PubMed:12881409 JSON TXT

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GlyCosmos600-CLO

{"project":"GlyCosmos600-CLO","denotations":[{"id":"T1","span":{"begin":646,"end":650},"obj":"http://purl.obolibrary.org/obo/GO_0005623"}],"text":"Galectin-8 modulates neutrophil function via interaction with integrin alphaM.\nThe members of the galectin family are associated with diverse cellular events, including immune response. We investigated the effects of galectin-8 on neutrophil function. Human galectin-8 induced firm and reversible adhesion of peripheral blood neutrophils but not eosinophils to a plastic surface in a lactose-sensitive manner. Other human galectins, galectins-1, -3, and -9, showed low or negligible effects on neutrophil adhesion. Confocal microscopy revealed actin bundle formation in the presence of galectin-8. Cytochalasins inhibited both actin assembly and cell adhesion induced by galectin-8. Affinity purification of galectin-interacting proteins from solubilized neutrophil membrane revealed that N-terminal carbohydrate recognition domain (CRD) of galectin-8 bound promatrix metalloproteinase-9 (proMMP-9), and C-terminal CRD bound integrin alphaM/CD11b and proMMP-9. A mutant galectin-8 lacking the carbohydrate-binding activity of N-terminal CRD (galectin-8R69H) retained adhesion-inducing activity, but inactivation of C-terminal CRD (galectin-8R233H) abolished the activity. MMP-3-mediated processing of proMMP-9 was accelerated by galectin-8, and this effect was inhibited by lactose. Galectins-1 and -3 did not affect the processing. Superoxide production, an essential event in bactericidal function of neutrophils, was stimulated by galectin-8 to an extent comparable to that induced by fMLP. Galectin-8R69H but not galectin-8R233H could stimulate superoxide production. Taken together, these results suggest that galectin-8 is a novel factor that modulates the neutrophil function related to transendothelial migration and microbial killing."}

sentences

{"project":"sentences","denotations":[{"id":"TextSentencer_T1","span":{"begin":0,"end":78},"obj":"Sentence"},{"id":"TextSentencer_T2","span":{"begin":79,"end":185},"obj":"Sentence"},{"id":"TextSentencer_T3","span":{"begin":186,"end":251},"obj":"Sentence"},{"id":"TextSentencer_T4","span":{"begin":252,"end":409},"obj":"Sentence"},{"id":"TextSentencer_T5","span":{"begin":410,"end":514},"obj":"Sentence"},{"id":"TextSentencer_T6","span":{"begin":515,"end":597},"obj":"Sentence"},{"id":"TextSentencer_T7","span":{"begin":598,"end":682},"obj":"Sentence"},{"id":"TextSentencer_T8","span":{"begin":683,"end":960},"obj":"Sentence"},{"id":"TextSentencer_T9","span":{"begin":961,"end":1171},"obj":"Sentence"},{"id":"TextSentencer_T10","span":{"begin":1172,"end":1282},"obj":"Sentence"},{"id":"TextSentencer_T11","span":{"begin":1283,"end":1332},"obj":"Sentence"},{"id":"TextSentencer_T12","span":{"begin":1333,"end":1493},"obj":"Sentence"},{"id":"TextSentencer_T13","span":{"begin":1494,"end":1571},"obj":"Sentence"},{"id":"TextSentencer_T14","span":{"begin":1572,"end":1743},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":78},"obj":"Sentence"},{"id":"T2","span":{"begin":79,"end":185},"obj":"Sentence"},{"id":"T3","span":{"begin":186,"end":251},"obj":"Sentence"},{"id":"T4","span":{"begin":252,"end":409},"obj":"Sentence"},{"id":"T5","span":{"begin":410,"end":514},"obj":"Sentence"},{"id":"T6","span":{"begin":515,"end":597},"obj":"Sentence"},{"id":"T7","span":{"begin":598,"end":682},"obj":"Sentence"},{"id":"T8","span":{"begin":683,"end":960},"obj":"Sentence"},{"id":"T9","span":{"begin":961,"end":1171},"obj":"Sentence"},{"id":"T10","span":{"begin":1172,"end":1282},"obj":"Sentence"},{"id":"T11","span":{"begin":1283,"end":1332},"obj":"Sentence"},{"id":"T12","span":{"begin":1333,"end":1493},"obj":"Sentence"},{"id":"T13","span":{"begin":1494,"end":1571},"obj":"Sentence"},{"id":"T14","span":{"begin":1572,"end":1743},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Galectin-8 modulates neutrophil function via interaction with integrin alphaM.\nThe members of the galectin family are associated with diverse cellular events, including immune response. We investigated the effects of galectin-8 on neutrophil function. Human galectin-8 induced firm and reversible adhesion of peripheral blood neutrophils but not eosinophils to a plastic surface in a lactose-sensitive manner. Other human galectins, galectins-1, -3, and -9, showed low or negligible effects on neutrophil adhesion. Confocal microscopy revealed actin bundle formation in the presence of galectin-8. Cytochalasins inhibited both actin assembly and cell adhesion induced by galectin-8. Affinity purification of galectin-interacting proteins from solubilized neutrophil membrane revealed that N-terminal carbohydrate recognition domain (CRD) of galectin-8 bound promatrix metalloproteinase-9 (proMMP-9), and C-terminal CRD bound integrin alphaM/CD11b and proMMP-9. A mutant galectin-8 lacking the carbohydrate-binding activity of N-terminal CRD (galectin-8R69H) retained adhesion-inducing activity, but inactivation of C-terminal CRD (galectin-8R233H) abolished the activity. MMP-3-mediated processing of proMMP-9 was accelerated by galectin-8, and this effect was inhibited by lactose. Galectins-1 and -3 did not affect the processing. Superoxide production, an essential event in bactericidal function of neutrophils, was stimulated by galectin-8 to an extent comparable to that induced by fMLP. Galectin-8R69H but not galectin-8R233H could stimulate superoxide production. Taken together, these results suggest that galectin-8 is a novel factor that modulates the neutrophil function related to transendothelial migration and microbial killing."}

Glycosmos6-MAT

{"project":"Glycosmos6-MAT","denotations":[{"id":"T1","span":{"begin":320,"end":325},"obj":"http://purl.obolibrary.org/obo/MAT_0000083"},{"id":"T2","span":{"begin":320,"end":325},"obj":"http://purl.obolibrary.org/obo/MAT_0000315"}],"text":"Galectin-8 modulates neutrophil function via interaction with integrin alphaM.\nThe members of the galectin family are associated with diverse cellular events, including immune response. We investigated the effects of galectin-8 on neutrophil function. Human galectin-8 induced firm and reversible adhesion of peripheral blood neutrophils but not eosinophils to a plastic surface in a lactose-sensitive manner. Other human galectins, galectins-1, -3, and -9, showed low or negligible effects on neutrophil adhesion. Confocal microscopy revealed actin bundle formation in the presence of galectin-8. Cytochalasins inhibited both actin assembly and cell adhesion induced by galectin-8. Affinity purification of galectin-interacting proteins from solubilized neutrophil membrane revealed that N-terminal carbohydrate recognition domain (CRD) of galectin-8 bound promatrix metalloproteinase-9 (proMMP-9), and C-terminal CRD bound integrin alphaM/CD11b and proMMP-9. A mutant galectin-8 lacking the carbohydrate-binding activity of N-terminal CRD (galectin-8R69H) retained adhesion-inducing activity, but inactivation of C-terminal CRD (galectin-8R233H) abolished the activity. MMP-3-mediated processing of proMMP-9 was accelerated by galectin-8, and this effect was inhibited by lactose. Galectins-1 and -3 did not affect the processing. Superoxide production, an essential event in bactericidal function of neutrophils, was stimulated by galectin-8 to an extent comparable to that induced by fMLP. Galectin-8R69H but not galectin-8R233H could stimulate superoxide production. Taken together, these results suggest that galectin-8 is a novel factor that modulates the neutrophil function related to transendothelial migration and microbial killing."}

GlycoBiology-FMA

uniprot-human

{"project":"uniprot-human","denotations":[{"id":"T1","span":{"begin":0,"end":10},"obj":"http://www.uniprot.org/uniprot/Q9H585"},{"id":"T2","span":{"begin":217,"end":227},"obj":"http://www.uniprot.org/uniprot/Q9H585"},{"id":"T3","span":{"begin":258,"end":268},"obj":"http://www.uniprot.org/uniprot/Q9H585"},{"id":"T4","span":{"begin":586,"end":596},"obj":"http://www.uniprot.org/uniprot/Q9H585"},{"id":"T5","span":{"begin":671,"end":681},"obj":"http://www.uniprot.org/uniprot/Q9H585"},{"id":"T6","span":{"begin":841,"end":851},"obj":"http://www.uniprot.org/uniprot/Q9H585"},{"id":"T7","span":{"begin":970,"end":980},"obj":"http://www.uniprot.org/uniprot/Q9H585"},{"id":"T8","span":{"begin":1229,"end":1239},"obj":"http://www.uniprot.org/uniprot/Q9H585"},{"id":"T9","span":{"begin":1434,"end":1444},"obj":"http://www.uniprot.org/uniprot/Q9H585"},{"id":"T10","span":{"begin":1615,"end":1625},"obj":"http://www.uniprot.org/uniprot/Q9H585"},{"id":"T11","span":{"begin":433,"end":444},"obj":"http://www.uniprot.org/uniprot/P09382"},{"id":"T12","span":{"begin":1283,"end":1294},"obj":"http://www.uniprot.org/uniprot/P09382"},{"id":"T13","span":{"begin":941,"end":946},"obj":"http://www.uniprot.org/uniprot/P11215"},{"id":"T14","span":{"begin":1172,"end":1177},"obj":"http://www.uniprot.org/uniprot/P08254"}],"text":"Galectin-8 modulates neutrophil function via interaction with integrin alphaM.\nThe members of the galectin family are associated with diverse cellular events, including immune response. We investigated the effects of galectin-8 on neutrophil function. Human galectin-8 induced firm and reversible adhesion of peripheral blood neutrophils but not eosinophils to a plastic surface in a lactose-sensitive manner. Other human galectins, galectins-1, -3, and -9, showed low or negligible effects on neutrophil adhesion. Confocal microscopy revealed actin bundle formation in the presence of galectin-8. Cytochalasins inhibited both actin assembly and cell adhesion induced by galectin-8. Affinity purification of galectin-interacting proteins from solubilized neutrophil membrane revealed that N-terminal carbohydrate recognition domain (CRD) of galectin-8 bound promatrix metalloproteinase-9 (proMMP-9), and C-terminal CRD bound integrin alphaM/CD11b and proMMP-9. A mutant galectin-8 lacking the carbohydrate-binding activity of N-terminal CRD (galectin-8R69H) retained adhesion-inducing activity, but inactivation of C-terminal CRD (galectin-8R233H) abolished the activity. MMP-3-mediated processing of proMMP-9 was accelerated by galectin-8, and this effect was inhibited by lactose. Galectins-1 and -3 did not affect the processing. Superoxide production, an essential event in bactericidal function of neutrophils, was stimulated by galectin-8 to an extent comparable to that induced by fMLP. Galectin-8R69H but not galectin-8R233H could stimulate superoxide production. Taken together, these results suggest that galectin-8 is a novel factor that modulates the neutrophil function related to transendothelial migration and microbial killing."}

