PubMed:23913163 JSONTXT

{"project":"sentences","denotations":[{"id":"TextSentencer_T1","span":{"begin":0,"end":78},"obj":"Sentence"},{"id":"TextSentencer_T2","span":{"begin":79,"end":90},"obj":"Sentence"},{"id":"TextSentencer_T3","span":{"begin":91,"end":211},"obj":"Sentence"},{"id":"TextSentencer_T4","span":{"begin":212,"end":349},"obj":"Sentence"},{"id":"TextSentencer_T5","span":{"begin":350,"end":529},"obj":"Sentence"},{"id":"TextSentencer_T6","span":{"begin":530,"end":625},"obj":"Sentence"},{"id":"TextSentencer_T7","span":{"begin":626,"end":764},"obj":"Sentence"},{"id":"TextSentencer_T8","span":{"begin":765,"end":904},"obj":"Sentence"},{"id":"TextSentencer_T9","span":{"begin":905,"end":1055},"obj":"Sentence"},{"id":"TextSentencer_T10","span":{"begin":1056,"end":1189},"obj":"Sentence"},{"id":"TextSentencer_T11","span":{"begin":1190,"end":1384},"obj":"Sentence"},{"id":"TextSentencer_T12","span":{"begin":1385,"end":1534},"obj":"Sentence"},{"id":"TextSentencer_T13","span":{"begin":1535,"end":1691},"obj":"Sentence"},{"id":"TextSentencer_T14","span":{"begin":1692,"end":1705},"obj":"Sentence"},{"id":"TextSentencer_T15","span":{"begin":1706,"end":1806},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":78},"obj":"Sentence"},{"id":"T2","span":{"begin":79,"end":90},"obj":"Sentence"},{"id":"T3","span":{"begin":91,"end":211},"obj":"Sentence"},{"id":"T4","span":{"begin":212,"end":349},"obj":"Sentence"},{"id":"T5","span":{"begin":350,"end":529},"obj":"Sentence"},{"id":"T6","span":{"begin":530,"end":625},"obj":"Sentence"},{"id":"T7","span":{"begin":626,"end":764},"obj":"Sentence"},{"id":"T8","span":{"begin":765,"end":904},"obj":"Sentence"},{"id":"T9","span":{"begin":905,"end":1055},"obj":"Sentence"},{"id":"T10","span":{"begin":1056,"end":1189},"obj":"Sentence"},{"id":"T11","span":{"begin":1190,"end":1384},"obj":"Sentence"},{"id":"T12","span":{"begin":1385,"end":1534},"obj":"Sentence"},{"id":"T13","span":{"begin":1535,"end":1691},"obj":"Sentence"},{"id":"T14","span":{"begin":1692,"end":1705},"obj":"Sentence"},{"id":"T15","span":{"begin":1706,"end":1806},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Inhibition of cell adhesion by a cadherin-11 antibody thwarts bone metastasis.\nUNLABELLED: Cadherin-11 (CDH11) is a member of the cadherin superfamily mainly expressed in osteoblasts but not in epithelial cells. However, prostate cancer cells with a propensity for bone metastasis express high levels of cadherin-11 and reduced levels of E-cadherin. Downregulation of cadherin-11 inhibits interaction of prostate cancer cells with osteoblasts in vitro and homing of prostate cancer cells to bone in an animal model of metastasis. These findings indicate that targeting cadherin-11 may prevent prostate cancer bone metastasis. To explore this possibility, a panel of 21 monoclonal antibodies (mAb) was generated against the extracellular (EC) domain of cadherin-11. Two antibodies, mAbs 2C7 and 1A5, inhibited cadherin-11-mediated cell-cell aggregation in vitro using L-cells transfected with cadherin-11. Both antibodies demonstrated specificity to cadherin-11, and neither antibody recognized E-cadherin or N-cadherin on C4-2B or PC3 cells, respectively. Furthermore, mAb 2C7 inhibited cadherin-11-mediated aggregation between the highly metastatic PC3-mm2 cells and MC3T3-E1 osteoblasts. Mechanistically, a series of deletion mutants revealed a unique motif, aa 343-348, in the cadherin-11 EC3 domain that is recognized by mAb 2C7 and that this motif coordinated cell-cell adhesion. Importantly, administration of mAb 2C7 in a prophylactic setting effectively prevented metastasis of PC3-mm2 cells to bone in an in vivo mouse model. These results show that targeting the extracellular domain of cadherin-11 can limit cellular adhesion and metastatic dissemination of prostate cancer cells.\nIMPLICATIONS: Monotherapy using a cadherin-11 antibody is a suitable option for the prevention of bone metastases."}

