PubMed:21170089 JSONTXT

{"project":"LitCoin-PubTator-for-Tuning","denotations":[{"id":"3","span":{"begin":0,"end":8},"obj":"GeneOrGeneProduct"},{"id":"4","span":{"begin":18,"end":49},"obj":"DiseaseOrPhenotypicFeature"},{"id":"5","span":{"begin":64,"end":68},"obj":"GeneOrGeneProduct"},{"id":"21","span":{"begin":104,"end":112},"obj":"GeneOrGeneProduct"},{"id":"22","span":{"begin":141,"end":170},"obj":"DiseaseOrPhenotypicFeature"},{"id":"23","span":{"begin":220,"end":228},"obj":"ChemicalEntity"},{"id":"24","span":{"begin":266,"end":293},"obj":"GeneOrGeneProduct"},{"id":"25","span":{"begin":295,"end":299},"obj":"GeneOrGeneProduct"},{"id":"26","span":{"begin":346,"end":359},"obj":"DiseaseOrPhenotypicFeature"},{"id":"27","span":{"begin":416,"end":424},"obj":"GeneOrGeneProduct"},{"id":"28","span":{"begin":426,"end":434},"obj":"GeneOrGeneProduct"},{"id":"29","span":{"begin":439,"end":443},"obj":"GeneOrGeneProduct"},{"id":"30","span":{"begin":490,"end":500},"obj":"GeneOrGeneProduct"},{"id":"31","span":{"begin":520,"end":528},"obj":"GeneOrGeneProduct"},{"id":"32","span":{"begin":532,"end":536},"obj":"GeneOrGeneProduct"},{"id":"33","span":{"begin":721,"end":729},"obj":"GeneOrGeneProduct"},{"id":"34","span":{"begin":734,"end":738},"obj":"GeneOrGeneProduct"},{"id":"35","span":{"begin":796,"end":802},"obj":"DiseaseOrPhenotypicFeature"}],"attributes":[{"id":"A4","pred":"tao:has_database_id","subj":"4","obj":"MESH:D001943"},{"id":"A31","pred":"tao:has_database_id","subj":"31","obj":"Gene:28814"},{"id":"A34","pred":"tao:has_database_id","subj":"34","obj":"Gene:6548"},{"id":"A35","pred":"tao:has_database_id","subj":"35","obj":"MESH:D009369"},{"id":"A30","pred":"tao:has_database_id","subj":"30","obj":"Gene:857"},{"id":"A32","pred":"tao:has_database_id","subj":"32","obj":"Gene:6548"},{"id":"A21","pred":"tao:has_database_id","subj":"21","obj":"Gene:28814"},{"id":"A22","pred":"tao:has_database_id","subj":"22","obj":"MESH:D001943"},{"id":"A24","pred":"tao:has_database_id","subj":"24","obj":"Gene:6548"},{"id":"A28","pred":"tao:has_database_id","subj":"28","obj":"Gene:28814"},{"id":"A23","pred":"tao:has_database_id","subj":"23","obj":"MESH:D003545"},{"id":"A26","pred":"tao:has_database_id","subj":"26","obj":"MESH:D001943"},{"id":"A27","pred":"tao:has_database_id","subj":"27","obj":"Gene:28814"},{"id":"A5","pred":"tao:has_database_id","subj":"5","obj":"Gene:6548"},{"id":"A3","pred":"tao:has_database_id","subj":"3","obj":"Gene:28814"},{"id":"A25","pred":"tao:has_database_id","subj":"25","obj":"Gene:6548"},{"id":"A29","pred":"tao:has_database_id","subj":"29","obj":"Gene:6548"},{"id":"A33","pred":"tao:has_database_id","subj":"33","obj":"Gene:28814"}],"text":"Na(V)1.5 enhances breast cancer cell invasiveness by increasing NHE1-dependent H(+) efflux in caveolae.\nNa(V)1.5 sodium channels enhance the invasiveness of breast cancer cells through the acidic-dependent activation of cysteine cathepsins. Here, we showed that the Na(+)/H(+) exchanger type 1 (NHE1) was an important regulator of H(+) efflux in breast cancer cells MDA-MB-231 and that its activity was increased by Na(V)1.5. Na(V)1.5 and NHE1 were colocalized in membrane rafts containing caveolin-1. The inhibition of Na(V)1.5 or NHE1 induced a similar reduction in cell invasiveness and extracellular matrix degradation; no additive effect was observed when they were simultaneously inhibited. Our study suggests that Na(V)1.5 and NHE1 are functionally coupled and enhance the invasiveness of cancer cells by increasing H(+) efflux."}

