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

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20, 33, 82, 101, 14023, 59, 72, 81, 92...109, 14847, 54, 85, 87, 89...86, 91, 114, 14875, 13539, 127, 1437, 13, 14, 25, 29...39, 49, 56, 68, 143...19, 58, 1198631, 39, 41, 127, 136...11, 17, 36, 49, 50, 70...74, 97, 108, 1291, 4, 15, 16, 22...43, 61, 65, 123, 124, 15940, 62, 80, 113, 138...53, 75, 13535, 62, 798, 34, 52, 71, 104...80, 9944, 55, 88, 1066, 9, 18, 38, 60...44, 55, 88, 89, 95...7527, 45, 119121, 13710, 21, 64, 134, 146105, 15251, 92, 1181, 3, 15, 16, 21...COLEC11 Trimer HemoglobinHPRAPOL1APOA1HDL3 COLEC11 Oligomer oxidized LDL spherical HDL LDL Tropocollagen type IV alpha-1X2 alpha-2 IgA COLEC12Ligand COLEC12 trimer Ligands of STAB1 Oxyhemoglobin Dimer Ligands of SCARF1 Hemoglobin betaferroheme boxygen Hemoglobin Dimer Alpha1-Microglobulinheme trimer COLEC12Ligand Ig Lamda Light Chain V Region Hemoglobin Dimer HemoglobinHaptoglobinCD163 STAB2Ligand MARCOLigand Ligands of MARCO Ligands of STAB2 Ig alpha C region acetylated LDL AGE adducts AGE adducts Hemoglobin alphaferroheme b AGE adductsPeptide HPR Dimer Deoxyhemoglobin Dimer Ig Antibody Light Chain SCARA5Ligand Hemoglobin betaferroheme b COLEC11 Trimer Hemoglobin Dimer Ig Lamda Light Chain V Region heme b SCARF1Ligand Ig Antibody Light Chain SCARA5 trimer AGE adducts Hemoglobin Dimer Alpha1-Microglobulinheme SCARB1Endocytosed Ligand MARCO trimer Hemoglobin alphaferroheme b Deoxyhemoglobin Dimer SCARF1Ligand MSR1 Haptoglobin Dimer SCARB1Endocytosed Ligand HemoglobinHaptoglobin Collagen alpha-1acetylated LDL Collagen alpha-1Oxyhemoglobin Dimer Ligands of COLEC12 STAB2Ligand acetylated LDL acetylated LDL Hemoglobin betaferroheme b Endocytosed Ligands of SCARB1 Ligands of MARCO oxidized LDL Deoxyhemoglobin Dimer HemoglobinHaptoglobin oxidized LDL Tropocollagen type I Ligands of STAB1 oxidized LDL AGE adducts AGE adductsPeptide MSR1 SCARA5 trimer IgA LRP1Hemopexinheme Ig Lambda C region Immunoglobulin Lambda Light Chain Tropocollagen type I Collagen alpha-2oxidized LDL MARCO trimer Collagen alpha-1MSR1 oxidized LDL Haptoglobin Truncated Alpha1-Microglobulinheme trimer acetylated LDL LDL AGE adducts oxidized LDL Ligands of STAB2 STAB1Ligand Methemoglobin AGE adductsPeptide STAB1Ligand COLEC11MASP1 acetylated LDL Ligands of CD36 endocytic vesiclespherical HDL AGE adductsPeptide Immunoglobulin Lambda Light Chain MSR1 oxidized LDL COLEC11Ligand AGE adductsPeptide AGE adducts Haptoglobin IgA Heavy Chain Ligands of COLEC12 HemoglobinHaptoglobin acetylated LDL LDL Hemoglobin alphaferriheme b Hemoglobin alphaferroheme boxygen Denatured Collagen I,III, Collagen IV HPR Dimer acetylated LDL COLEC11 Oligomer Platelet glycoprotein IVLigand Tropocollagen type IV alpha-1X2 alpha-2 Hemoglobin betaferroheme b spherical HDL Tropocollagen type III Tropocollagen type III Oxyhemoglobin Dimer HPXheme b cytosoloxidized LDL HPXferriheme b acetylated LDL SCARA5Ligand MSR1Ligand Platelet glycoprotein IVLigand HemoglobinHaptoglobinCD163 oxidized LDL Ig alpha C region MARCOLigand Ig Heavy Chain V Region LRP1Hemopexinheme Ligands of COLEC11 Hemoglobin alphaferroheme b Hemoglobin alphaferroheme boxygen Hemoglobin alphaferroheme boxygen oxidized LDL Ligands of SCARF1 Hemoglobin betaferroheme boxygen Ig Kappa Light Chain V Region Hemoglobin alphaferroheme b HPRAPOL1APOA1HDL3 Oxyhemoglobin Dimer Haptoglobin Deoxyhemoglobin Dimer Apohemoglobin Ligands of STAB1 Albuminferriheme Hemoglobin betaferroheme boxygen Hemoglobin alphaferroheme boxygen Collagen alpha-2Haptoglobin Ligands of CD36 Ig Lambda C region Ligands of SCARA5 Hemoglobin betaferroheme b Truncated Alpha1-Microglobulinheme AGE adductsPeptide Tropocollagen type IV alpha-1X3 Ligands of CD36 IgA Heavy Chain AGE adductsPeptide COLEC11MASP1 Ligands of SCARA5 LDL Endocytosed Ligands of SCARB1 Hemoglobin betaferroheme b Ligands of SCARB1 acetylated LDL Hemoglobin Dimer Denatured Collagen I,III, Collagen IV Ferritin Complex Chains