases. Whereas LRP1 is subsequently recycled to the plasma membrane, the destiny of hemopexin is controversial. Some studies have suggested that hemopexin can be recycled as an intact molecule to the extracellular milieu (Smith and Morgan, 1979). However, it has also been proposed that following hepatic uptake of heme from hemopexin:heme, varying proportions of the protein are either returned to the circulation or degraded in the liver (Potter et al., 1993). Recently, Hvidberg et al. have shown that most hemopexin is degraded in lysosomes (Hvidberg et al., 2005).
R-HSA-2247510 (Reactome) The MARCO:ligand complex is endocytosed (Arredouani et al. 2005, Thelen et al. 2010). In cases where the ligand is part of a bacterial cell the entire cell is phagocytosed.
R-HSA-2247511 (Reactome) The STAB2:ligand complex is endocytosed (Tamura et al. 2003, Li et al. 2011). Endocytosis of stabilin-1 or stabilin-2 can occur independently of ligand binding, via clathrin (Hansen et al. 2005).
R-HSA-2247512 (Reactome) The Platelet glycoprotein IV (CD36):ligand complex is endocytosed (Zeng et al. 2003, McDermott_Roe et al. 2008, Nilsen et al. 2008, Collins et al. 2009). The endocytosis of CD36:oxidized LDL is independent of caveolin (Zeng et al. 2003) and dependent on actin (Collins et al. 2009). As inferred from mouse, endocytosis of CD36:oxidized LDL is independent of caveolae, microtubules, and actin cytoskeleton, but dependent on dynamin (Sun et al. 2007).
R-HSA-2247513 (Reactome) The STAB1:ligand complex is endocytosed (Tamura et al. 2003, Kzhyshkowska et al. 2004, Li et al. 2011, Prevo et al. 2004; Kzhyshkowska et al. 2005). Endocytosis of stabilin-1 or stabilin-2 can occur independently of ligand binding, via clathrin (Hansen et al. 2005).
R-HSA-2247514 (Reactome) The SCARF1:ligand complex is endocytosed (Adachi et al. 1997, Berwin et al. 2004) and cross-presented on MHC class II (Murshid et al. 2010). SREC-I mediates host cell entry of Neisseria gonorrhoeae (Rechner et al. 2007)
R-HSA-2299677 (Reactome) As inferred from mouse, the SCARA5:ligand complex is endocytosed.
R-HSA-2507854 (Reactome) The MSR1:ligand complex (SCARA1:ligand, SR-A:ligand) is endocytosed (Matsumoto et al. 1990, Gough et al. 1998, Peiser et al. 2000, Aguilar-Gaytan and Mas-Oliva 2003, Wang and Chandawarkar 2010, Orr et al. 2011). In the cases in which the ligands are located on bacteria or yeast cells the entire cell is phagocytosed (Aguilar-Gaytan and Mas-Oliva 2003, Wang and Chandawarkar 2010). Uptake of modified LDL by macrophages via MSR1 appears to contribute to foam cell formation during atherosclerosis (Matsumoto et al. 1990).
R-HSA-2512800 (Reactome) The SCARB1 (SR-BI, SR-BII):ligand complex is endocytosed (Calvo et al. 1997, Murao et al. 1997, Rhainds et al. 1999, Vishnyakova et al. 2003, Baranova et al. 2005, Eckhardt et al. 2004) but selective lipid uptake from lipoprotein particles does not require SR-BI endocytosis in mouse (Nieland et al. 2005) but is partly dependent on endocytosis in human (Zhang et al. 2007). HDL particles are resecreted after lipid unloading in the endocytic pathway (Pagler et al. 2006; Zhang et al. 2007). SR-BI colocalizes with caveolae (inferred from mouse, Babitt et al. 1997) while SR-BII, an alternatively spliced form of SCARB1, localizes to clathrin-coated pits due to a dileucine motif in the cytosolic tail (inferred from mouse, Eckhardt et al. 2006). Endocytosis of oxidized LDL by SR-BI is independent of caveolae, microtubules, and actin cytoskeleton (inferred from mouse, Sun et al. 2007).
R-HSA-2981040 (Reactome) COLEC12 (CL-P1, SCARA4, SRCL, NSR2) bound to yeast or bacteria is phagocytosed (Jang et al. 2009, Ohtani et al. 2012). Endocytosis of other ligands bound to COLEC12 is inferred.
R-HSA-3221843 (Reactome) As inferred from mouse, MSR1 (SCARA1) binds denatured collagen I, denatured collagen III, and nondenatured or glycated collagen IV.
SCARA5 trimerR-HSA-2187266 (Reactome)
SCARA5:LigandArrowR-HSA-2187266 (Reactome)
SCARA5:LigandArrowR-HSA-2299677 (Reactome)
SCARA5:LigandR-HSA-2299677 (Reactome)
SCARB1-2R-HSA-2197646 (Reactome)
SCARB1:Endocytosed LigandArrowR-HSA-2512800 (Reactome)
SCARB1:Endocytosed LigandR-HSA-2512800 (Reactome)
SCARB1:LigandArrowR-HSA-2197646 (Reactome)
SCARF1:LigandArrowR-HSA-2197645 (Reactome)
SCARF1:LigandArrowR-HSA-2247514 (Reactome)
SCARF1:LigandR-HSA-2247514 (Reactome)
SCARF1R-HSA-2197645 (Reactome)
STAB1:LigandArrowR-HSA-2197770 (Reactome)
STAB1:LigandArrowR-HSA-2247513 (Reactome)
STAB1:LigandR-HSA-2247513 (Reactome)
STAB1R-HSA-2197770 (Reactome)
STAB2(1136-2551)R-HSA-2203479 (Reactome)
STAB2:LigandArrowR-HSA-2203479 (Reactome)
STAB2:LigandArrowR-HSA-2247511 (Reactome)
STAB2:LigandR-HSA-2247511 (Reactome)
Truncated Alpha1-Microglobulin:heme trimerArrowR-HSA-2168881 (Reactome)
heme bR-HSA-2168881 (Reactome)
heme bR-HSA-2168886 (Reactome)
heme bR-HSA-2168888 (Reactome)
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