{"project":"LitCoin-Disease-Tuning-1","denotations":[{"id":"T1","span":{"begin":18,"end":31},"obj":"DiseaseOrPhenotypicFeature"},{"id":"T2","span":{"begin":157,"end":170},"obj":"DiseaseOrPhenotypicFeature"},{"id":"T3","span":{"begin":346,"end":359},"obj":"DiseaseOrPhenotypicFeature"},{"id":"T4","span":{"begin":370,"end":372},"obj":"DiseaseOrPhenotypicFeature"},{"id":"T5","span":{"begin":796,"end":802},"obj":"DiseaseOrPhenotypicFeature"}],"attributes":[{"id":"A1","pred":"ID:","subj":"T1","obj":"D001943"},{"id":"A5","pred":"ID:","subj":"T5","obj":"D009369"},{"id":"A4","pred":"ID:","subj":"T4","obj":"DISEASE"},{"id":"A2","pred":"ID:","subj":"T2","obj":"D001943"},{"id":"A3","pred":"ID:","subj":"T3","obj":"D001943"}],"text":"Na(V)1.5 enhances breast cancer cell invasiveness by increasing NHE1-dependent H(+) efflux in caveolae.\nNa(V)1.5 sodium channels enhance the invasiveness of breast cancer cells through the acidic-dependent activation of cysteine cathepsins. Here, we showed that the Na(+)/H(+) exchanger type 1 (NHE1) was an important regulator of H(+) efflux in breast cancer cells MDA-MB-231 and that its activity was increased by Na(V)1.5. Na(V)1.5 and NHE1 were colocalized in membrane rafts containing caveolin-1. The inhibition of Na(V)1.5 or NHE1 induced a similar reduction in cell invasiveness and extracellular matrix degradation; no additive effect was observed when they were simultaneously inhibited. Our study suggests that Na(V)1.5 and NHE1 are functionally coupled and enhance the invasiveness of cancer cells by increasing H(+) efflux."}

{"project":"LitCoin-PubTator_CellLine","denotations":[{"id":"T1","span":{"begin":366,"end":376},"obj":"CellLine"}],"attributes":[{"id":"A1","pred":"cellosaurus_accession_id","subj":"T1","obj":"CVCL_0062"}],"text":"Na(V)1.5 enhances breast cancer cell invasiveness by increasing NHE1-dependent H(+) efflux in caveolae.\nNa(V)1.5 sodium channels enhance the invasiveness of breast cancer cells through the acidic-dependent activation of cysteine cathepsins. Here, we showed that the Na(+)/H(+) exchanger type 1 (NHE1) was an important regulator of H(+) efflux in breast cancer cells MDA-MB-231 and that its activity was increased by Na(V)1.5. Na(V)1.5 and NHE1 were colocalized in membrane rafts containing caveolin-1. The inhibition of Na(V)1.5 or NHE1 induced a similar reduction in cell invasiveness and extracellular matrix degradation; no additive effect was observed when they were simultaneously inhibited. Our study suggests that Na(V)1.5 and NHE1 are functionally coupled and enhance the invasiveness of cancer cells by increasing H(+) efflux."}

