PubMed:1657387 JSON TXT

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GlyCosmos6-Glycan-Motif-Image

Glycosmos6-MAT

{"project":"Glycosmos6-MAT","denotations":[{"id":"T1","span":{"begin":51,"end":56},"obj":"http://purl.obolibrary.org/obo/MAT_0000097"},{"id":"T2","span":{"begin":201,"end":206},"obj":"http://purl.obolibrary.org/obo/MAT_0000097"},{"id":"T3","span":{"begin":1024,"end":1029},"obj":"http://purl.obolibrary.org/obo/MAT_0000097"},{"id":"T4","span":{"begin":1476,"end":1481},"obj":"http://purl.obolibrary.org/obo/MAT_0000097"}],"text":"Participation of D-galactose-specific receptors of liver macrophages in recognition of fibronectin-opsonized particles.\nThe interaction of immobilized human or rat plasma fibronectin with isolated rat liver macrophages was studied in a model system using colloidal gold of 17-nm diameter (Au-17) as test particles. Plasma fibronectin (pFn)-coated gold particles were rapidly bound and endocytosed via the coated pit-coated vesicle pathway as demonstrated by photometry, and light and electron microscopy. The isolated macrophages bind 2.5 +/- 2 particles/10 microns of plasma membrane (incubation at 4 degrees), equalling a binding capacity of approximately 3.5 x 10(4) pFn-Au-17 particles per cell. Binding and uptake (at 37 degrees) was specifically inhibited by D-galactose-related carbohydrates, but not by D-mannose, N-acetyl-D-glucosamine, nor by excess soluble pFn. Uptake was also inhibited by lactosylated bovine serum albumin at a concentration of 10(-6) M but not by bovine serum albumin. India ink uptake by the liver macrophages in the presence of fibronectin was also inhibited by D-galactose-related monosaccharides. The presence of terminal, nonreducing D-galactosyl groups on pFn could be demonstrated by agglutination experiments with the D-galactose-specific plant lectin, Ricinus communis agglutinin (RCA), which could also be used for isolation of pFn from rat plasma. The 29-kDa molecular mass D-galactose-specific receptor, known to be expressed on the liver macrophage membrane and recently shown to be a membrane-bound form of C-reactive protein, was found to bind the pFn-coated gold particles in dot blotting experiments. It was concluded that the D-galactose-specific macrophage receptor binds to terminal D-galactose-related units of immobilized pFn and participates in recognition of fibronectin-opsonized particles."}

GlyCosmos6-Glycan-Motif-Structure

{"project":"GlyCosmos6-Glycan-Motif-Structure","denotations":[{"id":"T1","span":{"begin":19,"end":28},"obj":"https://glytoucan.org/Structures/Glycans/G65889KE"},{"id":"T2","span":{"begin":19,"end":28},"obj":"https://glytoucan.org/Structures/Glycans/G68158BT"},{"id":"T3","span":{"begin":767,"end":776},"obj":"https://glytoucan.org/Structures/Glycans/G65889KE"},{"id":"T4","span":{"begin":767,"end":776},"obj":"https://glytoucan.org/Structures/Glycans/G68158BT"},{"id":"T5","span":{"begin":813,"end":820},"obj":"https://glytoucan.org/Structures/Glycans/G70323CJ"},{"id":"T6","span":{"begin":1097,"end":1106},"obj":"https://glytoucan.org/Structures/Glycans/G65889KE"},{"id":"T7","span":{"begin":1097,"end":1106},"obj":"https://glytoucan.org/Structures/Glycans/G68158BT"},{"id":"T8","span":{"begin":1259,"end":1268},"obj":"https://glytoucan.org/Structures/Glycans/G65889KE"},{"id":"T9","span":{"begin":1259,"end":1268},"obj":"https://glytoucan.org/Structures/Glycans/G68158BT"},{"id":"T10","span":{"begin":1418,"end":1427},"obj":"https://glytoucan.org/Structures/Glycans/G65889KE"},{"id":"T11","span":{"begin":1418,"end":1427},"obj":"https://glytoucan.org/Structures/Glycans/G68158BT"},{"id":"T12","span":{"begin":1677,"end":1686},"obj":"https://glytoucan.org/Structures/Glycans/G65889KE"},{"id":"T13","span":{"begin":1677,"end":1686},"obj":"https://glytoucan.org/Structures/Glycans/G68158BT"},{"id":"T14","span":{"begin":1736,"end":1745},"obj":"https://glytoucan.org/Structures/Glycans/G65889KE"},{"id":"T15","span":{"begin":1736,"end":1745},"obj":"https://glytoucan.org/Structures/Glycans/G68158BT"}],"text":"Participation of D-galactose-specific receptors of liver macrophages in recognition of fibronectin-opsonized particles.\nThe interaction of immobilized human or rat plasma fibronectin with isolated rat liver macrophages was studied in a model system using colloidal gold of 17-nm diameter (Au-17) as test particles. Plasma fibronectin (pFn)-coated gold particles were rapidly bound and endocytosed via the coated pit-coated vesicle pathway as demonstrated by photometry, and light and electron microscopy. The isolated macrophages bind 2.5 +/- 2 particles/10 microns of plasma membrane (incubation at 4 degrees), equalling a binding capacity of approximately 3.5 x 10(4) pFn-Au-17 particles per cell. Binding and uptake (at 37 degrees) was specifically inhibited by D-galactose-related carbohydrates, but not by D-mannose, N-acetyl-D-glucosamine, nor by excess soluble pFn. Uptake was also inhibited by lactosylated bovine serum albumin at a concentration of 10(-6) M but not by bovine serum albumin. India ink uptake by the liver macrophages in the presence of fibronectin was also inhibited by D-galactose-related monosaccharides. The presence of terminal, nonreducing D-galactosyl groups on pFn could be demonstrated by agglutination experiments with the D-galactose-specific plant lectin, Ricinus communis agglutinin (RCA), which could also be used for isolation of pFn from rat plasma. The 29-kDa molecular mass D-galactose-specific receptor, known to be expressed on the liver macrophage membrane and recently shown to be a membrane-bound form of C-reactive protein, was found to bind the pFn-coated gold particles in dot blotting experiments. It was concluded that the D-galactose-specific macrophage receptor binds to terminal D-galactose-related units of immobilized pFn and participates in recognition of fibronectin-opsonized particles."}

