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

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40, 63, 91, 108, 141133, 15849, 62, 6715, 24, 129, 1424, 9, 29, 38, 80...32, 53, 7047, 51, 9321, 47, 97, 103, 135...146132, 13814, 132, 1384, 23, 29, 36, 52...13, 19, 146, 15816, 18, 26, 41, 43...1, 22, 54, 69, 71...20, 27, 35, 67, 101...3, 5, 34, 39, 45...8, 31, 82, 107, 110...1328, 31, 110, 12668, 9625, 29, 38, 48, 99...29, 38, 482, 42, 95, 102, 104...7, 10, 33, 37, 50...53, 109, 11528, 44, 85, 90, 15565, 136135, 1546, 11, 30, 85, 87...11, 17, 46, 89, 106...endocytic vesiclecytosol10xdHF-10xglutamyl semialdehyde (Pro)-6xL-tyrosine residue-3xOxoH-2xmodified L-lysine residue-N'-formyl-L-kynurenine-APOB(28-4563) Ig lambda chain V-IV region Bau LRP1:Hemopexin:hemeNECML 3x4Hyp-GlcGalHyl-COL1A1 Ig lambda chain V-II region WIN SCARF1:LigandIg kappa chain V-I region Rei Ig lambda chain V-VI region SUT HPX GalHyl-COL1A1 TAGs hematite nanoparticle oxidized phospholipids LRP1IGKV4-1(21-?) TAGs 3x4Hyp-3Hyp-GlcGalHyl-COL3A1 3x4Hyp-GalHyl-COL3A1 3x4Hyp-3Hyp-GalHyl-COL3A1 NECML lysophosphatidylcholine Ig kappa chain V-III region CLL ferriheme b ferriheme b Ig kappa chain V-I region Bi Ig heavy chain V-I region WOL Peptide HSPH1 HBB Ig lambda chain V-VII region MOT IGLV2-23(1-?) Ig lambda chain V-I region NEWM IGHA1 MSR1:CollagenI,III,IVPL LPS poly(I) Ig heavy chain V-III region KOL 3x4Hyp-5Hyl-COL1A1 HBA1 NECML Ig kappa chain V-I region Lay 3x4Hyp-COL1A1 Ig kappa chain V-I region BAN lysophosphatidylcholine Ig lambda chain V-II region BOH Ig heavy chain V-I region HG3 APOA1(25-266) Ig kappa chain V-I region Ka PL HPX Ig kappa chain V-I region Wes Peptide 10xdHF-10xglutamyl semialdehyde (Pro)-6xL-tyrosine residue-3xOxoH-2xmodified L-lysine residue-N'-formyl-L-kynurenine-APOB(28-4563) 3x4Hyp-GalHyl-COL1A2 Ig kappa chain V-III region HAH HSP90B1 6xHC-MSR1 lysophosphatidylcholine HSPH1 CHEST TAGs 3x4Hyp-COL1A2 Ig heavy chain V-III region HIL 3x4Hyp-3Hyp-GlcGalHyl-COL1A1 3x4Hyp-3Hyp-GlcGalHyl-COL1A1 PL IGLC3 5Hyl-COL1A2 Ig heavy chain V-II region COR Ig kappa chain V-IV region STH 6xHC-MSR1 TAGs Ig kappa chain V-II region Cum STAB1 Unmethylated CpG DNA hydroxy fatty acid STAB2:LigandIGLV3-12(1-?) CHEST hydroxy fatty acid PL TruncatedAlpha1-Microglobulin:heme trimerHBB PL hydroxy fatty acid Heparins IGHV7-81(1-?) heme PL PL GlcGalHyl-COL1A1 Ig kappa chain V-III region B6 Ig heavy chain V-II region DAW Ig kappa chain V-II region RPMI 6410 TAGs Phosphatidylserine 10xdHF-10xglutamyl semialdehyde (Pro)-6xL-tyrosine residue-3xOxoH-2xmodified L-lysine residue-N'-formyl-L-kynurenine-APOB(28-4563) Ligands of SCARF1poly(G) carrageenan Ig kappa chain V-I region Scw 3x4Hyp-3Hyp-GalHyl-COL1A2 APOA1(25-266) Ig heavy chain V-III region BUR CHOL hydroxy fatty acid Ig kappa chain V-I region Daudi Ig kappa chain V-I region Gal cholesterol esters hydroxy fatty acid 7-ketocholesterol