Ig Kappa Light Chain V Region Hemoglobin betaferriheme b oxidized LDL acetylated LDL Hemoglobin alphaferroheme boxygen Ligands of SCARB1 Oxyhemoglobin Dimer Tropocollagen type IV alpha-1X3 COLEC12 trimer SCARA5 trimer Ligands of MSR1 HPXheme b Collagen alpha-1Haptoglobin Dimer AGE adducts MARCO trimer Ferritin SCARB1Ligand HPRAPOL1APOA1HDL3 ferriheme b or ferroheme b Hemoglobin betaferroheme boxygen oxidized LDL spherical HDL Haptoglobin Dimer IgAAlpha-1-Microglobulin MSR1Ligand Haptoglobin Dimer Deoxyhemoglobin Dimer Ferritin Complex Chains Hemoglobin betaferroheme boxygen Immunoglobulin Kappa Light Chain Ferritin COLEC12 trimer spherical HDL Hemoglobin alphaferroheme b Immunoglobulin Kappa Light Chain acetylated LDL HPXheme b acetylated LDL Ligands of MSR1 heme b MSR1Collagen I,III,IV Ig Heavy Chain V Region Man Ig kappa chain V-I region WEA Ig heavy chain V-III region BRO IGKVA18Ig kappa chain V-I region HK101 10xdHF-10xglutamyl semialdehyde Phosphatidylserine IGLV1-36Ig heavy chain V-III region KOL LRP1 Ig kappa chain V-I region OU phosphatidylinositol CALR Ig kappa chain V-I region Gal Ig kappa chain V-II region MIL 3x4Hyp-GalHyl-COL3A1 5xHC-HPCALR Phosphatidylserine Ig kappa chain V-I region Rei Ig kappa chain V-I region BAN Ig kappa chain V-III region IARC/BL41 5Hyl-COL1A2 NECML HBA1 Ig heavy chain V-I region SIE Ig heavy chain V-III region NIE carrageenan Phosphatidylserine phosphatidylinositol Ligands of CD36hydroxy fatty acid IGLC1GalHyl-COL1A2 Ig kappa chain V-III region NG9 Ig kappa chain V-III region HIC titanium dioxide nanoparticle STAB1Ig kappa chain V-IV region B17 Ig kappa chain V-I region DEE APOE Lipoteichoic acid IGKCIGLV3-12CHEST 6xHC-MARCO 7-ketocholesterol N-epsilon-COLEC11 Ig heavy chain V-III region GA PL IGLV1-40Ig kappa chain V-III region HAH 3x4Hyp-3Hyp-COL3A1 Ig heavy chain V-III region TIL AMBP7-ketocholesterol LPS ferriheme b GlcGalHyl-COL1A2 Lipoteichoic acid MSR1Collagen I,III,IVIg kappa chain V-I region Kue IGLV3-12ferroheme b 3x4Hyp-3Hyp-GlcGalHyl-COL3A1 Peptide Ig lambda chain V-IV region Hil lysophosphatidylcholine ferriheme b AcK-APOBIGLC3cholesterol esters 10xdHF-10xglutamyl semialdehyde COL3A1 Ig heavy chain V-III region WEA PL Ig kappa chain V-I region Lay STAB1 IGLV2-23Truncated Alpha1-Microglobulinheme trimerIGLV10-54TAGs MARCO trimercholesterol esters Peptide PL 4xPalmC-CD36 Ig heavy chain V-III region LAY Ig heavy chain V-III region DOB 7-ketocholesterol 3x4Hyp-GalHyl-COL1A2 lysophosphatidylcholine Ig heavy chain V-II region NEWM Ig kappa chain V-IV region JI HYOU1 Ig lambda chain V-II region NIG-84 Ig kappa chain V-I region Bi IGHVIg kappa chain V-I region Walker hydroperoxy fatty acid SAA1ferriheme b 3x4Hyp-GlcGalHyl-COL1A1 cholesterol Ig kappa chain V-I region Roy 3x4Hyp-3Hyp-COL1A2 IgAAlpha-1-MicroglobulinIg lambda chain V-II region MGC IGLC2AcK-APOBIGLV1-44Ig heavy chain V-III region TEI 3x4Hyp-3Hyp-GlcGalHyl-COL1A1 Ig heavy chain V-III region KOL IGLC6CHEST IGLC7COLEC12LigandMARCOLigandIGKV1-5Phosphatidylserine Ig lambda chain V-V region DEL porB IGLC2N-epsilon-10xdHF-10xglutamyl semialdehyde Ligands of MSR1Ig kappa chain V-IV region STH 7xHC-HPIg heavy chain V-I region HG3 TAGs Ig lambda chain V-III region LOI MSR1LigandIg kappa chain V region EV15 TAGs Ig kappa chain V-IV region B17 5Hyl-COL3A1 Ig heavy chain V-III region ZAP Ig heavy chain V-III region NIE hydroperoxy fatty acid ApohemoglobinAPOA1Ig heavy chain V-III region CAM N-epsilon-Ligands of MARCOIg kappa chain V-III region HAH hydroxy fatty acid SPARC MARCOLigandIg heavy chain V-II region MCE Ig lambda chain V-II region BUR IGLV4-60N-epsilon-Ig lambda chain V-IV region Kern hydroxy fatty acid LPS Ig lambda chain V-III region SH COLEC12 LPS Ig heavy chain V-III region WEA COLEC11 Ig heavy chain V-II region ARH-77 HBB hydroxy fatty acid GlcNAc Ig kappa chain V-I region Daudi SCGB3A2 3x4Hyp-3Hyp-5Hyl-COL1A1 IGLC6Ig lambda chain V-IV region Hil 3x4Hyp-COL1A1 TAGs 3x4Hyp-3Hyp-COL3A1 hydroxy fatty acid