uniprot-mouse

{"project":"uniprot-mouse","denotations":[{"id":"T1","span":{"begin":0,"end":10},"obj":"http://www.uniprot.org/uniprot/Q9JL15"},{"id":"T2","span":{"begin":217,"end":227},"obj":"http://www.uniprot.org/uniprot/Q9JL15"},{"id":"T3","span":{"begin":258,"end":268},"obj":"http://www.uniprot.org/uniprot/Q9JL15"},{"id":"T4","span":{"begin":586,"end":596},"obj":"http://www.uniprot.org/uniprot/Q9JL15"},{"id":"T5","span":{"begin":671,"end":681},"obj":"http://www.uniprot.org/uniprot/Q9JL15"},{"id":"T6","span":{"begin":841,"end":851},"obj":"http://www.uniprot.org/uniprot/Q9JL15"},{"id":"T7","span":{"begin":970,"end":980},"obj":"http://www.uniprot.org/uniprot/Q9JL15"},{"id":"T8","span":{"begin":1229,"end":1239},"obj":"http://www.uniprot.org/uniprot/Q9JL15"},{"id":"T9","span":{"begin":1434,"end":1444},"obj":"http://www.uniprot.org/uniprot/Q9JL15"},{"id":"T10","span":{"begin":1615,"end":1625},"obj":"http://www.uniprot.org/uniprot/Q9JL15"},{"id":"T11","span":{"begin":433,"end":444},"obj":"http://www.uniprot.org/uniprot/P16045"},{"id":"T12","span":{"begin":1283,"end":1294},"obj":"http://www.uniprot.org/uniprot/P16045"},{"id":"T13","span":{"begin":941,"end":946},"obj":"http://www.uniprot.org/uniprot/P05555"},{"id":"T14","span":{"begin":1172,"end":1177},"obj":"http://www.uniprot.org/uniprot/P28862"}],"text":"Galectin-8 modulates neutrophil function via interaction with integrin alphaM.\nThe members of the galectin family are associated with diverse cellular events, including immune response. We investigated the effects of galectin-8 on neutrophil function. Human galectin-8 induced firm and reversible adhesion of peripheral blood neutrophils but not eosinophils to a plastic surface in a lactose-sensitive manner. Other human galectins, galectins-1, -3, and -9, showed low or negligible effects on neutrophil adhesion. Confocal microscopy revealed actin bundle formation in the presence of galectin-8. Cytochalasins inhibited both actin assembly and cell adhesion induced by galectin-8. Affinity purification of galectin-interacting proteins from solubilized neutrophil membrane revealed that N-terminal carbohydrate recognition domain (CRD) of galectin-8 bound promatrix metalloproteinase-9 (proMMP-9), and C-terminal CRD bound integrin alphaM/CD11b and proMMP-9. A mutant galectin-8 lacking the carbohydrate-binding activity of N-terminal CRD (galectin-8R69H) retained adhesion-inducing activity, but inactivation of C-terminal CRD (galectin-8R233H) abolished the activity. MMP-3-mediated processing of proMMP-9 was accelerated by galectin-8, and this effect was inhibited by lactose. Galectins-1 and -3 did not affect the processing. Superoxide production, an essential event in bactericidal function of neutrophils, was stimulated by galectin-8 to an extent comparable to that induced by fMLP. Galectin-8R69H but not galectin-8R233H could stimulate superoxide production. Taken together, these results suggest that galectin-8 is a novel factor that modulates the neutrophil function related to transendothelial migration and microbial killing."}

GlycoBiology-NCBITAXON

{"project":"GlycoBiology-NCBITAXON","denotations":[{"id":"T1","span":{"begin":151,"end":157},"obj":"http://purl.bioontology.org/ontology/STY/T051"},{"id":"T2","span":{"begin":1369,"end":1374},"obj":"http://purl.bioontology.org/ontology/STY/T051"},{"id":"T3","span":{"begin":1683,"end":1690},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/353209"}],"text":"Galectin-8 modulates neutrophil function via interaction with integrin alphaM.\nThe members of the galectin family are associated with diverse cellular events, including immune response. We investigated the effects of galectin-8 on neutrophil function. Human galectin-8 induced firm and reversible adhesion of peripheral blood neutrophils but not eosinophils to a plastic surface in a lactose-sensitive manner. Other human galectins, galectins-1, -3, and -9, showed low or negligible effects on neutrophil adhesion. Confocal microscopy revealed actin bundle formation in the presence of galectin-8. Cytochalasins inhibited both actin assembly and cell adhesion induced by galectin-8. Affinity purification of galectin-interacting proteins from solubilized neutrophil membrane revealed that N-terminal carbohydrate recognition domain (CRD) of galectin-8 bound promatrix metalloproteinase-9 (proMMP-9), and C-terminal CRD bound integrin alphaM/CD11b and proMMP-9. A mutant galectin-8 lacking the carbohydrate-binding activity of N-terminal CRD (galectin-8R69H) retained adhesion-inducing activity, but inactivation of C-terminal CRD (galectin-8R233H) abolished the activity. MMP-3-mediated processing of proMMP-9 was accelerated by galectin-8, and this effect was inhibited by lactose. Galectins-1 and -3 did not affect the processing. Superoxide production, an essential event in bactericidal function of neutrophils, was stimulated by galectin-8 to an extent comparable to that induced by fMLP. Galectin-8R69H but not galectin-8R233H could stimulate superoxide production. Taken together, these results suggest that galectin-8 is a novel factor that modulates the neutrophil function related to transendothelial migration and microbial killing."}

GO-BP

{"project":"GO-BP","denotations":[{"id":"T1","span":{"begin":142,"end":150},"obj":"http://purl.obolibrary.org/obo/GO_0007349"},{"id":"T2","span":{"begin":169,"end":184},"obj":"http://purl.obolibrary.org/obo/GO_0006955"},{"id":"T3","span":{"begin":392,"end":401},"obj":"http://purl.obolibrary.org/obo/GO_0046960"},{"id":"T4","span":{"begin":544,"end":556},"obj":"http://purl.obolibrary.org/obo/GO_0051764"},{"id":"T5","span":{"begin":557,"end":566},"obj":"http://purl.obolibrary.org/obo/GO_0009058"},{"id":"T6","span":{"begin":646,"end":659},"obj":"http://purl.obolibrary.org/obo/GO_0007155"},{"id":"T7","span":{"begin":1006,"end":1022},"obj":"http://purl.obolibrary.org/obo/GO_0051099"},{"id":"T8","span":{"begin":1014,"end":1036},"obj":"http://purl.obolibrary.org/obo/GO_0061607"}],"text":"Galectin-8 modulates neutrophil function via interaction with integrin alphaM.\nThe members of the galectin family are associated with diverse cellular events, including immune response. We investigated the effects of galectin-8 on neutrophil function. Human galectin-8 induced firm and reversible adhesion of peripheral blood neutrophils but not eosinophils to a plastic surface in a lactose-sensitive manner. Other human galectins, galectins-1, -3, and -9, showed low or negligible effects on neutrophil adhesion. Confocal microscopy revealed actin bundle formation in the presence of galectin-8. Cytochalasins inhibited both actin assembly and cell adhesion induced by galectin-8. Affinity purification of galectin-interacting proteins from solubilized neutrophil membrane revealed that N-terminal carbohydrate recognition domain (CRD) of galectin-8 bound promatrix metalloproteinase-9 (proMMP-9), and C-terminal CRD bound integrin alphaM/CD11b and proMMP-9. A mutant galectin-8 lacking the carbohydrate-binding activity of N-terminal CRD (galectin-8R69H) retained adhesion-inducing activity, but inactivation of C-terminal CRD (galectin-8R233H) abolished the activity. MMP-3-mediated processing of proMMP-9 was accelerated by galectin-8, and this effect was inhibited by lactose. Galectins-1 and -3 did not affect the processing. Superoxide production, an essential event in bactericidal function of neutrophils, was stimulated by galectin-8 to an extent comparable to that induced by fMLP. Galectin-8R69H but not galectin-8R233H could stimulate superoxide production. Taken together, these results suggest that galectin-8 is a novel factor that modulates the neutrophil function related to transendothelial migration and microbial killing."}