CHEST 3x4Hyp-3Hyp-5Hyl-COL3A1 Ig lambda chain V-II region WIN APOA1(25-266) 7xHC-HP(19-160) AMBP(20-202) Fe3+ SCARA5:LigandIg lambda chain V-II region MGC AcK-APOB(28-4563) MARCO:Ligandcholesterol IGLV2-18(1-?) heme SCARF1PL Ig lambda chain V-II region VIL Ig lambda chain V-IV region Hil CHOL Ig heavy chain V-II region COR APOL1 O2 Ig lambda chain V-II region NEI hydroxy fatty acid Ig heavy chain V-III region CAM CD163porB CHEST ferriheme b PL O2 Ig lambda chain V region 4A LCFAs GalNAc Ig lambda chain V-I region MEM CHEST PL Ig heavy chain V-II region WAH Ig kappa chain V-I region Mev Ig heavy chain V-II region NEWM IGLC3 HBA1 CHOL IGLV5-45(1-?) Ig heavy chain V-III region BRO HBA1 lysophosphatidylcholine COLEC11:LigandIGHV(1-?) 3x4Hyp-GlcGalHyl-COL1A1 CHOL LPS Ig lambda chain V-IV region MOL HSP90AA1 lysophosphatidylcholine APOE Ig kappa chain V-I region AU Phosphatidylserine CHEST IGKC Ig heavy chain V-III region CAM hydroperoxy fatty acid CALR 5xHC-HP(162-406) lysophosphatidylcholine TAGs IGLV2-23(1-?) CALR Ig kappa chain V-III region SIE TAGs SCARF1 HSP90B1 O2 1,3-beta-D-glucan Ig heavy chain V-I region HG3 IGKV4-1(21-?) CHOL hydroperoxy fatty acid 10xdHF-10xglutamyl semialdehyde (Pro)-6xL-tyrosine residue-3xOxoH-2xmodified L-lysine residue-N'-formyl-L-kynurenine-APOB(28-4563) TAGs IGLV5-45(1-?) STAB1 Ig lambda chain V-I region NEWM IGLV2-11(1-?) Ig heavy chain V-I region ND N-epsilon-(1-(1-carboxy)ethyl)lysine CHEST IgA:J-CHAIN:IgA1,3-beta-D-glucan Ig lambda chain V-I region EPS 3x4Hyp-5Hyl-COL3A1 Ig lambda chain V-II region BUR COLEC12 Man hydroperoxy fatty acid PL Ig kappa chain V-IV region JI Ig kappa chain V-II region RPMI 6410 cholesterol CHOL 3x4Hyp-3Hyp-GlcGalHyl-COL1A2 10xdHF-10xglutamyl semialdehyde (Pro)-6xL-tyrosine residue-3xOxoH-2xmodified L-lysine residue-N'-formyl-L-kynurenine-APOB(28-4563) IGLV11-55(1-?) TAGs IGLV7-46(1-?) 3x4Hyp-3Hyp-GalHyl-COL1A1 FTH1 Ig kappa chain V-I region Hau Ig kappa chain V-I region AU Phosphatidylserine Ig lambda chain V-II region VIL GalHyl-COL1A2 5Hyl-COL3A1 PL heme IGLV3-12(1-?) STAB2(1136-2551) IGLV5-37(1-?) hydroxy fatty acid N-epsilon-(1-(1-carboxy)ethyl)lysine Ig heavy chain V-III region WEA Ig kappa chain V-III region POM AcK-APOB(28-4563) SCGB3A2 poly(G) HBB Ig kappa chain V-I region WAT CHEST Lipoteichoic acid IGLV2-18(1-?) lysophosphatidylcholine Ig kappa chain V-III region HIC Double-stranded RNA PL Ig kappa chain V-II region FR Ig lambda chain V-IV region Hil Double-stranded RNA CHEST Ig kappa chain V-I region AG Ig kappa chain V-II region TEW IGLV1-36(1-?) Ig kappa chain V-I region Wes Alpha1-Microglobulin:heme trimerIg lambda chain V-I region NEW 3x4Hyp-3Hyp-GlcGalHyl-COL3A1 titanium dioxide nanoparticle Ig kappa chain V-I region WEA Ig heavy chain V-I region EU Lipoteichoic acid hematite nanoparticle cholesterol esters Haptoglobin DimerIg kappa chain V-IV region JI hydroxy fatty acid