PL Ig lambda chain V-I region NIG-64 Ig lambda chain V-IV region Bau SCARB1-2 IGLV3-16HUA Ig kappa chain V-I region Ni SCARB1Endocytosed LigandO2 APOBAMBPAPOBIg heavy chain V-II region MCE O2 Ig lambda chain V-II region TRO 3x4Hyp-3Hyp-GlcGalHyl-COL1A1 Ig heavy chain V-I region ND Ig lambda chain V-V region DEL 3x4Hyp-3Hyp-5Hyl-COL3A1 Ig lambda chain V-II region NIG-84 STAB2Ligand3x4Hyp-COL1A2 3x4Hyp-GalHyl-COL1A1 HBA1 Ligands of SCARB1FTL Ig heavy chain V-III region WAS TAGs oxidized phospholipids CHOL HBA1 10xdHF-10xglutamyl semialdehyde HPXheme bIg kappa chain V region EV15 IGLV7-4610xdHF-10xglutamyl semialdehyde 6xHC-MARCO Ig heavy chain V-III region BUR Ig heavy chain V-III region POM ferroheme b IGLV1-44Ig kappa chain V-I region WEA Ig kappa chain V-I region Mev IGLC3Ig kappa chain V-I region OU CHEST Ig heavy chain V-I region Mot phosphatidylinositol APOBSPARC Ig lambda chain V-VI region AR silicon dioxide nanoparticle 3x4Hyp-GlcGalHyl-COL1A2 Ig heavy chain V-III region ZAP HSP90AA1 TAGs SCARA5Ligandhydroxy fatty acid LPS Ig kappa chain V-I region Rei IGLV5-45TAGs 7-ketocholesterol SCARB1-2Phosphatidylserine PL lysophosphatidylcholine Ig kappa chain V-II region RPMI 6410 COLEC12 IGHVIGLV4-3APOA1STAB1LigandIg kappa chain V-III region CLL IGLV2-23Ig lambda chain V-I region MEM 3x4Hyp-GalHyl-COL1A2 Ig kappa chain V-II region MIL Ig kappa chain V-I region Scw 3x4Hyp-3Hyp-5Hyl-COL1A2 cholesterol Ig lambda chain V-VI region AR Ig lambda chain V-II region WIN IGLV8-61Ig kappa chain V-III region Ti Ig heavy chain V-III region GA AcK-APOBGalHyl-COL3A1 LRP1 Ig kappa chain V-II region TEW TAGs 10xdHF-10xglutamyl semialdehyde 3x4Hyp-COL3A1 5xHC-HPGlcGalHyl-COL1A1 NECML SCARA5 trimercholesterol Ig heavy chain V-II region COR IgA3x4Hyp-GlcGalHyl-COL1A1 Ig kappa chain V-III region SIE HBA1 hydroxy fatty acid thioether crosslinked residues-AMBPLPS COL3A1 HBB SCARF1LigandIg heavy chain V-II region ARH-77 3x4Hyp-COL1A2 Ig kappa chain V-III region B6 3x4Hyp-5Hyl-COL3A1 3x4Hyp-3Hyp-COL1A2 ferroheme b Ig heavy chain V-III region CAM PL Ig heavy chain V-II region DAW 10xdHF-10xglutamyl semialdehyde Ig lambda chain V-IV region X 1,3-beta-D-glucan CHOL HemoglobinHaptoglobinHBA1 IGLV4-60Ig heavy chain V-III region TIL lysophosphatidylcholine 3x4Hyp-3Hyp-GalHyl-COL3A1 3x4Hyp-COL1A1 Ig heavy chain V-II region OU IGLVIg kappa chain V-III region NG9 carrageenan IGLV3-25Ig kappa chain V-I region Lay 3x4Hyp-GlcGalHyl-COL1A2 IGLV5-37HYOU1 PL Ig lambda chain V-III region SH Ig lambda chain V-VI region EB4 10xdHF-10xglutamyl semialdehyde 7xHC-HPIg heavy chain V-III region LAY HBB Hemoglobin DimerHeparins HBB IGHA1Ig kappa chain V-IV region STH Ig lambda chain V-IV region X 3x4Hyp-3Hyp-5Hyl-COL1A1 Ig heavy chain V-I region Mot 3x4Hyp-3Hyp-5Hyl-COL3A1 Ig kappa chain V-II region GM607 Phosphatidylserine Ig lambda chain V-II region VIL GalNAc Ig lambda chain V-II region NIG-58 5xHC-HPIg heavy chain V-II region WAH 7-ketocholesterol Ig kappa chain V-I region CAR 7xHC-HPIGKV4-1HSP90B1 APOE Ig heavy chain V-III region BUR IGLV2-18cholesterol esters Ig lambda chain V-I region EPS Ig heavy chain V-III region BUT Ig kappa chain V-II region FR Ig heavy chain V-III region TRO Ig kappa chain V-II region RPMI 6410 heme b 1,3-beta-D-glucan Ig lambda chain V-VI region NIG-48 CALR Ig kappa chain V-III region VH APOB3x4Hyp-3Hyp-GlcGalHyl-COL3A1 IGKV4-1IGHA2COL1A2 TAGs LCFAs Ig heavy chain V-III region TUR 7-ketocholesterol ferroheme b IGKCIg kappa chain V-I region Daudi CHOL Platelet glycoprotein IVLigandIGHV7-81PL hydroxy fatty acid IGLV3-16CHEST IGHA2LPS APOA1CHEST Ig lambda chain V-I region WAH APOL1 Ig kappa chain V-III region WOL FTH1Ligands of COLEC12Ig kappa chain V-III region WOL Ig heavy chain V-I region ND Ig heavy chain V-I region WOL AcK-APOB10xdHF-10xglutamyl semialdehyde GalHyl-COL1A1 IGKV1-5Ig lambda chain V-II region TOG Ig kappa chain V-II region TEW AcK-APOBCHEST 3x4Hyp-3Hyp-GalHyl-COL3A1 Ig kappa chain V-III region VG CHEST Ig heavy chain