GO-MF

{"project":"GO-MF","denotations":[{"id":"T1","span":{"begin":993,"end":1013},"obj":"http://purl.obolibrary.org/obo/GO_0030246"},{"id":"T2","span":{"begin":1006,"end":1013},"obj":"http://purl.obolibrary.org/obo/GO_0070026"},{"id":"T3","span":{"begin":1006,"end":1013},"obj":"http://purl.obolibrary.org/obo/GO_0003680"},{"id":"T4","span":{"begin":1006,"end":1013},"obj":"http://purl.obolibrary.org/obo/GO_0017091"},{"id":"T5","span":{"begin":1006,"end":1013},"obj":"http://purl.obolibrary.org/obo/GO_0005488"}],"text":"Galectin-8 modulates neutrophil function via interaction with integrin alphaM.\nThe members of the galectin family are associated with diverse cellular events, including immune response. We investigated the effects of galectin-8 on neutrophil function. Human galectin-8 induced firm and reversible adhesion of peripheral blood neutrophils but not eosinophils to a plastic surface in a lactose-sensitive manner. Other human galectins, galectins-1, -3, and -9, showed low or negligible effects on neutrophil adhesion. Confocal microscopy revealed actin bundle formation in the presence of galectin-8. Cytochalasins inhibited both actin assembly and cell adhesion induced by galectin-8. Affinity purification of galectin-interacting proteins from solubilized neutrophil membrane revealed that N-terminal carbohydrate recognition domain (CRD) of galectin-8 bound promatrix metalloproteinase-9 (proMMP-9), and C-terminal CRD bound integrin alphaM/CD11b and proMMP-9. A mutant galectin-8 lacking the carbohydrate-binding activity of N-terminal CRD (galectin-8R69H) retained adhesion-inducing activity, but inactivation of C-terminal CRD (galectin-8R233H) abolished the activity. MMP-3-mediated processing of proMMP-9 was accelerated by galectin-8, and this effect was inhibited by lactose. Galectins-1 and -3 did not affect the processing. Superoxide production, an essential event in bactericidal function of neutrophils, was stimulated by galectin-8 to an extent comparable to that induced by fMLP. Galectin-8R69H but not galectin-8R233H could stimulate superoxide production. Taken together, these results suggest that galectin-8 is a novel factor that modulates the neutrophil function related to transendothelial migration and microbial killing."}

GO-CC

{"project":"GO-CC","denotations":[{"id":"T1","span":{"begin":646,"end":650},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T2","span":{"begin":766,"end":774},"obj":"http://purl.obolibrary.org/obo/GO_0016020"}],"text":"Galectin-8 modulates neutrophil function via interaction with integrin alphaM.\nThe members of the galectin family are associated with diverse cellular events, including immune response. We investigated the effects of galectin-8 on neutrophil function. Human galectin-8 induced firm and reversible adhesion of peripheral blood neutrophils but not eosinophils to a plastic surface in a lactose-sensitive manner. Other human galectins, galectins-1, -3, and -9, showed low or negligible effects on neutrophil adhesion. Confocal microscopy revealed actin bundle formation in the presence of galectin-8. Cytochalasins inhibited both actin assembly and cell adhesion induced by galectin-8. Affinity purification of galectin-interacting proteins from solubilized neutrophil membrane revealed that N-terminal carbohydrate recognition domain (CRD) of galectin-8 bound promatrix metalloproteinase-9 (proMMP-9), and C-terminal CRD bound integrin alphaM/CD11b and proMMP-9. A mutant galectin-8 lacking the carbohydrate-binding activity of N-terminal CRD (galectin-8R69H) retained adhesion-inducing activity, but inactivation of C-terminal CRD (galectin-8R233H) abolished the activity. MMP-3-mediated processing of proMMP-9 was accelerated by galectin-8, and this effect was inhibited by lactose. Galectins-1 and -3 did not affect the processing. Superoxide production, an essential event in bactericidal function of neutrophils, was stimulated by galectin-8 to an extent comparable to that induced by fMLP. Galectin-8R69H but not galectin-8R233H could stimulate superoxide production. Taken together, these results suggest that galectin-8 is a novel factor that modulates the neutrophil function related to transendothelial migration and microbial killing."}

UBERON-AE

{"project":"UBERON-AE","denotations":[{"id":"T1","span":{"begin":320,"end":325},"obj":"http://purl.obolibrary.org/obo/UBERON_0000178"}],"text":"Galectin-8 modulates neutrophil function via interaction with integrin alphaM.\nThe members of the galectin family are associated with diverse cellular events, including immune response. We investigated the effects of galectin-8 on neutrophil function. Human galectin-8 induced firm and reversible adhesion of peripheral blood neutrophils but not eosinophils to a plastic surface in a lactose-sensitive manner. Other human galectins, galectins-1, -3, and -9, showed low or negligible effects on neutrophil adhesion. Confocal microscopy revealed actin bundle formation in the presence of galectin-8. Cytochalasins inhibited both actin assembly and cell adhesion induced by galectin-8. Affinity purification of galectin-interacting proteins from solubilized neutrophil membrane revealed that N-terminal carbohydrate recognition domain (CRD) of galectin-8 bound promatrix metalloproteinase-9 (proMMP-9), and C-terminal CRD bound integrin alphaM/CD11b and proMMP-9. A mutant galectin-8 lacking the carbohydrate-binding activity of N-terminal CRD (galectin-8R69H) retained adhesion-inducing activity, but inactivation of C-terminal CRD (galectin-8R233H) abolished the activity. MMP-3-mediated processing of proMMP-9 was accelerated by galectin-8, and this effect was inhibited by lactose. Galectins-1 and -3 did not affect the processing. Superoxide production, an essential event in bactericidal function of neutrophils, was stimulated by galectin-8 to an extent comparable to that induced by fMLP. Galectin-8R69H but not galectin-8R233H could stimulate superoxide production. Taken together, these results suggest that galectin-8 is a novel factor that modulates the neutrophil function related to transendothelial migration and microbial killing."}

EDAM-topics

{"project":"EDAM-topics","denotations":[{"id":"T1","span":{"begin":45,"end":56},"obj":"http://edamontology.org/topic_0602"},{"id":"T2","span":{"begin":252,"end":257},"obj":"http://edamontology.org/topic_2815"},{"id":"T3","span":{"begin":416,"end":421},"obj":"http://edamontology.org/topic_2815"},{"id":"T4","span":{"begin":524,"end":534},"obj":"http://edamontology.org/topic_3382"},{"id":"T5","span":{"begin":633,"end":641},"obj":"http://edamontology.org/topic_0196"},{"id":"T6","span":{"begin":717,"end":728},"obj":"http://edamontology.org/topic_0602"},{"id":"T7","span":{"begin":729,"end":737},"obj":"http://edamontology.org/topic_0078"},{"id":"T8","span":{"begin":791,"end":799},"obj":"http://edamontology.org/topic_0749"},{"id":"T9","span":{"begin":800,"end":812},"obj":"http://edamontology.org/topic_0152"},{"id":"T10","span":{"begin":906,"end":914},"obj":"http://edamontology.org/topic_0749"},{"id":"T11","span":{"begin":993,"end":1005},"obj":"http://edamontology.org/topic_0152"},{"id":"T12","span":{"begin":1028,"end":1036},"obj":"http://edamontology.org/topic_0749"},{"id":"T13","span":{"begin":1117,"end":1125},"obj":"http://edamontology.org/topic_0749"}],"text":"Galectin-8 modulates neutrophil function via interaction with integrin alphaM.\nThe members of the galectin family are associated with diverse cellular events, including immune response. We investigated the effects of galectin-8 on neutrophil function. Human galectin-8 induced firm and reversible adhesion of peripheral blood neutrophils but not eosinophils to a plastic surface in a lactose-sensitive manner. Other human galectins, galectins-1, -3, and -9, showed low or negligible effects on neutrophil adhesion. Confocal microscopy revealed actin bundle formation in the presence of galectin-8. Cytochalasins inhibited both actin assembly and cell adhesion induced by galectin-8. Affinity purification of galectin-interacting proteins from solubilized neutrophil membrane revealed that N-terminal carbohydrate recognition domain (CRD) of galectin-8 bound promatrix metalloproteinase-9 (proMMP-9), and C-terminal CRD bound integrin alphaM/CD11b and proMMP-9. A mutant galectin-8 lacking the carbohydrate-binding activity of N-terminal CRD (galectin-8R69H) retained adhesion-inducing activity, but inactivation of C-terminal CRD (galectin-8R233H) abolished the activity. MMP-3-mediated processing of proMMP-9 was accelerated by galectin-8, and this effect was inhibited by lactose. Galectins-1 and -3 did not affect the processing. Superoxide production, an essential event in bactericidal function of neutrophils, was stimulated by galectin-8 to an extent comparable to that induced by fMLP. Galectin-8R69H but not galectin-8R233H could stimulate superoxide production. Taken together, these results suggest that galectin-8 is a novel factor that modulates the neutrophil function related to transendothelial migration and microbial killing."}