N-epsilon-(1-(1-carboxy)ethyl)lysine HPXPhosphatidylserine cholesterol esters Peptide 10xdHF-10xglutamyl semialdehyde (Pro)-6xL-tyrosine residue-3xOxoH-2xmodified L-lysine residue-N'-formyl-L-kynurenine-APOB(28-4563) carrageenan COLEC12:LigandCOLEC12 trimerIg kappa chain V-II region GM607 hydroxy fatty acid Ig lambda chain V-I region BL2 LCFAs SCARA5 Ig heavy chain V-III region ZAP Ig kappa chain V-IV region Len COLEC12:LigandAPOB(28-4563) FTL Double-stranded RNA Ig kappa chain V-III region IARC/BL41 TAGs IGLV1-44(1-?) 3x4Hyp-5Hyl-COL1A1 Ig lambda chain V-II region BO Ig kappa chain V-I region OU Ig kappa chain V-I region Bi N-epsilon-(1-(1-carboxy)ethyl)lysine hydroxy fatty acid Ig kappa chain V-III region VH Denatured CollagenI,III, Collagen IVcholesterol esters AMBP(20-202)TAGs JCHAIN Ig kappa chain V-I region OU 5Hyl-COL3A1 PL IGLV7-46(1-?) Ig kappa chain V-I region Ni Ig kappa chain V-I region EU Ig lambda chain V-V region DEL 7-ketocholesterol N-epsilon-(1-(1-carboxy)ethyl)lysine 3x4Hyp-3Hyp-COL1A2 1,3-beta-D-glucan cholesterol esters Ig heavy chain V-III region ZAP LPS GlcGalHyl-COL1A2 HUA TAGs CHOL GalHyl-COL1A1 LPS Ig heavy chain V-III region TIL CHEST Ligands of COLEC12Hemoglobin:Haptoglobin:CD163ferriheme b NECML Lipoteichoic acid HPX oxidized phospholipids GlcNAc PlateletglycoproteinIV:LigandALB IGKV1-5(23-?) NECML AcK-APOB(28-4563) cholesterol COL1A1 APOA1(25-266) COL4A1(173-1669) MSR1 (SCARA1) trimer3x4Hyp-3Hyp-5Hyl-COL3A1 Ig heavy chain V-III region BUT CD163 3x4Hyp-GalHyl-COL1A1 oxidized phospholipids COL3A1 IGLV3-27(1-?) IGLC6 Ig kappa chain V-III region Ti AcK-APOB(28-4563) dextran sulfate Ig kappa chain V-II region MIL Ig heavy chain V-III region JON HPR Ig heavy chain V-III region GAL MASP1(20-699) SCGB3A2 HUA Phosphatidylserine ferroheme b HBB Ig kappa chain V-I region CAR 7-ketocholesterol 3x4Hyp-3Hyp-COL1A1 GalNAc Phosphatidylserine SCARB1-2AcK-APOB(28-4563) IGLV4-60(1-?) IGLV11-55(1-?) LPS Ig lambda chain V-VI region WLT CHOL ALBHBB CHEST Albumin:ferrihemeCHOL IGLV1-40(1-?) Ig heavy chain V-III region POM IGKC 10xdHF-10xglutamyl semialdehyde (Pro)-6xL-tyrosine residue-3xOxoH-2xmodified L-lysine residue-N'-formyl-L-kynurenine-APOB(28-4563) IGLV3-22(1-?) cholesterol IGLV3-16(1-?) HBB 3x4Hyp-3Hyp-COL1A2 AcK-APOB(28-4563) 3x4Hyp-COL1A2 N-epsilon-(1-(1-carboxy)ethyl)lysine Ig heavy chain V-III region WEA HPR:APOL1:APOA1:HDL3Ig kappa chain V-I region Roy TAGs Ig lambda chain V-IV region Kern thioether crosslinked C53-AMBP(20-202) IGLC6 CHOL Ig kappa chain V-II region MIL IGKVA18(21-?) IGKV1-5(23-?) Ig heavy chain V-II region MCE 5Hyl-COL1A1 7-ketocholesterol IGLV4-69(1-?) Ig heavy chain V-II region ARH-77 APOA1(25-266) Ig kappa chain V-I region HK101 Lipoteichoic acid COLEC11 Ligands of COLEC11HBA1 HPX:ferriheme bSPARC cholesterol titanium dioxide nanoparticle IGLC7 MARCO trimerIg kappa chain V region EV15 Ig lambda chain V-VI region SUT 