sentences

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Anatomy-MAT

{"project":"Anatomy-MAT","denotations":[{"id":"T1","span":{"begin":51,"end":56},"obj":"Body_part"},{"id":"T2","span":{"begin":201,"end":206},"obj":"Body_part"},{"id":"T3","span":{"begin":1024,"end":1029},"obj":"Body_part"},{"id":"T4","span":{"begin":1476,"end":1481},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"mat_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MAT_0000097"},{"id":"A2","pred":"mat_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/MAT_0000097"},{"id":"A3","pred":"mat_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/MAT_0000097"},{"id":"A4","pred":"mat_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/MAT_0000097"}],"text":"Participation of D-galactose-specific receptors of liver macrophages in recognition of fibronectin-opsonized particles.\nThe interaction of immobilized human or rat plasma fibronectin with isolated rat liver macrophages was studied in a model system using colloidal gold of 17-nm diameter (Au-17) as test particles. Plasma fibronectin (pFn)-coated gold particles were rapidly bound and endocytosed via the coated pit-coated vesicle pathway as demonstrated by photometry, and light and electron microscopy. The isolated macrophages bind 2.5 +/- 2 particles/10 microns of plasma membrane (incubation at 4 degrees), equalling a binding capacity of approximately 3.5 x 10(4) pFn-Au-17 particles per cell. Binding and uptake (at 37 degrees) was specifically inhibited by D-galactose-related carbohydrates, but not by D-mannose, N-acetyl-D-glucosamine, nor by excess soluble pFn. Uptake was also inhibited by lactosylated bovine serum albumin at a concentration of 10(-6) M but not by bovine serum albumin. India ink uptake by the liver macrophages in the presence of fibronectin was also inhibited by D-galactose-related monosaccharides. The presence of terminal, nonreducing D-galactosyl groups on pFn could be demonstrated by agglutination experiments with the D-galactose-specific plant lectin, Ricinus communis agglutinin (RCA), which could also be used for isolation of pFn from rat plasma. The 29-kDa molecular mass D-galactose-specific receptor, known to be expressed on the liver macrophage membrane and recently shown to be a membrane-bound form of C-reactive protein, was found to bind the pFn-coated gold particles in dot blotting experiments. It was concluded that the D-galactose-specific macrophage receptor binds to terminal D-galactose-related units of immobilized pFn and participates in recognition of fibronectin-opsonized particles."}