EDAM-DFO

{"project":"EDAM-DFO","denotations":[{"id":"T1","span":{"begin":557,"end":566},"obj":"http://edamontology.org/format_1915"},{"id":"T2","span":{"begin":557,"end":566},"obj":"http://edamontology.org/operation_0335"},{"id":"T3","span":{"begin":633,"end":641},"obj":"http://edamontology.org/operation_3433"},{"id":"T4","span":{"begin":729,"end":737},"obj":"http://edamontology.org/data_1467"},{"id":"T5","span":{"begin":729,"end":737},"obj":"http://edamontology.org/format_1208"},{"id":"T6","span":{"begin":813,"end":824},"obj":"http://edamontology.org/operation_2423"},{"id":"T7","span":{"begin":1187,"end":1197},"obj":"http://edamontology.org/operation_0004"},{"id":"T8","span":{"begin":1187,"end":1197},"obj":"http://edamontology.org/operation_2409"},{"id":"T9","span":{"begin":1321,"end":1331},"obj":"http://edamontology.org/operation_2409"},{"id":"T10","span":{"begin":1321,"end":1331},"obj":"http://edamontology.org/operation_0004"}],"text":"Galectin-8 modulates neutrophil function via interaction with integrin alphaM.\nThe members of the galectin family are associated with diverse cellular events, including immune response. We investigated the effects of galectin-8 on neutrophil function. Human galectin-8 induced firm and reversible adhesion of peripheral blood neutrophils but not eosinophils to a plastic surface in a lactose-sensitive manner. Other human galectins, galectins-1, -3, and -9, showed low or negligible effects on neutrophil adhesion. Confocal microscopy revealed actin bundle formation in the presence of galectin-8. Cytochalasins inhibited both actin assembly and cell adhesion induced by galectin-8. Affinity purification of galectin-interacting proteins from solubilized neutrophil membrane revealed that N-terminal carbohydrate recognition domain (CRD) of galectin-8 bound promatrix metalloproteinase-9 (proMMP-9), and C-terminal CRD bound integrin alphaM/CD11b and proMMP-9. A mutant galectin-8 lacking the carbohydrate-binding activity of N-terminal CRD (galectin-8R69H) retained adhesion-inducing activity, but inactivation of C-terminal CRD (galectin-8R233H) abolished the activity. MMP-3-mediated processing of proMMP-9 was accelerated by galectin-8, and this effect was inhibited by lactose. Galectins-1 and -3 did not affect the processing. Superoxide production, an essential event in bactericidal function of neutrophils, was stimulated by galectin-8 to an extent comparable to that induced by fMLP. Galectin-8R69H but not galectin-8R233H could stimulate superoxide production. Taken together, these results suggest that galectin-8 is a novel factor that modulates the neutrophil function related to transendothelial migration and microbial killing."}

GlyCosmos600-FMA

GlycoBiology-MAT

{"project":"GlycoBiology-MAT","denotations":[{"id":"T1","span":{"begin":320,"end":325},"obj":"http://purl.obolibrary.org/obo/MAT_0000315"},{"id":"T2","span":{"begin":320,"end":325},"obj":"http://purl.obolibrary.org/obo/MAT_0000083"}],"text":"Galectin-8 modulates neutrophil function via interaction with integrin alphaM.\nThe members of the galectin family are associated with diverse cellular events, including immune response. We investigated the effects of galectin-8 on neutrophil function. Human galectin-8 induced firm and reversible adhesion of peripheral blood neutrophils but not eosinophils to a plastic surface in a lactose-sensitive manner. Other human galectins, galectins-1, -3, and -9, showed low or negligible effects on neutrophil adhesion. Confocal microscopy revealed actin bundle formation in the presence of galectin-8. Cytochalasins inhibited both actin assembly and cell adhesion induced by galectin-8. Affinity purification of galectin-interacting proteins from solubilized neutrophil membrane revealed that N-terminal carbohydrate recognition domain (CRD) of galectin-8 bound promatrix metalloproteinase-9 (proMMP-9), and C-terminal CRD bound integrin alphaM/CD11b and proMMP-9. A mutant galectin-8 lacking the carbohydrate-binding activity of N-terminal CRD (galectin-8R69H) retained adhesion-inducing activity, but inactivation of C-terminal CRD (galectin-8R233H) abolished the activity. MMP-3-mediated processing of proMMP-9 was accelerated by galectin-8, and this effect was inhibited by lactose. Galectins-1 and -3 did not affect the processing. Superoxide production, an essential event in bactericidal function of neutrophils, was stimulated by galectin-8 to an extent comparable to that induced by fMLP. Galectin-8R69H but not galectin-8R233H could stimulate superoxide production. Taken together, these results suggest that galectin-8 is a novel factor that modulates the neutrophil function related to transendothelial migration and microbial killing."}

glycosmos-test-structure-v1

{"project":"glycosmos-test-structure-v1","denotations":[{"id":"PD-GlycanStructures-B_T1","span":{"begin":384,"end":391},"obj":"http://rdf.glyconavi.org/CarTNa/CarTNa157/trivialname"},{"id":"PD-GlycanStructures-B_T3","span":{"begin":384,"end":391},"obj":"http://rdf.glyconavi.org/CarTNa/CarTNa235/trivialname"},{"id":"PD-GlycanStructures-B_T2","span":{"begin":1274,"end":1281},"obj":"http://rdf.glyconavi.org/CarTNa/CarTNa157/trivialname"},{"id":"PD-GlycanStructures-B_T4","span":{"begin":1274,"end":1281},"obj":"http://rdf.glyconavi.org/CarTNa/CarTNa235/trivialname"}],"text":"Galectin-8 modulates neutrophil function via interaction with integrin alphaM.\nThe members of the galectin family are associated with diverse cellular events, including immune response. We investigated the effects of galectin-8 on neutrophil function. Human galectin-8 induced firm and reversible adhesion of peripheral blood neutrophils but not eosinophils to a plastic surface in a lactose-sensitive manner. Other human galectins, galectins-1, -3, and -9, showed low or negligible effects on neutrophil adhesion. Confocal microscopy revealed actin bundle formation in the presence of galectin-8. Cytochalasins inhibited both actin assembly and cell adhesion induced by galectin-8. Affinity purification of galectin-interacting proteins from solubilized neutrophil membrane revealed that N-terminal carbohydrate recognition domain (CRD) of galectin-8 bound promatrix metalloproteinase-9 (proMMP-9), and C-terminal CRD bound integrin alphaM/CD11b and proMMP-9. A mutant galectin-8 lacking the carbohydrate-binding activity of N-terminal CRD (galectin-8R69H) retained adhesion-inducing activity, but inactivation of C-terminal CRD (galectin-8R233H) abolished the activity. MMP-3-mediated processing of proMMP-9 was accelerated by galectin-8, and this effect was inhibited by lactose. Galectins-1 and -3 did not affect the processing. Superoxide production, an essential event in bactericidal function of neutrophils, was stimulated by galectin-8 to an extent comparable to that induced by fMLP. Galectin-8R69H but not galectin-8R233H could stimulate superoxide production. Taken together, these results suggest that galectin-8 is a novel factor that modulates the neutrophil function related to transendothelial migration and microbial killing."}

glycosmos-test-glycan-structure

{"project":"glycosmos-test-glycan-structure","denotations":[{"id":"PD-GlycanStructures-B_T1","span":{"begin":384,"end":391},"obj":"http://rdf.glyconavi.org/CarTNa/CarTNa157/trivialname"},{"id":"PD-GlycanStructures-B_T2","span":{"begin":1274,"end":1281},"obj":"http://rdf.glyconavi.org/CarTNa/CarTNa157/trivialname"},{"id":"PD-GlycanStructures-B_T3","span":{"begin":384,"end":391},"obj":"http://rdf.glyconavi.org/CarTNa/CarTNa235/trivialname"},{"id":"PD-GlycanStructures-B_T4","span":{"begin":1274,"end":1281},"obj":"http://rdf.glyconavi.org/CarTNa/CarTNa235/trivialname"}],"text":"Galectin-8 modulates neutrophil function via interaction with integrin alphaM.\nThe members of the galectin family are associated with diverse cellular events, including immune response. We investigated the effects of galectin-8 on neutrophil function. Human galectin-8 induced firm and reversible adhesion of peripheral blood neutrophils but not eosinophils to a plastic surface in a lactose-sensitive manner. Other human galectins, galectins-1, -3, and -9, showed low or negligible effects on neutrophil adhesion. Confocal microscopy revealed actin bundle formation in the presence of galectin-8. Cytochalasins inhibited both actin assembly and cell adhesion induced by galectin-8. Affinity purification of galectin-interacting proteins from solubilized neutrophil membrane revealed that N-terminal carbohydrate recognition domain (CRD) of galectin-8 bound promatrix metalloproteinase-9 (proMMP-9), and C-terminal CRD bound integrin alphaM/CD11b and proMMP-9. A mutant galectin-8 lacking the carbohydrate-binding activity of N-terminal CRD (galectin-8R69H) retained adhesion-inducing activity, but inactivation of C-terminal CRD (galectin-8R233H) abolished the activity. MMP-3-mediated processing of proMMP-9 was accelerated by galectin-8, and this effect was inhibited by lactose. Galectins-1 and -3 did not affect the processing. Superoxide production, an essential event in bactericidal function of neutrophils, was stimulated by galectin-8 to an extent comparable to that induced by fMLP. Galectin-8R69H but not galectin-8R233H could stimulate superoxide production. Taken together, these results suggest that galectin-8 is a novel factor that modulates the neutrophil function related to transendothelial migration and microbial killing."}