5Hyl-COL1A2 MethemoglobinLPS ferriheme b hydroxy fatty acid 3x4Hyp-GlcGalHyl-COL1A2 Ig kappa chain V-I region Ni Unmethylated CpG DNA Ig lambda chain V-I region WAH SCARA5:Ligand1,3-beta-D-glucan FTH1 Ig kappa chain V-I region WAT Fe3+ Ig kappa chain V-III region NG9 GalHyl-COL1A2 Ig heavy chain V-I region WOL 3x4Hyp-5Hyl-COL1A2 SCARA5 Ig heavy chain V-III region WAS CHEST Hemoglobin DimerAPOA1(25-266) HSP90AA1 Ig kappa chain V-I region Hau Ig lambda chain V-II region MGC Ig lambda chain V-II region NIG-58 hydroperoxy fatty acid Ig heavy chain V-III region HIL Peptide IGLV1-40(1-?) IGLV(23-?) Lipoteichoic acid PL Ligands of STAB2Ig kappa chain V-I region Gal TAGs ferriheme b 7-ketocholesterol CHOL ferroheme b Double-stranded RNA hydroperoxy fatty acid APOL1 GlcGalHyl-COL3A1(154-1241) 3x4Hyp-GalHyl-COL1A2 Ligands of CD36heme TAGs Ligands of SCARB1MSR1:LigandIg heavy chain V-II region MCE Ig heavy chain V-III region TUR IGHA2 3x4Hyp-COL3A1 HSPH1 Ig kappa chain V-III region NG9 PL LPS Ig heavy chain V-II region ARH-77 Ig kappa chain V region EV15 Phosphatidylserine 3x4Hyp-GalHyl-COL1A1 IGLV4-69(1-?) Ig heavy chain V-II region OU 3x4Hyp-GlcGalHyl-COL3A1 IgH heavy chain V-III region VH26 precursor Ig heavy chain V-III region KOL PI Ig lambda chain V-I region VOR NECML STAB2:Ligand4xPalmC-CD36 TAGs HYOU1 Peptide TAGs titanium dioxide nanoparticle Ig lambda chain V-VI region WLT AcK-APOB(28-4563) Phosphatidylserine Ig lambda chain V-II region TRO Unmethylated CpG DNA Ig kappa chain V-III region GOL SCARB1-2 IGLV2-33(1-?) 3x4Hyp-3Hyp-GalHyl-COL1A1 Ig lambda chain V region 4A Ig lambda chain V-II region NIG-84 Ig kappa chain V-I region Ka Double-stranded RNA silicon dioxide nanoparticle L-fucose 3x4Hyp-3Hyp-COL3A1 Ig lambda chain V-III region SH COL4A2(184-1712) Double-stranded RNA N-epsilon-(1-(1-carboxy)ethyl)lysine Ig kappa chain V-I region Roy Double-stranded RNA HSP90AA1 Peptide Ig lambda chain V-I region NIG-64 lysophosphatidylcholine 5xHC-HP(162-406) Lipoteichoic acid Ig kappa chain V-III region VG SCARB1-2 Ig kappa chain V-III region B6 Double-stranded RNA Ig lambda chain V-I region HA silicon dioxide nanoparticle DNA Ig heavy chain V-III region GA NECML 1,3-beta-D-glucan Lipoteichoic acid Peptide hydroperoxy fatty acid Phosphatidylserine APOB(28-4563) COL1A2 heme bL-fucose PI AMBP(20-198) LPS hydroxy fatty acid Ig kappa chain V-IV region B17 Ig lambda chain V-I region MEM 3x4Hyp-3Hyp-5Hyl-COL1A1 Ig lambda chain V-I region BL2 IGLC7 Ig heavy chain V-III region BUT Heparins O2 CHS Ig lambda chain V-VI region NIG-48 7xHC-HP(19-160) 7-ketocholesterol 3x4Hyp-GlcGalHyl-COL1A2 LCFAs LPS LPS CHOL Ig heavy chain V-III region TIL AcK-APOB(28-4563) HBB hydroperoxy fatty acid Ig heavy chain V-III region TRO 3x4Hyp-3Hyp-5Hyl-COL1A1 Ig lambda chain V-I region NIG-64 Ig kappa chain V-I region Kue Ig heavy chain V-III region NIE SAA1(19-122) Ig heavy chain V-III region LAY IGHV7-81(1-?) 