V-II region SESS hydroxy fatty acid AcK-APOBIg kappa chain V-I region Roy oxidized phospholipids Ig heavy chain V-III region BUT Ig kappa chain V-III region POM 7-ketocholesterol Ig lambda chain V-I region NEWM IGLV5-45Ig kappa chain V-I region EU CHEST SCARF1LigandIGLV3-22CHOL dextran sulfate COLEC12 trimerIGLV4-69AcK-APOBHemoglobinHaptoglobinCD163Phosphatidylserine CALR Ig kappa chain V-III region CLL Ig lambda chain V-II region BOH Fe3+ 6xHC-MSR1 Ig heavy chain V-III region WAS SCARA5LigandLRP1HemopexinhemeAlbuminferriheme3x4Hyp-COL3A1 3x4Hyp-3Hyp-GalHyl-COL1A2 SCARF1 3x4Hyp-5Hyl-COL1A1 COLEC12 lysophosphatidylcholine O2 3x4Hyp-3Hyp-COL1A1 1,3-beta-D-glucan AcK-APOBPlatelet glycoprotein IVLigandIg heavy chain V-II region HE PL LRP1HemopexinhemeSCARF1 Ig lambda chain V-II region NEI Ig lambda chain V-VI region SUT SCARB1LigandCHOL 3x4Hyp-5Hyl-COL3A1 O2 LPS HBA1 AcK-APOBCOLEC11MASP13x4Hyp-GlcGalHyl-COL3A1 IGLC71,3-beta-D-glucan Ig lambda chain V-VI region NIG-48 CD163 GalHyl-COL3A1 Ig lambda chain V-I region HA Phosphatidylserine Ig kappa chain V-III region GOL Ligands of SCARA5PL 3x4Hyp-GlcGalHyl-COL3A1 TAGs SCARA5 lysophosphatidylcholine Ig kappa chain V-I region AG 3x4Hyp-5Hyl-COL1A1 NECML 5Hyl-COL1A2 TAGs Ig lambda chain V-II region NIG-58 Ig kappa chain V-I region WAT HPXCOL4A2SAA1cholesterol Lipoteichoic acid IGLV2-18Ig kappa chain V-II region FR 10xdHF-10xglutamyl semialdehyde Ig lambda chain V-VI region WLT CHOL GlcGalHyl-COL1A2 Ig heavy chain V-III region BRO 5Hyl-COL1A1 Ig lambda chain V-VI region EB4 PL Ligands of SCARF1O2 cholesterol hydroperoxy fatty acid CHOL Peptide ALBHeparins Ig kappa chain V-I region AG APOBIg lambda chain V-II region VIL Ig kappa chain V-I region AU HPX heme b MethemoglobinHSPH1 APOA15Hyl-COL3A1 cholesterol esters IGLV3-27Ig heavy chain V-II region NEWM Ig kappa chain V-I region EU HPR IGLV2-33CHOL 3x4Hyp-3Hyp-GlcGalHyl-COL1A2 hematite nanoparticle STAB1 SCARA5 LCFAs IGLV4-3APOA1STAB21,3-beta-D-glucan SCARA5 HBB 7xHC-HPtitanium dioxide nanoparticle STAB2LigandIg heavy chain V-I region EU Ig heavy chain V-III region GAL Ig heavy chain V-I region HG3 5,6beta-epoxy-cholesterol IgH heavy chain V-III region VH26 precursor Ig lambda chain V region 4A Ig kappa chain V-III region Ti 6xHC-MSR1 APOA1Ig heavy chain V-II region COR Ig lambda chain V-II region MGC GlcGalHyl-COL3A1Ig kappa chain V-I region Wes 10xdHF-10xglutamyl semialdehyde hydroxy fatty acid COL4A1GlcGalHyl-COL3A1Ig lambda chain V-I region NEW lysophosphatidylcholine Haptoglobin DimerIg heavy chain V-III region JON Ig kappa chain V-I region Hau Ig heavy chain V-I region SIE cholesterol esters 3x4Hyp-GalHyl-COL3A1 TAGs CHS 1,3-beta-D-glucan Ig lambda chain V-I region NIG-64 dextran sulfate CHEST Ig heavy chain V-III region DOB GalHyl-COL1A1 7-ketocholesterol PL hydroperoxy fatty acid Ig lambda chain V-IV region MOL Ig heavy chain V-II region DAW PL hydroperoxy fatty acid Lipoteichoic acid ferroheme b Peptide AMBPIg lambda chain V-I region EPS IGLV3-22lysophosphatidylcholine PL Ig kappa chain V-IV region JI IGLV7-43Fe3+ Ig kappa chain V-III region IARC/BL41 HPX AcK-APOBSCGB3A2 5,6beta-epoxy-cholesterol 5xHC-HPlysophosphatidylcholine Ig kappa chain V-I region Walker oxidized phospholipids hydroperoxy fatty acid HBB N-epsilon-lysophosphatidylcholine HPR Ig lambda chain V-II region WIN Ig lambda chain V-I region MEM GalNAc Ig kappa chain V-II region Cum NECML Ig lambda chain V-I region NEW N-epsilon-Ig lambda chain V-I region WAH CHOL COL1A2 3x4Hyp-5Hyl-COL1A2 FTH1TAGs HPRAPOL1APOA1HDL3Phosphatidylserine Ig lambda chain V-II region BO Ig lambda chain V-III region LOI Ig kappa chain V-I region AU ALB 3x4Hyp-3Hyp-5Hyl-COL1A2 Phosphatidylserine Ig lambda chain V-VII region MOT 3x4Hyp-3Hyp-GalHyl-COL1A1 Ig lambda chain V-VI region SUT TAGs Ig lambda chain V-I region NEWM Ig kappa chain V-I region WAT IGLV1-364xPalmC-CD36CHOL Denatured Collagen I,III, Collagen IVcholesterol CHOL IGLVIg kappa chain V-I region Gal CHOL