{"project":"LitEisuke","denotations":[{"id":"T1","span":{"begin":18,"end":31},"obj":"DiseaseOrPhenotypicFeature"},{"id":"T2","span":{"begin":157,"end":170},"obj":"DiseaseOrPhenotypicFeature"},{"id":"T3","span":{"begin":346,"end":359},"obj":"DiseaseOrPhenotypicFeature"},{"id":"T4","span":{"begin":370,"end":372},"obj":"DiseaseOrPhenotypicFeature"},{"id":"T5","span":{"begin":796,"end":802},"obj":"DiseaseOrPhenotypicFeature"}],"attributes":[{"id":"A3","pred":"#label","subj":"T3","obj":"D001943"},{"id":"A4","pred":"#label","subj":"T4","obj":"DISEASE"},{"id":"A1","pred":"#label","subj":"T1","obj":"D001943"},{"id":"A5","pred":"#label","subj":"T5","obj":"D009369"},{"id":"A2","pred":"#label","subj":"T2","obj":"D001943"}],"text":"Na(V)1.5 enhances breast cancer cell invasiveness by increasing NHE1-dependent H(+) efflux in caveolae.\nNa(V)1.5 sodium channels enhance the invasiveness of breast cancer cells through the acidic-dependent activation of cysteine cathepsins. Here, we showed that the Na(+)/H(+) exchanger type 1 (NHE1) was an important regulator of H(+) efflux in breast cancer cells MDA-MB-231 and that its activity was increased by Na(V)1.5. Na(V)1.5 and NHE1 were colocalized in membrane rafts containing caveolin-1. The inhibition of Na(V)1.5 or NHE1 induced a similar reduction in cell invasiveness and extracellular matrix degradation; no additive effect was observed when they were simultaneously inhibited. Our study suggests that Na(V)1.5 and NHE1 are functionally coupled and enhance the invasiveness of cancer cells by increasing H(+) efflux."}

{"project":"DisGeNET","denotations":[{"id":"T0","span":{"begin":734,"end":738},"obj":"gene:6548"},{"id":"T1","span":{"begin":796,"end":802},"obj":"disease:C0006826"},{"id":"T2","span":{"begin":734,"end":738},"obj":"gene:6548"},{"id":"T3","span":{"begin":796,"end":802},"obj":"disease:C1306459"}],"relations":[{"id":"R1","pred":"associated_with","subj":"T0","obj":"T1"},{"id":"R2","pred":"associated_with","subj":"T2","obj":"T3"}],"namespaces":[{"prefix":"gene","uri":"http://www.ncbi.nlm.nih.gov/gene/"},{"prefix":"disease","uri":"http://purl.bioontology.org/ontology/MEDLINEPLUS/"}],"text":"Na(V)1.5 enhances breast cancer cell invasiveness by increasing NHE1-dependent H(+) efflux in caveolae.\nNa(V)1.5 sodium channels enhance the invasiveness of breast cancer cells through the acidic-dependent activation of cysteine cathepsins. Here, we showed that the Na(+)/H(+) exchanger type 1 (NHE1) was an important regulator of H(+) efflux in breast cancer cells MDA-MB-231 and that its activity was increased by Na(V)1.5. Na(V)1.5 and NHE1 were colocalized in membrane rafts containing caveolin-1. The inhibition of Na(V)1.5 or NHE1 induced a similar reduction in cell invasiveness and extracellular matrix degradation; no additive effect was observed when they were simultaneously inhibited. Our study suggests that Na(V)1.5 and NHE1 are functionally coupled and enhance the invasiveness of cancer cells by increasing H(+) efflux."}