7-ketocholesterol Phosphatidylserine 6xHC-MARCO HBA1 3x4Hyp-COL3A1 10xdHF-10xglutamyl semialdehyde (Pro)-6xL-tyrosine residue-3xOxoH-2xmodified L-lysine residue-N'-formyl-L-kynurenine-APOB(28-4563) AcK-APOB(28-4563) poly(I) GlcGalHyl-COL1A2 SAA1(19-122) CALR IGLV4-3(1-?) Ig kappa chain V-III region VH Lipoteichoic acid Ig kappa chain V-III region HAH silicon dioxide nanoparticle lysophosphatidylcholine COLEC11:MASP1Ligands of MARCO3x4Hyp-3Hyp-COL1A1 Lipoteichoic acid 6xHC-MSR1 hydroperoxy fatty acid 5xHC-HP(162-406) IGLV2-33(1-?) Ig lambda chain V-VI region AR Ig lambda chain V-II region BUR CHOL Ig lambda chain V-I region VOR Ig lambda chain V-I region NEW Ig heavy chain V-III region BUR CHOL Ig lambda chain V-II region NIG-84 3x4Hyp-5Hyl-COL1A2 CHS heme b hematite nanoparticle 7-ketocholesterol DNA Man Ig kappa chain V-III region WOL Ig lambda chain V-VI region AR Ig heavy chain V-III region LAY Ig heavy chain V-III region GA IGLV10-54(1-?) Ig lambda chain V-VI region NIG-48 LRP1 Ig lambda chain V-III region LOI Ig lambda chain V-II region NEI heme b GlcNAc Ig lambda chain V-IV region X hydroperoxy fatty acid SCARF1 3x4Hyp-3Hyp-5Hyl-COL1A2 Ig lambda chain V-II region BO Ligands of STAB1Double-stranded RNA SCARB1-2 Ig lambda chain V-IV region X Phosphatidylserine IGLV4-60(1-?) 1,3-beta-D-glucan IGLC1 SCARB1:EndocytosedLigandlysophosphatidylcholine heme COL1A1 Ig lambda chain V-II region TOG Ig heavy chain V-III region DOB Ig heavy chain V-III region JON Ig heavy chain V-III region TEI Ig kappa chain V-I region BAN 3x4Hyp-COL1A1 3x4Hyp-3Hyp-GlcGalHyl-COL1A2 cholesterol Ig heavy chain V-II region HE Ig kappa chain V-III region Ti Ig kappa chain V-II region Cum APOA1(25-266) 7-ketocholesterol Ig kappa chain V-I region Kue carrageenan CHEST poly(G) 7-ketocholesterol FTL hydroperoxy fatty acid 5,6beta-epoxy-cholesterol Ligands of MSR110xdHF-10xglutamyl semialdehyde (Pro)-6xL-tyrosine residue-3xOxoH-2xmodified L-lysine residue-N'-formyl-L-kynurenine-APOB(28-4563) HSP90B1 Ig lambda chain V-VI region EB4 IGLV3-27(1-?) Ig lambda chain V-V region DEL IGLV7-43(1-?) IGLV7-43(1-?) COL1A2 SPARC Ig kappa chain V-III region VG 10xdHF-10xglutamyl semialdehyde (Pro)-6xL-tyrosine residue-3xOxoH-2xmodified L-lysine residue-N'-formyl-L-kynurenine-APOB(28-4563) AcK-APOB(28-4563) Ig heavy chain V-II region OU Ig heavy chain V-III region TUR Ig kappa chain V-IV region STH FTL CHS PL IGLV2-11(1-?) dextran sulfate 5,6beta-epoxy-cholesterol Ig heavy chain V-III region TEI MARCO:LigandIGLV8-61(1-?) heme b3x4Hyp-5Hyl-COL3A1 TAGs GlcGalHyl-COL1A1 SCGB3A2 5xHC-HP(162-406) CHOL Hemoglobin:HaptoglobinGalHyl-COL3A1 Ig heavy chain V-II region WAH SCARA5 Ig kappa chain V-I region CAR Ig kappa chain V-IV region B17 Peptide SCARB1:EndocytosedLigandSTAB1TAGs cholesterol esters Ig heavy chain V-I region Mot 10xdHF-10xglutamyl semialdehyde (Pro)-6xL-tyrosine residue-3xOxoH-2xmodified