AcK-APOB3x4Hyp-3Hyp-COL1A1 IGLV2-337-ketocholesterol 3x4Hyp-3Hyp-GalHyl-COL1A2 cholesterol phosphatidylinositol HBB IGLV11-55hydroperoxy fatty acid IGLV5-37lysophosphatidylcholine LPS Ig kappa chain V-I region Ka CD163 L-fucose Ig kappa chain V-III region POM silicon dioxide nanoparticle COLEC12Ligandhydroperoxy fatty acid ferroheme b PL Ig lambda chain V-IV region Bau 10xdHF-10xglutamyl semialdehyde 7-ketocholesterol Lipoteichoic acid Ig lambda chain V-IV region Kern hydroxy fatty acid hydroperoxy fatty acid Ig kappa chain V-III region VG Ig heavy chain V-I region WOL CHOL Ig kappa chain V-I region BAN Ig kappa chain V-I region Wes Ig kappa chain V-I region Hau MSR1 phosphatidylinositol Ig kappa chain V-I region Bi Ig lambda chain V-I region VOR SCARF1Ig lambda chain V-I region HA IGLV2-113x4Hyp-3Hyp-GlcGalHyl-COL1A2 Ig heavy chain V-III region HIL LRP1SCARB1Endocytosed Ligandferriheme b AcK-APOBAcK-APOBNECML Ig kappa chain V-II region Cum GlcGalHyl-COL1A1 Ig kappa chain V-III region GOL HSP90B1 COLEC11LigandTAGs CHEST ferriheme b Ig kappa chain V-I region HK101 Ig lambda chain V-II region BUR Ig heavy chain V-II region SESS CHEST SCARB1-2 Ig kappa chain V-IV region Len Alpha1-Microglobulinheme trimerhydroxy fatty acid hydroperoxy fatty acid HPX Ig heavy chain V-III region TRO 3x4Hyp-3Hyp-GalHyl-COL1A1 IGLV8-61Peptide NECML MSR1LigandLCFAs Ig lambda chain V-II region NEI heme bHUA HPXferriheme bHSPH1 3x4Hyp-5Hyl-COL1A2 COL4A2Lipoteichoic acid IGLV4-695Hyl-COL1A1 STAB1Ligand6xHC-MSR1 HemoglobinHaptoglobinCD163Ig heavy chain V-II region HE GalHyl-COL1A2 ferroheme b PL SAA1ferriheme b CHEST Ig heavy chain V-III region TUR 1,3-beta-D-glucan STAB2PL IGLV3-25Ig lambda chain V-IV region MOL CHS Ig kappa chain V-I region CAR 7-ketocholesterol Peptide Ig lambda chain V-II region TOG Ig lambda chain V-II region BOH PL TAGs HPX CD163COL1A1 IGHA1AMBPTAGs LPS IGLV10-547-ketocholesterol Ligands of COLEC11IGLV7-467-ketocholesterol LPS heme b6xHC-MSR1 FTL Ig kappa chain V-I region Mev Lipoteichoic acid Ig kappa chain V-IV region Len Ig lambda chain V region 4A APOA1MASP1HSP90AA1 Ig kappa chain V-III region VH SCARB1-2 TAGs 3x4Hyp-GalHyl-COL1A1 Ig lambda chain V-II region TRO lysophosphatidylcholine cholesterol esters PL PL IGLV1-40Ig heavy chain V-III region JON Ig heavy chain V-III region POM cholesterol esters Ig kappa chain V-III region B6 Ig kappa chain V-I region DEE Ig lambda chain V-I region BL2 Ig heavy chain V-III region GAL Ig lambda chain V-VII region MOT Ig heavy chain V-II region OU Ig lambda chain V-I region BL2 Ig kappa chain V-II region GM607 10xdHF-10xglutamyl semialdehyde Ig heavy chain V-III region TEI APOA1Lipoteichoic acid Ligands of STAB1CHEST IGLC1Ig kappa chain V-I region Kue IGLV7-43IGKVA18MASP1COL4A1COL1A1 Ig heavy chain V-II region WAH SPARC Ig kappa chain V-III region SIE Ig lambda chain V-I region VOR NECML STAB2hydroperoxy fatty acid Ig heavy chain V-III region HIL hematite nanoparticle IGHV7-81IGLV11-55Ig lambda chain V-II region BO APOL1 Ig kappa chain V-I region Ka HemoglobinHPRAPOL1APOA1HDL36xHC-MARCO IgH heavy chain V-III region VH26 precursor 4xPalmC-CD36 ferroheme b hydroxy fatty acid Ligands of STAB2Ig kappa chain V-I region Scw Peptide IGLV3-27Ig heavy chain V-I region EU HBA1 hydroperoxy fatty acid porB IGLV2-11Ig kappa chain V-III region HIC N-epsilon-LPS Ig kappa chain V-I region Ni lysophosphatidylcholine hydroperoxy fatty acid Ig lambda chain V-VI region WLT SAA13123829, 30, 57, 86, 124...1, 15, 16, 22, 633875, 13121913075576, 3880, 138, 14551056, 389239, 49, 56, 68, 143...5757869838981, 15, 16, 22, 635712529811, 17, 36, 49, 50, 70...5755, 8911, 17, 36, 49, 50, 70...10555, 8986, 91, 114, 1489257105, 15275286, 91, 114, 148228, 84, 85, 87, 89...571307531105, 152257579875, 13526, 74, 97, 108, 12997, 108315739, 49, 56, 68, 143...80, 138, 145104, 1542211, 17, 36, 49, 50, 70...13025735, 62, 66, 79, 1021355786, 91, 109, 114, 1487527551, 15, 16, 22, 6357512, 15244, 55, 892239, 49, 56, 68, 143...6, 382