{"project":"PubmedHPO","denotations":[{"id":"T1","span":{"begin":157,"end":170},"obj":"HP_0003002"},{"id":"T2","span":{"begin":157,"end":170},"obj":"HP_0100013"},{"id":"T3","span":{"begin":164,"end":170},"obj":"HP_0002664"},{"id":"T4","span":{"begin":346,"end":359},"obj":"HP_0003002"},{"id":"T5","span":{"begin":346,"end":359},"obj":"HP_0100013"},{"id":"T6","span":{"begin":353,"end":359},"obj":"HP_0002664"},{"id":"T7","span":{"begin":796,"end":802},"obj":"HP_0002664"}],"text":"Na(V)1.5 enhances breast cancer cell invasiveness by increasing NHE1-dependent H(+) efflux in caveolae.\nNa(V)1.5 sodium channels enhance the invasiveness of breast cancer cells through the acidic-dependent activation of cysteine cathepsins. Here, we showed that the Na(+)/H(+) exchanger type 1 (NHE1) was an important regulator of H(+) efflux in breast cancer cells MDA-MB-231 and that its activity was increased by Na(V)1.5. Na(V)1.5 and NHE1 were colocalized in membrane rafts containing caveolin-1. The inhibition of Na(V)1.5 or NHE1 induced a similar reduction in cell invasiveness and extracellular matrix degradation; no additive effect was observed when they were simultaneously inhibited. Our study suggests that Na(V)1.5 and NHE1 are functionally coupled and enhance the invasiveness of cancer cells by increasing H(+) efflux."}

{"project":"Allie","denotations":[{"id":"SS1_21170089_2_0","span":{"begin":266,"end":293},"obj":"expanded"},{"id":"SS2_21170089_2_0","span":{"begin":295,"end":299},"obj":"abbr"}],"relations":[{"id":"AE1_21170089_2_0","pred":"abbreviatedTo","subj":"SS1_21170089_2_0","obj":"SS2_21170089_2_0"}],"text":"Na(V)1.5 enhances breast cancer cell invasiveness by increasing NHE1-dependent H(+) efflux in caveolae.\nNa(V)1.5 sodium channels enhance the invasiveness of breast cancer cells through the acidic-dependent activation of cysteine cathepsins. Here, we showed that the Na(+)/H(+) exchanger type 1 (NHE1) was an important regulator of H(+) efflux in breast cancer cells MDA-MB-231 and that its activity was increased by Na(V)1.5. Na(V)1.5 and NHE1 were colocalized in membrane rafts containing caveolin-1. The inhibition of Na(V)1.5 or NHE1 induced a similar reduction in cell invasiveness and extracellular matrix degradation; no additive effect was observed when they were simultaneously inhibited. Our study suggests that Na(V)1.5 and NHE1 are functionally coupled and enhance the invasiveness of cancer cells by increasing H(+) efflux."}

{"project":"DisGeNET5_gene_disease","denotations":[{"id":"21170089-2#54#58#gene6548","span":{"begin":295,"end":299},"obj":"gene6548"},{"id":"21170089-2#105#118#diseaseC0006142","span":{"begin":346,"end":359},"obj":"diseaseC0006142"},{"id":"21170089-2#105#118#diseaseC0678222","span":{"begin":346,"end":359},"obj":"diseaseC0678222"}],"relations":[{"id":"54#58#gene6548105#118#diseaseC0006142","pred":"associated_with","subj":"21170089-2#54#58#gene6548","obj":"21170089-2#105#118#diseaseC0006142"},{"id":"54#58#gene6548105#118#diseaseC0678222","pred":"associated_with","subj":"21170089-2#54#58#gene6548","obj":"21170089-2#105#118#diseaseC0678222"}],"text":"Na(V)1.5 enhances breast cancer cell invasiveness by increasing NHE1-dependent H(+) efflux in caveolae.\nNa(V)1.5 sodium channels enhance the invasiveness of breast cancer cells through the acidic-dependent activation of cysteine cathepsins. Here, we showed that the Na(+)/H(+) exchanger type 1 (NHE1) was an important regulator of H(+) efflux in breast cancer cells MDA-MB-231 and that its activity was increased by Na(V)1.5. Na(V)1.5 and NHE1 were colocalized in membrane rafts containing caveolin-1. The inhibition of Na(V)1.5 or NHE1 induced a similar reduction in cell invasiveness and extracellular matrix degradation; no additive effect was observed when they were simultaneously inhibited. Our study suggests that Na(V)1.5 and NHE1 are functionally coupled and enhance the invasiveness of cancer cells by increasing H(+) efflux."}