GlyCosmos600-MAT

{"project":"GlyCosmos600-MAT","denotations":[{"id":"PD-MAT-B_T1","span":{"begin":320,"end":325},"obj":"http://purl.obolibrary.org/obo/MAT_0000083"},{"id":"PD-MAT-B_T2","span":{"begin":320,"end":325},"obj":"http://purl.obolibrary.org/obo/MAT_0000315"}],"text":"Galectin-8 modulates neutrophil function via interaction with integrin alphaM.\nThe members of the galectin family are associated with diverse cellular events, including immune response. We investigated the effects of galectin-8 on neutrophil function. Human galectin-8 induced firm and reversible adhesion of peripheral blood neutrophils but not eosinophils to a plastic surface in a lactose-sensitive manner. Other human galectins, galectins-1, -3, and -9, showed low or negligible effects on neutrophil adhesion. Confocal microscopy revealed actin bundle formation in the presence of galectin-8. Cytochalasins inhibited both actin assembly and cell adhesion induced by galectin-8. Affinity purification of galectin-interacting proteins from solubilized neutrophil membrane revealed that N-terminal carbohydrate recognition domain (CRD) of galectin-8 bound promatrix metalloproteinase-9 (proMMP-9), and C-terminal CRD bound integrin alphaM/CD11b and proMMP-9. A mutant galectin-8 lacking the carbohydrate-binding activity of N-terminal CRD (galectin-8R69H) retained adhesion-inducing activity, but inactivation of C-terminal CRD (galectin-8R233H) abolished the activity. MMP-3-mediated processing of proMMP-9 was accelerated by galectin-8, and this effect was inhibited by lactose. Galectins-1 and -3 did not affect the processing. Superoxide production, an essential event in bactericidal function of neutrophils, was stimulated by galectin-8 to an extent comparable to that induced by fMLP. Galectin-8R69H but not galectin-8R233H could stimulate superoxide production. Taken together, these results suggest that galectin-8 is a novel factor that modulates the neutrophil function related to transendothelial migration and microbial killing."}

GlyCosmos600-GlycoProteins

pubmed-enju-pas

Lectin

{"project":"Lectin","denotations":[{"id":"Lectin_T1","span":{"begin":0,"end":8},"obj":"https://acgg.asia/db/lfdb/LfDB0270"},{"id":"Lectin_T2","span":{"begin":433,"end":444},"obj":"https://acgg.asia/db/lfdb/LfDB0270"},{"id":"Lectin_T3","span":{"begin":1283,"end":1294},"obj":"https://acgg.asia/db/lfdb/LfDB0270"},{"id":"Lectin_T4","span":{"begin":1494,"end":1502},"obj":"https://acgg.asia/db/lfdb/LfDB0270"},{"id":"Lectin_T5","span":{"begin":0,"end":8},"obj":"https://acgg.asia/db/lfdb/LfDB0272"},{"id":"Lectin_T6","span":{"begin":1494,"end":1502},"obj":"https://acgg.asia/db/lfdb/LfDB0272"},{"id":"Lectin_T7","span":{"begin":0,"end":8},"obj":"https://acgg.asia/db/lfdb/LfDB0274"},{"id":"Lectin_T8","span":{"begin":1494,"end":1502},"obj":"https://acgg.asia/db/lfdb/LfDB0274"}],"text":"Galectin-8 modulates neutrophil function via interaction with integrin alphaM.\nThe members of the galectin family are associated with diverse cellular events, including immune response. We investigated the effects of galectin-8 on neutrophil function. Human galectin-8 induced firm and reversible adhesion of peripheral blood neutrophils but not eosinophils to a plastic surface in a lactose-sensitive manner. Other human galectins, galectins-1, -3, and -9, showed low or negligible effects on neutrophil adhesion. Confocal microscopy revealed actin bundle formation in the presence of galectin-8. Cytochalasins inhibited both actin assembly and cell adhesion induced by galectin-8. Affinity purification of galectin-interacting proteins from solubilized neutrophil membrane revealed that N-terminal carbohydrate recognition domain (CRD) of galectin-8 bound promatrix metalloproteinase-9 (proMMP-9), and C-terminal CRD bound integrin alphaM/CD11b and proMMP-9. A mutant galectin-8 lacking the carbohydrate-binding activity of N-terminal CRD (galectin-8R69H) retained adhesion-inducing activity, but inactivation of C-terminal CRD (galectin-8R233H) abolished the activity. MMP-3-mediated processing of proMMP-9 was accelerated by galectin-8, and this effect was inhibited by lactose. Galectins-1 and -3 did not affect the processing. Superoxide production, an essential event in bactericidal function of neutrophils, was stimulated by galectin-8 to an extent comparable to that induced by fMLP. Galectin-8R69H but not galectin-8R233H could stimulate superoxide production. Taken together, these results suggest that galectin-8 is a novel factor that modulates the neutrophil function related to transendothelial migration and microbial killing."}

performance-test

{"project":"performance-test","denotations":[{"id":"PD-UBERON-AE-B_T1","span":{"begin":320,"end":325},"obj":"http://purl.obolibrary.org/obo/UBERON_0000178"}],"text":"Galectin-8 modulates neutrophil function via interaction with integrin alphaM.\nThe members of the galectin family are associated with diverse cellular events, including immune response. We investigated the effects of galectin-8 on neutrophil function. Human galectin-8 induced firm and reversible adhesion of peripheral blood neutrophils but not eosinophils to a plastic surface in a lactose-sensitive manner. Other human galectins, galectins-1, -3, and -9, showed low or negligible effects on neutrophil adhesion. Confocal microscopy revealed actin bundle formation in the presence of galectin-8. Cytochalasins inhibited both actin assembly and cell adhesion induced by galectin-8. Affinity purification of galectin-interacting proteins from solubilized neutrophil membrane revealed that N-terminal carbohydrate recognition domain (CRD) of galectin-8 bound promatrix metalloproteinase-9 (proMMP-9), and C-terminal CRD bound integrin alphaM/CD11b and proMMP-9. A mutant galectin-8 lacking the carbohydrate-binding activity of N-terminal CRD (galectin-8R69H) retained adhesion-inducing activity, but inactivation of C-terminal CRD (galectin-8R233H) abolished the activity. MMP-3-mediated processing of proMMP-9 was accelerated by galectin-8, and this effect was inhibited by lactose. Galectins-1 and -3 did not affect the processing. Superoxide production, an essential event in bactericidal function of neutrophils, was stimulated by galectin-8 to an extent comparable to that induced by fMLP. Galectin-8R69H but not galectin-8R233H could stimulate superoxide production. Taken together, these results suggest that galectin-8 is a novel factor that modulates the neutrophil function related to transendothelial migration and microbial killing."}

GlyCosmos15-Glycan

{"project":"GlyCosmos15-Glycan","denotations":[{"id":"T1","span":{"begin":384,"end":391},"obj":"Glycan"},{"id":"T2","span":{"begin":1274,"end":1281},"obj":"Glycan"}],"attributes":[{"id":"A1","pred":"glycosmos_id","subj":"T1","obj":"https://glycosmos.org/glycans/show/G15541SE"},{"id":"A3","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G15541SE"},{"id":"A2","pred":"glycosmos_id","subj":"T2","obj":"https://glycosmos.org/glycans/show/G15541SE"},{"id":"A4","pred":"image","subj":"T2","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G15541SE"}],"text":"Galectin-8 modulates neutrophil function via interaction with integrin alphaM.\nThe members of the galectin family are associated with diverse cellular events, including immune response. We investigated the effects of galectin-8 on neutrophil function. Human galectin-8 induced firm and reversible adhesion of peripheral blood neutrophils but not eosinophils to a plastic surface in a lactose-sensitive manner. Other human galectins, galectins-1, -3, and -9, showed low or negligible effects on neutrophil adhesion. Confocal microscopy revealed actin bundle formation in the presence of galectin-8. Cytochalasins inhibited both actin assembly and cell adhesion induced by galectin-8. Affinity purification of galectin-interacting proteins from solubilized neutrophil membrane revealed that N-terminal carbohydrate recognition domain (CRD) of galectin-8 bound promatrix metalloproteinase-9 (proMMP-9), and C-terminal CRD bound integrin alphaM/CD11b and proMMP-9. A mutant galectin-8 lacking the carbohydrate-binding activity of N-terminal CRD (galectin-8R69H) retained adhesion-inducing activity, but inactivation of C-terminal CRD (galectin-8R233H) abolished the activity. MMP-3-mediated processing of proMMP-9 was accelerated by galectin-8, and this effect was inhibited by lactose. Galectins-1 and -3 did not affect the processing. Superoxide production, an essential event in bactericidal function of neutrophils, was stimulated by galectin-8 to an extent comparable to that induced by fMLP. Galectin-8R69H but not galectin-8R233H could stimulate superoxide production. Taken together, these results suggest that galectin-8 is a novel factor that modulates the neutrophil function related to transendothelial migration and microbial killing."}

Glycan-GlyCosmos

{"project":"Glycan-GlyCosmos","denotations":[{"id":"T1","span":{"begin":384,"end":391},"obj":"Glycan"},{"id":"T2","span":{"begin":1274,"end":1281},"obj":"Glycan"}],"attributes":[{"id":"A1","pred":"glycosmos_id","subj":"T1","obj":"https://glycosmos.org/glycans/show/G15541SE"},{"id":"A3","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G15541SE"},{"id":"A2","pred":"glycosmos_id","subj":"T2","obj":"https://glycosmos.org/glycans/show/G15541SE"},{"id":"A4","pred":"image","subj":"T2","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G15541SE"}],"text":"Galectin-8 modulates neutrophil function via interaction with integrin alphaM.\nThe members of the galectin family are associated with diverse cellular events, including immune response. We investigated the effects of galectin-8 on neutrophil function. Human galectin-8 induced firm and reversible adhesion of peripheral blood neutrophils but not eosinophils to a plastic surface in a lactose-sensitive manner. Other human galectins, galectins-1, -3, and -9, showed low or negligible effects on neutrophil adhesion. Confocal microscopy revealed actin bundle formation in the presence of galectin-8. Cytochalasins inhibited both actin assembly and cell adhesion induced by galectin-8. Affinity purification of galectin-interacting proteins from solubilized neutrophil membrane revealed that N-terminal carbohydrate recognition domain (CRD) of galectin-8 bound promatrix metalloproteinase-9 (proMMP-9), and C-terminal CRD bound integrin alphaM/CD11b and proMMP-9. A mutant galectin-8 lacking the carbohydrate-binding activity of N-terminal CRD (galectin-8R69H) retained adhesion-inducing activity, but inactivation of C-terminal CRD (galectin-8R233H) abolished the activity. MMP-3-mediated processing of proMMP-9 was accelerated by galectin-8, and this effect was inhibited by lactose. Galectins-1 and -3 did not affect the processing. Superoxide production, an essential event in bactericidal function of neutrophils, was stimulated by galectin-8 to an extent comparable to that induced by fMLP. Galectin-8R69H but not galectin-8R233H could stimulate superoxide production. Taken together, these results suggest that galectin-8 is a novel factor that modulates the neutrophil function related to transendothelial migration and microbial killing."}