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Wikipathways-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).

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Bibliography

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  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 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-HPProteinP00738 (Uniprot-TrEMBL)
6xHC-MARCO ProteinQ9UEW3 (Uniprot-TrEMBL)
6xHC-MSR1 ProteinP21757 (Uniprot-TrEMBL)
7-ketocholesterol MetaboliteCHEBI:64294 (ChEBI)
7xHC-HPProteinP00738 (Uniprot-TrEMBL)
ALB ProteinP02768 (Uniprot-TrEMBL)
ALBProteinP02768 (Uniprot-TrEMBL)
AMBPProteinP02760 (Uniprot-TrEMBL)
APOA1ProteinP02647 (Uniprot-TrEMBL)
APOBProteinP04114 (Uniprot-TrEMBL)
APOE ProteinP02649 (Uniprot-TrEMBL)
APOL1 ProteinO14791 (Uniprot-TrEMBL)
AcK-APOBProteinP04114 (Uniprot-TrEMBL)
Albumin ferrihemeComplexREACT_160718 (Reactome)
Alpha1-Microglobulin heme trimerComplexREACT_161267 (Reactome)
ApohemoglobinComplexREACT_161051 (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)
COL4A1ProteinP02462 (Uniprot-TrEMBL)
COL4A2ProteinP08572 (Uniprot-TrEMBL)
COLEC11 LigandComplexREACT_164610 (Reactome)
COLEC11 MASP1ComplexREACT_165089 (Reactome)
COLEC11 ProteinQ9BWP8 (Uniprot-TrEMBL)
COLEC12 LigandComplexREACT_164817 (Reactome)
COLEC12 LigandComplexREACT_164862 (Reactome)
COLEC12 ProteinQ5KU26 (Uniprot-TrEMBL)
COLEC12 trimerComplexREACT_164280 (Reactome)
Denatured Collagen I,III, Collagen IVComplexREACT_164920 (Reactome)
FTH1ProteinP02794 (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-COL3A1ProteinP02461 (Uniprot-TrEMBL)
GlcNAc MetaboliteCHEBI:17411 (ChEBI)
HBA1 ProteinP69905 (Uniprot-TrEMBL)
HBB ProteinP68871 (Uniprot-TrEMBL)
HPR

APOL1 APOA1

HDL3		ComplexREACT_160983 (Reactome)
HPR ProteinP00739 (Uniprot-TrEMBL)
HPX ferriheme bComplexREACT_161270 (Reactome)
HPX heme bComplexREACT_160999 (Reactome)
HPX ProteinP02790 (Uniprot-TrEMBL)
HPXProteinP02790 (Uniprot-TrEMBL)
HSP90AA1 ProteinP07900 (Uniprot-TrEMBL)
HSP90B1 ProteinP14625 (Uniprot-TrEMBL)
HSPH1 ProteinQ92598 (Uniprot-TrEMBL)
HUA MetaboliteCHEBI:16336 (ChEBI)
HYOU1 ProteinQ9Y4L1 (Uniprot-TrEMBL)
Haptoglobin DimerComplexREACT_161554 (Reactome)
Hemoglobin

