Search results for MSR1

Showing 13 results out of 13

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Species

Types

Compartments

Reaction types

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Protein (2 results from a total of 2)

Identifier: R-HSA-2173717
Species: Homo sapiens
Compartment: plasma membrane
Primary external reference: UniProt: MSR1: P21757
Identifier: R-HSA-2507846
Species: Homo sapiens
Compartment: endocytic vesicle membrane
Primary external reference: UniProt: MSR1: P21757

Set (2 results from a total of 2)

Identifier: R-HSA-2173760
Species: Homo sapiens
Compartment: extracellular region
Identifier: R-HSA-2507844
Species: Homo sapiens
Compartment: endocytic vesicle lumen

Complex (5 results from a total of 5)

Identifier: R-HSA-2173771
Species: Homo sapiens
Compartment: plasma membrane
Identifier: R-HSA-2507852
Species: Homo sapiens
Compartment: endocytic vesicle membrane
Identifier: R-HSA-2173774
Species: Homo sapiens
Compartment: plasma membrane
Identifier: R-HSA-2507847
Species: Homo sapiens
Compartment: endocytic vesicle membrane
Identifier: R-HSA-3221871
Species: Homo sapiens
Compartment: extracellular region

Reaction (4 results from a total of 4)

Identifier: R-HSA-3221843
Species: Homo sapiens
Compartment: extracellular region, plasma membrane
As inferred from mouse, MSR1 (SCARA1) binds denatured collagen I, denatured collagen III, and nondenatured or glycated collagen IV.
Identifier: R-HSA-2173778
Species: Homo sapiens
Compartment: extracellular region, plasma membrane
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.
Identifier: R-HSA-2507854
Species: Homo sapiens
Compartment: endocytic vesicle membrane, plasma membrane
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).
Identifier: R-HSA-2173781
Species: Homo sapiens
Compartment: extracellular region, plasma membrane
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.
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