GlyCosmos15-CL

{"project":"GlyCosmos15-CL","denotations":[{"id":"T1","span":{"begin":21,"end":31},"obj":"Cell"},{"id":"T2","span":{"begin":231,"end":241},"obj":"Cell"},{"id":"T3","span":{"begin":326,"end":337},"obj":"Cell"},{"id":"T4","span":{"begin":346,"end":357},"obj":"Cell"},{"id":"T5","span":{"begin":494,"end":504},"obj":"Cell"},{"id":"T6","span":{"begin":755,"end":765},"obj":"Cell"},{"id":"T7","span":{"begin":1403,"end":1414},"obj":"Cell"},{"id":"T8","span":{"begin":1663,"end":1673},"obj":"Cell"}],"attributes":[{"id":"A1","pred":"cl_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CL:0000775"},{"id":"A2","pred":"cl_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/CL:0000775"},{"id":"A3","pred":"cl_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/CL:0000775"},{"id":"A4","pred":"cl_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/CL:0000771"},{"id":"A5","pred":"cl_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/CL:0000775"},{"id":"A6","pred":"cl_id","subj":"T6","obj":"http://purl.obolibrary.org/obo/CL:0000775"},{"id":"A7","pred":"cl_id","subj":"T7","obj":"http://purl.obolibrary.org/obo/CL:0000775"},{"id":"A8","pred":"cl_id","subj":"T8","obj":"http://purl.obolibrary.org/obo/CL:0000775"}],"text":"Galectin-8 modulates neutrophil function via interaction with integrin alphaM.\nThe members of the galectin family are associated with diverse cellular events, including immune response. We investigated the effects of galectin-8 on neutrophil function. Human galectin-8 induced firm and reversible adhesion of peripheral blood neutrophils but not eosinophils to a plastic surface in a lactose-sensitive manner. Other human galectins, galectins-1, -3, and -9, showed low or negligible effects on neutrophil adhesion. Confocal microscopy revealed actin bundle formation in the presence of galectin-8. Cytochalasins inhibited both actin assembly and cell adhesion induced by galectin-8. Affinity purification of galectin-interacting proteins from solubilized neutrophil membrane revealed that N-terminal carbohydrate recognition domain (CRD) of galectin-8 bound promatrix metalloproteinase-9 (proMMP-9), and C-terminal CRD bound integrin alphaM/CD11b and proMMP-9. A mutant galectin-8 lacking the carbohydrate-binding activity of N-terminal CRD (galectin-8R69H) retained adhesion-inducing activity, but inactivation of C-terminal CRD (galectin-8R233H) abolished the activity. MMP-3-mediated processing of proMMP-9 was accelerated by galectin-8, and this effect was inhibited by lactose. Galectins-1 and -3 did not affect the processing. Superoxide production, an essential event in bactericidal function of neutrophils, was stimulated by galectin-8 to an extent comparable to that induced by fMLP. Galectin-8R69H but not galectin-8R233H could stimulate superoxide production. Taken together, these results suggest that galectin-8 is a novel factor that modulates the neutrophil function related to transendothelial migration and microbial killing."}

GlyCosmos15-UBERON

{"project":"GlyCosmos15-UBERON","denotations":[{"id":"T1","span":{"begin":21,"end":31},"obj":"Body_part"},{"id":"T2","span":{"begin":231,"end":241},"obj":"Body_part"},{"id":"T3","span":{"begin":320,"end":325},"obj":"Body_part"},{"id":"T4","span":{"begin":326,"end":337},"obj":"Body_part"},{"id":"T5","span":{"begin":346,"end":357},"obj":"Body_part"},{"id":"T6","span":{"begin":494,"end":504},"obj":"Body_part"},{"id":"T7","span":{"begin":755,"end":765},"obj":"Body_part"},{"id":"T8","span":{"begin":766,"end":774},"obj":"Body_part"},{"id":"T9","span":{"begin":1403,"end":1414},"obj":"Body_part"},{"id":"T10","span":{"begin":1663,"end":1673},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CL_0000775"},{"id":"A2","pred":"uberon_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/CL_0000775"},{"id":"A3","pred":"uberon_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/UBERON_0000178"},{"id":"A4","pred":"uberon_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/CL_0000775"},{"id":"A5","pred":"uberon_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/CL_0017502"},{"id":"A6","pred":"uberon_id","subj":"T6","obj":"http://purl.obolibrary.org/obo/CL_0000775"},{"id":"A7","pred":"uberon_id","subj":"T7","obj":"http://purl.obolibrary.org/obo/CL_0000775"},{"id":"A8","pred":"uberon_id","subj":"T8","obj":"http://purl.obolibrary.org/obo/UBERON_0000094"},{"id":"A9","pred":"uberon_id","subj":"T9","obj":"http://purl.obolibrary.org/obo/CL_0000775"},{"id":"A10","pred":"uberon_id","subj":"T10","obj":"http://purl.obolibrary.org/obo/CL_0000775"}],"text":"Galectin-8 modulates neutrophil function via interaction with integrin alphaM.\nThe members of the galectin family are associated with diverse cellular events, including immune response. We investigated the effects of galectin-8 on neutrophil function. Human galectin-8 induced firm and reversible adhesion of peripheral blood neutrophils but not eosinophils to a plastic surface in a lactose-sensitive manner. Other human galectins, galectins-1, -3, and -9, showed low or negligible effects on neutrophil adhesion. Confocal microscopy revealed actin bundle formation in the presence of galectin-8. Cytochalasins inhibited both actin assembly and cell adhesion induced by galectin-8. Affinity purification of galectin-interacting proteins from solubilized neutrophil membrane revealed that N-terminal carbohydrate recognition domain (CRD) of galectin-8 bound promatrix metalloproteinase-9 (proMMP-9), and C-terminal CRD bound integrin alphaM/CD11b and proMMP-9. A mutant galectin-8 lacking the carbohydrate-binding activity of N-terminal CRD (galectin-8R69H) retained adhesion-inducing activity, but inactivation of C-terminal CRD (galectin-8R233H) abolished the activity. MMP-3-mediated processing of proMMP-9 was accelerated by galectin-8, and this effect was inhibited by lactose. Galectins-1 and -3 did not affect the processing. Superoxide production, an essential event in bactericidal function of neutrophils, was stimulated by galectin-8 to an extent comparable to that induced by fMLP. Galectin-8R69H but not galectin-8R233H could stimulate superoxide production. Taken together, these results suggest that galectin-8 is a novel factor that modulates the neutrophil function related to transendothelial migration and microbial killing."}

GlyCosmos15-Taxon

{"project":"GlyCosmos15-Taxon","denotations":[{"id":"T1","span":{"begin":252,"end":257},"obj":"Organism"},{"id":"T2","span":{"begin":416,"end":421},"obj":"Organism"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"9606"},{"id":"A2","pred":"db_id","subj":"T2","obj":"9606"}],"text":"Galectin-8 modulates neutrophil function via interaction with integrin alphaM.\nThe members of the galectin family are associated with diverse cellular events, including immune response. We investigated the effects of galectin-8 on neutrophil function. Human galectin-8 induced firm and reversible adhesion of peripheral blood neutrophils but not eosinophils to a plastic surface in a lactose-sensitive manner. Other human galectins, galectins-1, -3, and -9, showed low or negligible effects on neutrophil adhesion. Confocal microscopy revealed actin bundle formation in the presence of galectin-8. Cytochalasins inhibited both actin assembly and cell adhesion induced by galectin-8. Affinity purification of galectin-interacting proteins from solubilized neutrophil membrane revealed that N-terminal carbohydrate recognition domain (CRD) of galectin-8 bound promatrix metalloproteinase-9 (proMMP-9), and C-terminal CRD bound integrin alphaM/CD11b and proMMP-9. A mutant galectin-8 lacking the carbohydrate-binding activity of N-terminal CRD (galectin-8R69H) retained adhesion-inducing activity, but inactivation of C-terminal CRD (galectin-8R233H) abolished the activity. MMP-3-mediated processing of proMMP-9 was accelerated by galectin-8, and this effect was inhibited by lactose. Galectins-1 and -3 did not affect the processing. Superoxide production, an essential event in bactericidal function of neutrophils, was stimulated by galectin-8 to an extent comparable to that induced by fMLP. Galectin-8R69H but not galectin-8R233H could stimulate superoxide production. Taken together, these results suggest that galectin-8 is a novel factor that modulates the neutrophil function related to transendothelial migration and microbial killing."}