HPR APOL1 APOA1

HDL3		ComplexREACT_160920 (Reactome)
Hemoglobin

Haptoglobin

CD163		ComplexREACT_161113 (Reactome)
Hemoglobin

Haptoglobin

CD163		ComplexREACT_161221 (Reactome)
Hemoglobin HaptoglobinComplexREACT_160524 (Reactome)
Hemoglobin DimerComplexREACT_161542 (Reactome)
Heparins MetaboliteCHEBI:24505 (ChEBI)
IGHA1ProteinP01876 (Uniprot-TrEMBL)
IGHA2ProteinP01877 (Uniprot-TrEMBL)
IGHV7-81ProteinQ6PIL0 (Uniprot-TrEMBL)
IGHVProteinA2KUC3 (Uniprot-TrEMBL)
IGKCProteinP01834 (Uniprot-TrEMBL)
IGKV1-5ProteinP01602 (Uniprot-TrEMBL)
IGKV4-1ProteinP06312 (Uniprot-TrEMBL)
IGKVA18ProteinA2NJV5 (Uniprot-TrEMBL)
IGLC1ProteinP0CG04 (Uniprot-TrEMBL)
IGLC2ProteinP0CG05 (Uniprot-TrEMBL)
IGLC3ProteinP0CG06 (Uniprot-TrEMBL)
IGLC6ProteinP0CF74 (Uniprot-TrEMBL)
IGLC7ProteinA0M8Q6 (Uniprot-TrEMBL)
IGLV1-36ProteinQ5NV67 (Uniprot-TrEMBL)
IGLV1-40ProteinQ5NV69 (Uniprot-TrEMBL)
IGLV1-44ProteinQ5NV81 (Uniprot-TrEMBL)
IGLV10-54ProteinQ5NV86 (Uniprot-TrEMBL)
IGLV11-55ProteinQ5NV87 (Uniprot-TrEMBL)
IGLV2-11ProteinQ5NV84 (Uniprot-TrEMBL)
IGLV2-18ProteinQ5NV65 (Uniprot-TrEMBL)
IGLV2-23ProteinQ5NV89 (Uniprot-TrEMBL)
IGLV2-33ProteinQ5NV66 (Uniprot-TrEMBL)
IGLV3-12ProteinQ5NV85 (Uniprot-TrEMBL)
IGLV3-16ProteinQ5NV64 (Uniprot-TrEMBL)
IGLV3-22ProteinQ5NV75 (Uniprot-TrEMBL)
IGLV3-25ProteinQ5NV90 (Uniprot-TrEMBL)
IGLV3-27ProteinQ5NV91 (Uniprot-TrEMBL)
IGLV4-3ProteinQ5NV61 (Uniprot-TrEMBL)
IGLV4-60ProteinQ5NV79 (Uniprot-TrEMBL)
IGLV4-69ProteinQ5NV92 (Uniprot-TrEMBL)
IGLV5-37ProteinQ5NV68 (Uniprot-TrEMBL)
IGLV5-45ProteinQ5NV82 (Uniprot-TrEMBL)
IGLV7-43ProteinQ5NV80 (Uniprot-TrEMBL)
IGLV7-46ProteinQ5NV83 (Uniprot-TrEMBL)
IGLV8-61ProteinQ5NV62 (Uniprot-TrEMBL)
IGLVProteinA2NXD2 (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-MicroglobulinComplexREACT_161115 (Reactome)
IgAComplexREACT_160552 (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

Hemopexin

heme		ComplexREACT_160657 (Reactome)
LRP1

Hemopexin

heme		ComplexREACT_161454 (Reactome)
LRP1 ProteinQ07954 (Uniprot-TrEMBL)
LRP1ProteinQ07954 (Uniprot-TrEMBL)
Ligands of CD36ComplexREACT_164594 (Reactome)
Ligands of COLEC11MetaboliteREACT_164682 (Reactome)
Ligands of COLEC12REACT_164668 (Reactome)
Ligands of MARCOMetaboliteREACT_164133 (Reactome)
Ligands of MSR1MetaboliteREACT_164161 (Reactome)
Ligands of SCARA5REACT_165390 (Reactome)
Ligands of SCARB1ComplexREACT_165375 (Reactome)
Ligands of SCARF1MetaboliteREACT_165072 (Reactome)
Ligands of STAB1ComplexREACT_165287 (Reactome)
Ligands of STAB2MetaboliteREACT_165222 (Reactome)
Lipoteichoic acid MetaboliteCHEBI:28640 (ChEBI)
MARCO LigandComplexREACT_164163 (Reactome)
MARCO LigandComplexREACT_164178 (Reactome)
MARCO trimerComplexREACT_165245 (Reactome)
MASP1ProteinP48740 (Uniprot-TrEMBL)
MSR1 Collagen I,III,IVComplexREACT_165150 (Reactome)
MSR1 LigandComplexREACT_164371 (Reactome)
MSR1 LigandComplexREACT_165339 (Reactome)
MSR1 ComplexREACT_164470 (Reactome)
Man MetaboliteCHEBI:4208 (ChEBI)
MethemoglobinComplexREACT_160621 (Reactome)
N-epsilon-MetaboliteCHEBI:60125 (ChEBI)
NECML MetaboliteCHEBI:53014 (ChEBI)
O2 MetaboliteCHEBI:15379 (ChEBI)
PL MetaboliteCHEBI:16247 (ChEBI)
Peptide MetaboliteCHEBI:16670 (ChEBI)
Phosphatidylserine MetaboliteCHEBI:18303 (ChEBI)
Platelet glycoprotein IV LigandComplexREACT_165052 (Reactome)
Platelet glycoprotein IV LigandComplexREACT_165582 (Reactome)
SAA1ProteinP0DJI8 (Uniprot-TrEMBL)
SCARA5 LigandComplexREACT_164504 (Reactome)
SCARA5 LigandComplexREACT_164789 (Reactome)
SCARA5 ProteinQ6ZMJ2 (Uniprot-TrEMBL)
SCARA5 trimerComplexREACT_164905 (Reactome)
SCARB1 Endocytosed LigandComplexREACT_164502 (Reactome)
SCARB1 Endocytosed LigandComplexREACT_164891 (Reactome)
SCARB1 LigandComplexREACT_164882 (Reactome)
SCARB1-2 ProteinQ8WTV0-2 (Uniprot-TrEMBL)
SCARB1-2ProteinQ8WTV0-2 (Uniprot-TrEMBL)
SCARF1 LigandComplexREACT_165139 (Reactome)
SCARF1 LigandComplexREACT_165478 (Reactome)
SCARF1 ProteinQ14162 (Uniprot-TrEMBL)
SCARF1ProteinQ14162 (Uniprot-TrEMBL)
SCGB3A2 ProteinQ96PL1 (Uniprot-TrEMBL)
SPARC ProteinP09486 (Uniprot-TrEMBL)
STAB1 LigandComplexREACT_164343 (Reactome)
STAB1 LigandComplexREACT_164896 (Reactome)
STAB1 ProteinQ9NY15 (Uniprot-TrEMBL)
STAB1ProteinQ9NY15 (Uniprot-TrEMBL)
STAB2 LigandComplexREACT_164253 (Reactome)
STAB2 LigandComplexREACT_164299 (Reactome)
STAB2ProteinQ8WWQ8 (Uniprot-TrEMBL)
TAGs MetaboliteCHEBI:17855 (ChEBI)
Truncated Alpha1-Microglobulin heme trimerComplexREACT_161123 (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 bMetaboliteREACT_161398 (Reactome)
hydroperoxy fatty acid MetaboliteCHEBI:64009 (ChEBI)
hydroxy fatty acid MetaboliteCHEBI:24654 (ChEBI)
lysophosphatidylcholine MetaboliteCHEBI:60479 (ChEBI)
oxidized phospholipids MetaboliteCHEBI:60156 (ChEBI)
phosphatidylinositol MetaboliteCHEBI:16749 (ChEBI)
porB ProteinP18195 (Uniprot-TrEMBL)
silicon dioxide nanoparticle MetaboliteCHEBI:50828 (ChEBI)
thioether crosslinked residues-AMBPProteinP02760 (Uniprot-TrEMBL)
titanium dioxide nanoparticle MetaboliteCHEBI:51050 (ChEBI)