L-lysine residue-N'-formyl-L-kynurenine-APOB(28-4563) 7-ketocholesterol Ligands of SCARA5COL4A2(184-1712) CHEST Ig kappa chain V-I region Scw Fe3+ STAB1:Ligand7-ketocholesterol Ig heavy chain V-I region Mot 3x4Hyp-3Hyp-GalHyl-COL3A1 APOE Ig kappa chain V-I region WEA hydroperoxy fatty acid Ig lambda chain V-IV region MOL CHEST HPX hydroxy fatty acid Ig kappa chain V-I region DEE Ig lambda chain V-IV region Bau MSR1:LigandSCARF1:LigandPL Ig heavy chain V-II region HE APOB(28-4563) IGLV10-54(1-?) APOB(28-4563) Ig heavy chain V-III region NIE 7-ketocholesterol HBA1 FTH1 Ig lambda chain V-VII region MOT Phosphatidylserine O2 3x4Hyp-GlcGalHyl-COL3A1 IGHA2 IGLV(23-?) IGLV3-25(1-?) Ig heavy chain V-II region NEWM Ig kappa chain V-I region Rei 6xHC-MARCO heme 6xHC-MSR1 Ig lambda chain V-II region NIG-58 APOA1(25-266) hydroperoxy fatty acid AcK-APOB(28-4563) Ig lambda chain V-VI region EB4 Ig heavy chain V-III region WAS IGLC2 10xdHF-10xglutamyl semialdehyde (Pro)-6xL-tyrosine residue-3xOxoH-2xmodified L-lysine residue-N'-formyl-L-kynurenine-APOB(28-4563) 4xPalmC-CD36 3x4Hyp-3Hyp-5Hyl-COL1A2 Ig heavy chain V-III region GAL lysophosphatidylcholine Ig heavy chain V-III region TRO IgA:Alpha-1-MicroglobulinSPARC Ig lambda chain V-I region WAH Ig kappa chain V-I region AG lysophosphatidylcholine Ig heavy chain V-II region SESS AcK-APOB(28-4563) AMBP(20-198)PI hydroxy fatty acid IGLV1-36(1-?) Ig heavy chain V-I region ND LPS LPS 10xdHF-10xglutamyl semialdehyde (Pro)-6xL-tyrosine residue-3xOxoH-2xmodified L-lysine residue-N'-formyl-L-kynurenine-APOB(28-4563) lysophosphatidylcholine HBA1 Ig kappa chain V-II region GM607 STAB1:LigandTAGs hydroxy fatty acid Ig kappa chain V-I region Walker JCHAIN NECML PL cholesterol esters CHEST Ig kappa chain V-III region HIC Ig lambda chain V-II region TRO Ig heavy chain V-I region EU PI PL HUA dextran sulfate IGLV3-16(1-?) NECML LPS APOA1(25-266) 7xHC-HP(19-160) Peptide CALR IGLV5-37(1-?) Ig heavy chain V-I region SIE Ig heavy chain V-II region SESS PlateletglycoproteinIV:LigandIGLV3-22(1-?) lysophosphatidylcholine 3x4Hyp-3Hyp-GalHyl-COL1A2 IGLV8-61(1-?) COLEC12 heme Lipoteichoic acid hydroperoxy fatty acid hydroperoxy fatty acid Ig kappa chain V-III region CLL Ig lambda chain V-II region TOG IGLV3-25(1-?) TAGs HPX:heme bhydroxy fatty acid hydroperoxy fatty acid IGLV4-3(1-?) SAA1(19-122) Heparins Ig heavy chain V-I region SIE poly(I) 4xPalmC-CD36CALR MASP1(20-699) Ig heavy chain V-II region DAW 3x4Hyp-GalHyl-COL3A1 COLEC11 TAGs CHOL Ig heavy chain V-III region POM Ig kappa chain V-I region Mev STAB2(1136-2551) APOE LRP1:Hemopexin:hemeGalNAc AcK-APOB(28-4563) Ig kappa chain V-I region Lay Ig kappa chain V-III region POM Ig lambda chain V-IV region Kern SCARA5 trimerHYOU1 LPS Ig heavy chain V-III region DOB 7-ketocholesterol 10xdHF-10xglutamyl semialdehyde (Pro)-6xL-tyrosine residue-3xOxoH-2xmodified L-lysine residue-N'-formyl-L-kynurenine-APOB(28-4563) 6xHC-MARCO PL Ig kappa chain V-I region EU IGLV1-44(1-?) 