GlyCosmos15-Sentences

{"project":"GlyCosmos15-Sentences","blocks":[{"id":"T1","span":{"begin":0,"end":78},"obj":"Sentence"},{"id":"T2","span":{"begin":79,"end":185},"obj":"Sentence"},{"id":"T3","span":{"begin":186,"end":251},"obj":"Sentence"},{"id":"T4","span":{"begin":252,"end":409},"obj":"Sentence"},{"id":"T5","span":{"begin":410,"end":514},"obj":"Sentence"},{"id":"T6","span":{"begin":515,"end":597},"obj":"Sentence"},{"id":"T7","span":{"begin":598,"end":682},"obj":"Sentence"},{"id":"T8","span":{"begin":683,"end":960},"obj":"Sentence"},{"id":"T9","span":{"begin":961,"end":1171},"obj":"Sentence"},{"id":"T10","span":{"begin":1172,"end":1282},"obj":"Sentence"},{"id":"T11","span":{"begin":1283,"end":1332},"obj":"Sentence"},{"id":"T12","span":{"begin":1333,"end":1493},"obj":"Sentence"},{"id":"T13","span":{"begin":1494,"end":1571},"obj":"Sentence"},{"id":"T14","span":{"begin":1572,"end":1743},"obj":"Sentence"}],"text":"Galectin-8 modulates neutrophil function via interaction with integrin alphaM.\nThe members of the galectin family are associated with diverse cellular events, including immune response. We investigated the effects of galectin-8 on neutrophil function. Human galectin-8 induced firm and reversible adhesion of peripheral blood neutrophils but not eosinophils to a plastic surface in a lactose-sensitive manner. Other human galectins, galectins-1, -3, and -9, showed low or negligible effects on neutrophil adhesion. Confocal microscopy revealed actin bundle formation in the presence of galectin-8. Cytochalasins inhibited both actin assembly and cell adhesion induced by galectin-8. Affinity purification of galectin-interacting proteins from solubilized neutrophil membrane revealed that N-terminal carbohydrate recognition domain (CRD) of galectin-8 bound promatrix metalloproteinase-9 (proMMP-9), and C-terminal CRD bound integrin alphaM/CD11b and proMMP-9. A mutant galectin-8 lacking the carbohydrate-binding activity of N-terminal CRD (galectin-8R69H) retained adhesion-inducing activity, but inactivation of C-terminal CRD (galectin-8R233H) abolished the activity. MMP-3-mediated processing of proMMP-9 was accelerated by galectin-8, and this effect was inhibited by lactose. Galectins-1 and -3 did not affect the processing. Superoxide production, an essential event in bactericidal function of neutrophils, was stimulated by galectin-8 to an extent comparable to that induced by fMLP. Galectin-8R69H but not galectin-8R233H could stimulate superoxide production. Taken together, these results suggest that galectin-8 is a novel factor that modulates the neutrophil function related to transendothelial migration and microbial killing."}

GlyCosmos15-Lectin-Jamboree

{"project":"GlyCosmos15-Lectin-Jamboree","denotations":[{"id":"T1","span":{"begin":0,"end":10},"obj":"Lectin"}],"attributes":[{"id":"A1","pred":"glycosmos_id","subj":"T1","obj":"GL_001001"}],"text":"Galectin-8 modulates neutrophil function via interaction with integrin alphaM.\nThe members of the galectin family are associated with diverse cellular events, including immune response. We investigated the effects of galectin-8 on neutrophil function. Human galectin-8 induced firm and reversible adhesion of peripheral blood neutrophils but not eosinophils to a plastic surface in a lactose-sensitive manner. Other human galectins, galectins-1, -3, and -9, showed low or negligible effects on neutrophil adhesion. Confocal microscopy revealed actin bundle formation in the presence of galectin-8. Cytochalasins inhibited both actin assembly and cell adhesion induced by galectin-8. Affinity purification of galectin-interacting proteins from solubilized neutrophil membrane revealed that N-terminal carbohydrate recognition domain (CRD) of galectin-8 bound promatrix metalloproteinase-9 (proMMP-9), and C-terminal CRD bound integrin alphaM/CD11b and proMMP-9. A mutant galectin-8 lacking the carbohydrate-binding activity of N-terminal CRD (galectin-8R69H) retained adhesion-inducing activity, but inactivation of C-terminal CRD (galectin-8R233H) abolished the activity. MMP-3-mediated processing of proMMP-9 was accelerated by galectin-8, and this effect was inhibited by lactose. Galectins-1 and -3 did not affect the processing. Superoxide production, an essential event in bactericidal function of neutrophils, was stimulated by galectin-8 to an extent comparable to that induced by fMLP. Galectin-8R69H but not galectin-8R233H could stimulate superoxide production. Taken together, these results suggest that galectin-8 is a novel factor that modulates the neutrophil function related to transendothelial migration and microbial killing."}

GlyCosmos15-FMA

{"project":"GlyCosmos15-FMA","denotations":[{"id":"T1","span":{"begin":21,"end":31},"obj":"Body_part"},{"id":"T2","span":{"begin":231,"end":241},"obj":"Body_part"},{"id":"T3","span":{"begin":320,"end":325},"obj":"Body_part"},{"id":"T4","span":{"begin":326,"end":337},"obj":"Body_part"},{"id":"T5","span":{"begin":346,"end":357},"obj":"Body_part"},{"id":"T6","span":{"begin":494,"end":504},"obj":"Body_part"},{"id":"T7","span":{"begin":755,"end":765},"obj":"Body_part"},{"id":"T8","span":{"begin":1403,"end":1414},"obj":"Body_part"},{"id":"T9","span":{"begin":1663,"end":1673},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"FMA:62860"},{"id":"A2","pred":"db_id","subj":"T2","obj":"FMA:62860"},{"id":"A3","pred":"db_id","subj":"T3","obj":"FMA:9670"},{"id":"A4","pred":"db_id","subj":"T4","obj":"FMA:62860"},{"id":"A5","pred":"db_id","subj":"T5","obj":"FMA:62861"},{"id":"A6","pred":"db_id","subj":"T6","obj":"FMA:62860"},{"id":"A7","pred":"db_id","subj":"T7","obj":"FMA:62860"},{"id":"A8","pred":"db_id","subj":"T8","obj":"FMA:62860"},{"id":"A9","pred":"db_id","subj":"T9","obj":"FMA:62860"}],"namespaces":[{"prefix":"FMA","uri":"http://purl.org/sig/ont/fma/fma"}],"text":"Galectin-8 modulates neutrophil function via interaction with integrin alphaM.\nThe members of the galectin family are associated with diverse cellular events, including immune response. We investigated the effects of galectin-8 on neutrophil function. Human galectin-8 induced firm and reversible adhesion of peripheral blood neutrophils but not eosinophils to a plastic surface in a lactose-sensitive manner. Other human galectins, galectins-1, -3, and -9, showed low or negligible effects on neutrophil adhesion. Confocal microscopy revealed actin bundle formation in the presence of galectin-8. Cytochalasins inhibited both actin assembly and cell adhesion induced by galectin-8. Affinity purification of galectin-interacting proteins from solubilized neutrophil membrane revealed that N-terminal carbohydrate recognition domain (CRD) of galectin-8 bound promatrix metalloproteinase-9 (proMMP-9), and C-terminal CRD bound integrin alphaM/CD11b and proMMP-9. A mutant galectin-8 lacking the carbohydrate-binding activity of N-terminal CRD (galectin-8R69H) retained adhesion-inducing activity, but inactivation of C-terminal CRD (galectin-8R233H) abolished the activity. MMP-3-mediated processing of proMMP-9 was accelerated by galectin-8, and this effect was inhibited by lactose. Galectins-1 and -3 did not affect the processing. Superoxide production, an essential event in bactericidal function of neutrophils, was stimulated by galectin-8 to an extent comparable to that induced by fMLP. Galectin-8R69H but not galectin-8R233H could stimulate superoxide production. Taken together, these results suggest that galectin-8 is a novel factor that modulates the neutrophil function related to transendothelial migration and microbial killing."}

GlyCosmos15-MAT

{"project":"GlyCosmos15-MAT","denotations":[{"id":"T1","span":{"begin":320,"end":325},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"mat_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MAT_0000315"}],"text":"Galectin-8 modulates neutrophil function via interaction with integrin alphaM.\nThe members of the galectin family are associated with diverse cellular events, including immune response. We investigated the effects of galectin-8 on neutrophil function. Human galectin-8 induced firm and reversible adhesion of peripheral blood neutrophils but not eosinophils to a plastic surface in a lactose-sensitive manner. Other human galectins, galectins-1, -3, and -9, showed low or negligible effects on neutrophil adhesion. Confocal microscopy revealed actin bundle formation in the presence of galectin-8. Cytochalasins inhibited both actin assembly and cell adhesion induced by galectin-8. Affinity purification of galectin-interacting proteins from solubilized neutrophil membrane revealed that N-terminal carbohydrate recognition domain (CRD) of galectin-8 bound promatrix metalloproteinase-9 (proMMP-9), and C-terminal CRD bound integrin alphaM/CD11b and proMMP-9. A mutant galectin-8 lacking the carbohydrate-binding activity of N-terminal CRD (galectin-8R69H) retained adhesion-inducing activity, but inactivation of C-terminal CRD (galectin-8R233H) abolished the activity. MMP-3-mediated processing of proMMP-9 was accelerated by galectin-8, and this effect was inhibited by lactose. Galectins-1 and -3 did not affect the processing. Superoxide production, an essential event in bactericidal function of neutrophils, was stimulated by galectin-8 to an extent comparable to that induced by fMLP. Galectin-8R69H but not galectin-8R233H could stimulate superoxide production. Taken together, these results suggest that galectin-8 is a novel factor that modulates the neutrophil function related to transendothelial migration and microbial killing."}