Annotated Interactions

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SourceTargetTypeDatabase referenceComment
4xPalmC-CD36REACT_163694 (Reactome)
ALBArrowREACT_160182 (Reactome)
AMBPArrowREACT_160303 (Reactome)
AMBPREACT_160079 (Reactome)
AMBPREACT_160136 (Reactome)
Albumin ferrihemeREACT_160182 (Reactome)
ApohemoglobinArrowREACT_160297 (Reactome)
CD163REACT_160225 (Reactome)
COLEC11 MASP1REACT_163764 (Reactome)
COLEC12 trimerREACT_163907 (Reactome)
Denatured Collagen I,III, Collagen IVREACT_163647 (Reactome)
HPR

APOL1 APOA1

HDL3		REACT_160200 (Reactome)
HPX ferriheme bArrowREACT_160182 (Reactome)
HPX ferriheme bArrowREACT_160297 (Reactome)
HPX heme bREACT_160235 (Reactome)
HPXREACT_160112 (Reactome)
HPXREACT_160182 (Reactome)
HPXREACT_160297 (Reactome)
Haptoglobin DimerREACT_160172 (Reactome)
Hemoglobin HaptoglobinREACT_160225 (Reactome)
Hemoglobin DimerREACT_160172 (Reactome)
Hemoglobin DimerREACT_160200 (Reactome)
IgAArrowREACT_160303 (Reactome)
LRP1REACT_160235 (Reactome)
Ligands of CD36REACT_163694 (Reactome)
Ligands of COLEC11REACT_163764 (Reactome)
Ligands of COLEC12REACT_163907 (Reactome)
Ligands of MARCOREACT_163964 (Reactome)
Ligands of MSR1REACT_163645 (Reactome)
Ligands of SCARA5REACT_163819 (Reactome)
Ligands of SCARB1REACT_163672 (Reactome)
Ligands of SCARF1REACT_164012 (Reactome)
Ligands of STAB1REACT_163850 (Reactome)
Ligands of STAB2REACT_163962 (Reactome)
MARCO trimerREACT_163964 (Reactome)
MSR1 REACT_163645 (Reactome)
MSR1 REACT_163647 (Reactome)
MethemoglobinREACT_160297 (Reactome)
REACT_160079 (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).
REACT_160112 (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).
REACT_160136 (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).
REACT_160172 (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.
REACT_160182 (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).
REACT_160193 (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.
REACT_160200 (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).
REACT_160225 (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.
REACT_160232 (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).
REACT_160235 (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).
REACT_160297 (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).
REACT_160303 (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.
REACT_163645 (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.
REACT_163647 (Reactome) As inferred from mouse, MSR1 (SCARA1) binds denatured collagen I, denatured collagen III, and nondenatured or glycated collagen IV.
REACT_163672 (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.
REACT_163694 (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.
REACT_163711 (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).
REACT_163736 (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).
REACT_163764 (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).
REACT_163777 (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).
REACT_163780 (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.
REACT_163819 (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.
REACT_163824 (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).
REACT_163850 (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).
REACT_163867 (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).
REACT_163907 (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
REACT_163962 (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).
REACT_163964 (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.
REACT_163969 (Reactome) As inferred from mouse, the SCARA5:ligand complex is endocytosed.
REACT_163998 (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.
REACT_164000 (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)
REACT_164012 (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).
SCARA5 trimerREACT_163819 (Reactome)
SCARB1-2REACT_163672 (Reactome)
SCARF1REACT_164012 (Reactome)
STAB1REACT_163850 (Reactome)
STAB2REACT_163962 (Reactome)
heme bREACT_160079 (Reactome)
heme bREACT_160112 (Reactome)
heme bREACT_160136 (Reactome)
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