1,3-beta-D-glucan 1,3-beta-D-glucan N-epsilon-(1-(1-carboxy)ethyl)lysine cholesterol Ig kappa chain V-I region Walker Hemoglobin:HPR:APOL1:APOA1:HDL3IGLC1 SAA1(19-122) IGKVA18(21-?) Ig kappa chain V-I region DEE PL GalHyl-COL3A1 Ig lambda chain V-I region EPS IGHV(1-?) Ig lambda chain V-III region LOI Ig kappa chain V-III region SIE Lipoteichoic acid IGLC2 LPS Ig kappa chain V-III region WOL AcK-APOB(28-4563) 1,3-beta-D-glucan APOB(28-4563) Ig lambda chain V-I region HA ferriheme b Ig kappa chain V-II region FR ApohemoglobinCALR STAB2(1136-2551)N-epsilon-(1-(1-carboxy)ethyl)lysine Ig lambda chain V-III region SH 7-ketocholesterol COL3A1 Ig kappa chain V-I region Daudi IGHA1 3x4Hyp-3Hyp-COL3A1 Ig kappa chain V-IV region Len AcK-APOB(28-4563) PL AcK-APOB(28-4563) HPR IgH heavy chain V-III region VH26 precursor hydroperoxy fatty acid CD163 Ig kappa chain V-III region IARC/BL41 GlcGalHyl-COL3A1(154-1241) PI Hemoglobin:Haptoglobin:CD1635,6beta-epoxy-cholesterol 5Hyl-COL1A1 PI 7-ketocholesterol HYOU1 CHOL Ig kappa chain V-III region GOL Ig lambda chain V-II region BOH 10xdHF-10xglutamyl semialdehyde (Pro)-6xL-tyrosine residue-3xOxoH-2xmodified L-lysine residue-N'-formyl-L-kynurenine-APOB(28-4563) SCARB1:LigandIg kappa chain V-II region TEW 10xdHF-10xglutamyl semialdehyde (Pro)-6xL-tyrosine residue-3xOxoH-2xmodified L-lysine residue-N'-formyl-L-kynurenine-APOB(28-4563) lysophosphatidylcholine LRP1 CHEST COLEC12 Ig kappa chain V-I region HK101 Ig heavy chain V-III region BRO lysophosphatidylcholine 7xHC-HP(19-160) COL4A1(173-1669) PL 57412415, 12915011, 89, 114, 120, 12347, 51, 93, 98, 130601504, 23, 29, 36, 52...18, 736074124606460743, 57413213, 19, 133, 146, 15811, 89, 114, 120, 123681327631, 82, 11013, 19, 146, 158113, 132145132741466054, 23, 29, 36, 52...124145132, 13831, 8259, 966068, 963, 512, 71, 72, 82, 84...60601387421, 135, 13931, 827421, 135, 13974601456015, 24, 112, 129, 14276604, 9, 29, 38, 80...60763, 574747456068, 966060, 81, 88, 95, 122...1327411, 89, 114, 120, 123150744, 23, 29, 36, 52...70677660607413, 19, 146, 158744, 9, 29, 38, 80...1324, 9, 29, 38, 80...746867


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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  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)
IgA:J-CHAIN:IgAComplexR-HSA-8858031 (Reactome)
IgH heavy chain V-III region VH26 precursor ProteinP01764 (Uniprot-TrEMBL)
JCHAIN ProteinP01591 (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-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 MetaboliteCHEBI:17627 (ChEBI)
heme b MetaboliteCHEBI:26355 (ChEBI)
heme bMetaboliteCHEBI:26355 (ChEBI)
heme bComplexR-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)
IgA:J-CHAIN: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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