NCBITAXON

{"project":"NCBITAXON","denotations":[{"id":"T1","span":{"begin":252,"end":257},"obj":"OrganismTaxon"},{"id":"T2","span":{"begin":416,"end":421},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"9606"},{"id":"A2","pred":"db_id","subj":"T2","obj":"9606"}],"text":"Galectin-8 modulates neutrophil function via interaction with integrin alphaM.\nThe members of the galectin family are associated with diverse cellular events, including immune response. We investigated the effects of galectin-8 on neutrophil function. Human galectin-8 induced firm and reversible adhesion of peripheral blood neutrophils but not eosinophils to a plastic surface in a lactose-sensitive manner. Other human galectins, galectins-1, -3, and -9, showed low or negligible effects on neutrophil adhesion. Confocal microscopy revealed actin bundle formation in the presence of galectin-8. Cytochalasins inhibited both actin assembly and cell adhesion induced by galectin-8. Affinity purification of galectin-interacting proteins from solubilized neutrophil membrane revealed that N-terminal carbohydrate recognition domain (CRD) of galectin-8 bound promatrix metalloproteinase-9 (proMMP-9), and C-terminal CRD bound integrin alphaM/CD11b and proMMP-9. A mutant galectin-8 lacking the carbohydrate-binding activity of N-terminal CRD (galectin-8R69H) retained adhesion-inducing activity, but inactivation of C-terminal CRD (galectin-8R233H) abolished the activity. MMP-3-mediated processing of proMMP-9 was accelerated by galectin-8, and this effect was inhibited by lactose. Galectins-1 and -3 did not affect the processing. Superoxide production, an essential event in bactericidal function of neutrophils, was stimulated by galectin-8 to an extent comparable to that induced by fMLP. Galectin-8R69H but not galectin-8R233H could stimulate superoxide production. Taken together, these results suggest that galectin-8 is a novel factor that modulates the neutrophil function related to transendothelial migration and microbial killing."}

Anatomy-UBERON

{"project":"Anatomy-UBERON","denotations":[{"id":"T1","span":{"begin":21,"end":31},"obj":"Body_part"},{"id":"T2","span":{"begin":231,"end":241},"obj":"Body_part"},{"id":"T3","span":{"begin":320,"end":325},"obj":"Body_part"},{"id":"T4","span":{"begin":326,"end":337},"obj":"Body_part"},{"id":"T5","span":{"begin":346,"end":357},"obj":"Body_part"},{"id":"T6","span":{"begin":494,"end":504},"obj":"Body_part"},{"id":"T7","span":{"begin":755,"end":765},"obj":"Body_part"},{"id":"T8","span":{"begin":766,"end":774},"obj":"Body_part"},{"id":"T11","span":{"begin":1403,"end":1414},"obj":"Body_part"},{"id":"T12","span":{"begin":1663,"end":1673},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CL_0000775"},{"id":"A2","pred":"uberon_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/CL_0000775"},{"id":"A3","pred":"uberon_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/UBERON_0000178"},{"id":"A4","pred":"uberon_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/CL_0000775"},{"id":"A5","pred":"uberon_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/CL_0017502"},{"id":"A6","pred":"uberon_id","subj":"T6","obj":"http://purl.obolibrary.org/obo/CL_0000775"},{"id":"A7","pred":"uberon_id","subj":"T7","obj":"http://purl.obolibrary.org/obo/CL_0000775"},{"id":"A8","pred":"uberon_id","subj":"T8","obj":"http://purl.obolibrary.org/obo/GO_0016020"},{"id":"A9","pred":"uberon_id","subj":"T8","obj":"http://purl.obolibrary.org/obo/UBERON_0000094"},{"id":"A10","pred":"uberon_id","subj":"T8","obj":"http://purl.obolibrary.org/obo/UBERON_0000158"},{"id":"A11","pred":"uberon_id","subj":"T11","obj":"http://purl.obolibrary.org/obo/CL_0000775"},{"id":"A12","pred":"uberon_id","subj":"T12","obj":"http://purl.obolibrary.org/obo/CL_0000775"}],"text":"Galectin-8 modulates neutrophil function via interaction with integrin alphaM.\nThe members of the galectin family are associated with diverse cellular events, including immune response. We investigated the effects of galectin-8 on neutrophil function. Human galectin-8 induced firm and reversible adhesion of peripheral blood neutrophils but not eosinophils to a plastic surface in a lactose-sensitive manner. Other human galectins, galectins-1, -3, and -9, showed low or negligible effects on neutrophil adhesion. Confocal microscopy revealed actin bundle formation in the presence of galectin-8. Cytochalasins inhibited both actin assembly and cell adhesion induced by galectin-8. Affinity purification of galectin-interacting proteins from solubilized neutrophil membrane revealed that N-terminal carbohydrate recognition domain (CRD) of galectin-8 bound promatrix metalloproteinase-9 (proMMP-9), and C-terminal CRD bound integrin alphaM/CD11b and proMMP-9. A mutant galectin-8 lacking the carbohydrate-binding activity of N-terminal CRD (galectin-8R69H) retained adhesion-inducing activity, but inactivation of C-terminal CRD (galectin-8R233H) abolished the activity. MMP-3-mediated processing of proMMP-9 was accelerated by galectin-8, and this effect was inhibited by lactose. Galectins-1 and -3 did not affect the processing. Superoxide production, an essential event in bactericidal function of neutrophils, was stimulated by galectin-8 to an extent comparable to that induced by fMLP. Galectin-8R69H but not galectin-8R233H could stimulate superoxide production. Taken together, these results suggest that galectin-8 is a novel factor that modulates the neutrophil function related to transendothelial migration and microbial killing."}

Anatomy-MAT

{"project":"Anatomy-MAT","denotations":[{"id":"T1","span":{"begin":320,"end":325},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"mat_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MAT_0000083"},{"id":"A2","pred":"mat_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MAT_0000315"}],"text":"Galectin-8 modulates neutrophil function via interaction with integrin alphaM.\nThe members of the galectin family are associated with diverse cellular events, including immune response. We investigated the effects of galectin-8 on neutrophil function. Human galectin-8 induced firm and reversible adhesion of peripheral blood neutrophils but not eosinophils to a plastic surface in a lactose-sensitive manner. Other human galectins, galectins-1, -3, and -9, showed low or negligible effects on neutrophil adhesion. Confocal microscopy revealed actin bundle formation in the presence of galectin-8. Cytochalasins inhibited both actin assembly and cell adhesion induced by galectin-8. Affinity purification of galectin-interacting proteins from solubilized neutrophil membrane revealed that N-terminal carbohydrate recognition domain (CRD) of galectin-8 bound promatrix metalloproteinase-9 (proMMP-9), and C-terminal CRD bound integrin alphaM/CD11b and proMMP-9. A mutant galectin-8 lacking the carbohydrate-binding activity of N-terminal CRD (galectin-8R69H) retained adhesion-inducing activity, but inactivation of C-terminal CRD (galectin-8R233H) abolished the activity. MMP-3-mediated processing of proMMP-9 was accelerated by galectin-8, and this effect was inhibited by lactose. Galectins-1 and -3 did not affect the processing. Superoxide production, an essential event in bactericidal function of neutrophils, was stimulated by galectin-8 to an extent comparable to that induced by fMLP. Galectin-8R69H but not galectin-8R233H could stimulate superoxide production. Taken together, these results suggest that galectin-8 is a novel factor that modulates the neutrophil function related to transendothelial migration and microbial killing."}

CL-cell

{"project":"CL-cell","denotations":[{"id":"T1","span":{"begin":21,"end":31},"obj":"Cell"},{"id":"T2","span":{"begin":231,"end":241},"obj":"Cell"},{"id":"T3","span":{"begin":326,"end":337},"obj":"Cell"},{"id":"T4","span":{"begin":346,"end":357},"obj":"Cell"},{"id":"T5","span":{"begin":494,"end":504},"obj":"Cell"},{"id":"T6","span":{"begin":755,"end":765},"obj":"Cell"},{"id":"T7","span":{"begin":1403,"end":1414},"obj":"Cell"},{"id":"T8","span":{"begin":1663,"end":1673},"obj":"Cell"}],"attributes":[{"id":"A1","pred":"cl_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CL:0000775"},{"id":"A2","pred":"cl_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/CL:0000775"},{"id":"A3","pred":"cl_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/CL:0000775"},{"id":"A4","pred":"cl_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/CL:0000771"},{"id":"A5","pred":"cl_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/CL:0000775"},{"id":"A6","pred":"cl_id","subj":"T6","obj":"http://purl.obolibrary.org/obo/CL:0000775"},{"id":"A7","pred":"cl_id","subj":"T7","obj":"http://purl.obolibrary.org/obo/CL:0000775"},{"id":"A8","pred":"cl_id","subj":"T8","obj":"http://purl.obolibrary.org/obo/CL:0000775"}],"text":"Galectin-8 modulates neutrophil function via interaction with integrin alphaM.\nThe members of the galectin family are associated with diverse cellular events, including immune response. We investigated the effects of galectin-8 on neutrophil function. Human galectin-8 induced firm and reversible adhesion of peripheral blood neutrophils but not eosinophils to a plastic surface in a lactose-sensitive manner. Other human galectins, galectins-1, -3, and -9, showed low or negligible effects on neutrophil adhesion. Confocal microscopy revealed actin bundle formation in the presence of galectin-8. Cytochalasins inhibited both actin assembly and cell adhesion induced by galectin-8. Affinity purification of galectin-interacting proteins from solubilized neutrophil membrane revealed that N-terminal carbohydrate recognition domain (CRD) of galectin-8 bound promatrix metalloproteinase-9 (proMMP-9), and C-terminal CRD bound integrin alphaM/CD11b and proMMP-9. A mutant galectin-8 lacking the carbohydrate-binding activity of N-terminal CRD (galectin-8R69H) retained adhesion-inducing activity, but inactivation of C-terminal CRD (galectin-8R233H) abolished the activity. MMP-3-mediated processing of proMMP-9 was accelerated by galectin-8, and this effect was inhibited by lactose. Galectins-1 and -3 did not affect the processing. Superoxide production, an essential event in bactericidal function of neutrophils, was stimulated by galectin-8 to an extent comparable to that induced by fMLP. Galectin-8R69H but not galectin-8R233H could stimulate superoxide production. Taken together, these results suggest that galectin-8 is a novel factor that modulates the neutrophil function related to transendothelial migration and microbial killing."}