NCBITAXON

{"project":"NCBITAXON","denotations":[{"id":"T1","span":{"begin":151,"end":156},"obj":"OrganismTaxon"},{"id":"T2","span":{"begin":160,"end":163},"obj":"OrganismTaxon"},{"id":"T4","span":{"begin":197,"end":200},"obj":"OrganismTaxon"},{"id":"T6","span":{"begin":915,"end":921},"obj":"OrganismTaxon"},{"id":"T7","span":{"begin":978,"end":984},"obj":"OrganismTaxon"},{"id":"T8","span":{"begin":1292,"end":1308},"obj":"OrganismTaxon"},{"id":"T9","span":{"begin":1378,"end":1381},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"9606"},{"id":"A2","pred":"db_id","subj":"T2","obj":"10114"},{"id":"A3","pred":"db_id","subj":"T2","obj":"10116"},{"id":"A4","pred":"db_id","subj":"T4","obj":"10114"},{"id":"A5","pred":"db_id","subj":"T4","obj":"10116"},{"id":"A6","pred":"db_id","subj":"T6","obj":"9913"},{"id":"A7","pred":"db_id","subj":"T7","obj":"9913"},{"id":"A8","pred":"db_id","subj":"T8","obj":"3988"},{"id":"A9","pred":"db_id","subj":"T9","obj":"10114"},{"id":"A10","pred":"db_id","subj":"T9","obj":"10116"}],"text":"Participation of D-galactose-specific receptors of liver macrophages in recognition of fibronectin-opsonized particles.\nThe interaction of immobilized human or rat plasma fibronectin with isolated rat liver macrophages was studied in a model system using colloidal gold of 17-nm diameter (Au-17) as test particles. Plasma fibronectin (pFn)-coated gold particles were rapidly bound and endocytosed via the coated pit-coated vesicle pathway as demonstrated by photometry, and light and electron microscopy. The isolated macrophages bind 2.5 +/- 2 particles/10 microns of plasma membrane (incubation at 4 degrees), equalling a binding capacity of approximately 3.5 x 10(4) pFn-Au-17 particles per cell. Binding and uptake (at 37 degrees) was specifically inhibited by D-galactose-related carbohydrates, but not by D-mannose, N-acetyl-D-glucosamine, nor by excess soluble pFn. Uptake was also inhibited by lactosylated bovine serum albumin at a concentration of 10(-6) M but not by bovine serum albumin. India ink uptake by the liver macrophages in the presence of fibronectin was also inhibited by D-galactose-related monosaccharides. The presence of terminal, nonreducing D-galactosyl groups on pFn could be demonstrated by agglutination experiments with the D-galactose-specific plant lectin, Ricinus communis agglutinin (RCA), which could also be used for isolation of pFn from rat plasma. The 29-kDa molecular mass D-galactose-specific receptor, known to be expressed on the liver macrophage membrane and recently shown to be a membrane-bound form of C-reactive protein, was found to bind the pFn-coated gold particles in dot blotting experiments. It was concluded that the D-galactose-specific macrophage receptor binds to terminal D-galactose-related units of immobilized pFn and participates in recognition of fibronectin-opsonized particles."}

Anatomy-UBERON

CL-cell

{"project":"CL-cell","denotations":[{"id":"T1","span":{"begin":51,"end":68},"obj":"Cell"},{"id":"T2","span":{"begin":201,"end":218},"obj":"Cell"},{"id":"T3","span":{"begin":518,"end":529},"obj":"Cell"},{"id":"T5","span":{"begin":1024,"end":1041},"obj":"Cell"},{"id":"T6","span":{"begin":1476,"end":1492},"obj":"Cell"},{"id":"T7","span":{"begin":1482,"end":1492},"obj":"Cell"},{"id":"T9","span":{"begin":1696,"end":1706},"obj":"Cell"}],"attributes":[{"id":"A1","pred":"cl_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CL:0000091"},{"id":"A2","pred":"cl_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/CL:0000091"},{"id":"A3","pred":"cl_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/CL:0000235"},{"id":"A4","pred":"cl_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/CL:0000394"},{"id":"A5","pred":"cl_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/CL:0000091"},{"id":"A6","pred":"cl_id","subj":"T6","obj":"http://purl.obolibrary.org/obo/CL:0000091"},{"id":"A7","pred":"cl_id","subj":"T7","obj":"http://purl.obolibrary.org/obo/CL:0000235"},{"id":"A8","pred":"cl_id","subj":"T7","obj":"http://purl.obolibrary.org/obo/CL:0000394"},{"id":"A9","pred":"cl_id","subj":"T9","obj":"http://purl.obolibrary.org/obo/CL:0000235"},{"id":"A10","pred":"cl_id","subj":"T9","obj":"http://purl.obolibrary.org/obo/CL:0000394"}],"text":"Participation of D-galactose-specific receptors of liver macrophages in recognition of fibronectin-opsonized particles.\nThe interaction of immobilized human or rat plasma fibronectin with isolated rat liver macrophages was studied in a model system using colloidal gold of 17-nm diameter (Au-17) as test particles. Plasma fibronectin (pFn)-coated gold particles were rapidly bound and endocytosed via the coated pit-coated vesicle pathway as demonstrated by photometry, and light and electron microscopy. The isolated macrophages bind 2.5 +/- 2 particles/10 microns of plasma membrane (incubation at 4 degrees), equalling a binding capacity of approximately 3.5 x 10(4) pFn-Au-17 particles per cell. Binding and uptake (at 37 degrees) was specifically inhibited by D-galactose-related carbohydrates, but not by D-mannose, N-acetyl-D-glucosamine, nor by excess soluble pFn. Uptake was also inhibited by lactosylated bovine serum albumin at a concentration of 10(-6) M but not by bovine serum albumin. India ink uptake by the liver macrophages in the presence of fibronectin was also inhibited by D-galactose-related monosaccharides. The presence of terminal, nonreducing D-galactosyl groups on pFn could be demonstrated by agglutination experiments with the D-galactose-specific plant lectin, Ricinus communis agglutinin (RCA), which could also be used for isolation of pFn from rat plasma. The 29-kDa molecular mass D-galactose-specific receptor, known to be expressed on the liver macrophage membrane and recently shown to be a membrane-bound form of C-reactive protein, was found to bind the pFn-coated gold particles in dot blotting experiments. It was concluded that the D-galactose-specific macrophage receptor binds to terminal D-galactose-related units of immobilized pFn and participates in recognition of fibronectin-opsonized particles."}