{"project":"DisGeNET","denotations":[{"id":"T0","span":{"begin":1726,"end":1737},"obj":"gene:1009"},{"id":"T1","span":{"begin":1790,"end":1805},"obj":"disease:C0153690"}],"relations":[{"id":"R1","pred":"associated_with","subj":"T0","obj":"T1"}],"namespaces":[{"prefix":"gene","uri":"http://www.ncbi.nlm.nih.gov/gene/"},{"prefix":"disease","uri":"http://purl.bioontology.org/ontology/MEDLINEPLUS/"}],"text":"Inhibition of cell adhesion by a cadherin-11 antibody thwarts bone metastasis.\nUNLABELLED: Cadherin-11 (CDH11) is a member of the cadherin superfamily mainly expressed in osteoblasts but not in epithelial cells. However, prostate cancer cells with a propensity for bone metastasis express high levels of cadherin-11 and reduced levels of E-cadherin. Downregulation of cadherin-11 inhibits interaction of prostate cancer cells with osteoblasts in vitro and homing of prostate cancer cells to bone in an animal model of metastasis. These findings indicate that targeting cadherin-11 may prevent prostate cancer bone metastasis. To explore this possibility, a panel of 21 monoclonal antibodies (mAb) was generated against the extracellular (EC) domain of cadherin-11. Two antibodies, mAbs 2C7 and 1A5, inhibited cadherin-11-mediated cell-cell aggregation in vitro using L-cells transfected with cadherin-11. Both antibodies demonstrated specificity to cadherin-11, and neither antibody recognized E-cadherin or N-cadherin on C4-2B or PC3 cells, respectively. Furthermore, mAb 2C7 inhibited cadherin-11-mediated aggregation between the highly metastatic PC3-mm2 cells and MC3T3-E1 osteoblasts. Mechanistically, a series of deletion mutants revealed a unique motif, aa 343-348, in the cadherin-11 EC3 domain that is recognized by mAb 2C7 and that this motif coordinated cell-cell adhesion. Importantly, administration of mAb 2C7 in a prophylactic setting effectively prevented metastasis of PC3-mm2 cells to bone in an in vivo mouse model. These results show that targeting the extracellular domain of cadherin-11 can limit cellular adhesion and metastatic dissemination of prostate cancer cells.\nIMPLICATIONS: Monotherapy using a cadherin-11 antibody is a suitable option for the prevention of bone metastases."}

{"project":"Allie","denotations":[{"id":"SS1_23913163_2_0","span":{"begin":91,"end":102},"obj":"expanded"},{"id":"SS2_23913163_2_0","span":{"begin":104,"end":109},"obj":"abbr"},{"id":"SS1_23913163_6_0","span":{"begin":669,"end":690},"obj":"expanded"},{"id":"SS2_23913163_6_0","span":{"begin":692,"end":695},"obj":"abbr"},{"id":"SS1_23913163_6_1","span":{"begin":723,"end":736},"obj":"expanded"},{"id":"SS2_23913163_6_1","span":{"begin":738,"end":740},"obj":"abbr"}],"relations":[{"id":"AE1_23913163_2_0","pred":"abbreviatedTo","subj":"SS1_23913163_2_0","obj":"SS2_23913163_2_0"},{"id":"AE1_23913163_6_0","pred":"abbreviatedTo","subj":"SS1_23913163_6_0","obj":"SS2_23913163_6_0"},{"id":"AE1_23913163_6_1","pred":"abbreviatedTo","subj":"SS1_23913163_6_1","obj":"SS2_23913163_6_1"}],"text":"Inhibition of cell adhesion by a cadherin-11 antibody thwarts bone metastasis.\nUNLABELLED: Cadherin-11 (CDH11) is a member of the cadherin superfamily mainly expressed in osteoblasts but not in epithelial cells. However, prostate cancer cells with a propensity for bone metastasis express high levels of cadherin-11 and reduced levels of E-cadherin. Downregulation of cadherin-11 inhibits interaction of prostate cancer cells with osteoblasts in vitro and homing of prostate cancer cells to bone in an animal model of metastasis. These findings indicate that targeting cadherin-11 may prevent prostate cancer bone metastasis. To explore this possibility, a panel of 21 monoclonal antibodies (mAb) was generated against the extracellular (EC) domain of cadherin-11. Two antibodies, mAbs 2C7 and 1A5, inhibited cadherin-11-mediated cell-cell aggregation in vitro using L-cells transfected with cadherin-11. Both antibodies demonstrated specificity to cadherin-11, and neither antibody recognized E-cadherin or N-cadherin on C4-2B or PC3 cells, respectively. Furthermore, mAb 2C7 inhibited cadherin-11-mediated aggregation between the highly metastatic PC3-mm2 cells and MC3T3-E1 osteoblasts. Mechanistically, a series of deletion mutants revealed a unique motif, aa 343-348, in the cadherin-11 EC3 domain that is recognized by mAb 2C7 and that this motif coordinated cell-cell adhesion. Importantly, administration of mAb 2C7 in a prophylactic setting effectively prevented metastasis of PC3-mm2 cells to bone in an in vivo mouse model. These results show that targeting the extracellular domain of cadherin-11 can limit cellular adhesion and metastatic dissemination of prostate cancer cells.\nIMPLICATIONS: Monotherapy using a cadherin-11 antibody is a suitable option for the prevention of bone metastases."}

{"project":"PubmedHPO","denotations":[{"id":"T1","span":{"begin":171,"end":182},"obj":"HP_0011846"},{"id":"T2","span":{"begin":221,"end":236},"obj":"HP_0012125"},{"id":"T3","span":{"begin":230,"end":236},"obj":"HP_0002664"},{"id":"T4","span":{"begin":404,"end":419},"obj":"HP_0012125"},{"id":"T5","span":{"begin":413,"end":419},"obj":"HP_0002664"},{"id":"T6","span":{"begin":431,"end":442},"obj":"HP_0011846"},{"id":"T7","span":{"begin":466,"end":481},"obj":"HP_0012125"},{"id":"T8","span":{"begin":475,"end":481},"obj":"HP_0002664"},{"id":"T9","span":{"begin":593,"end":608},"obj":"HP_0012125"},{"id":"T10","span":{"begin":602,"end":608},"obj":"HP_0002664"},{"id":"T11","span":{"begin":1177,"end":1188},"obj":"HP_0011846"},{"id":"T12","span":{"begin":1669,"end":1684},"obj":"HP_0012125"},{"id":"T13","span":{"begin":1678,"end":1684},"obj":"HP_0002664"}],"text":"Inhibition of cell adhesion by a cadherin-11 antibody thwarts bone metastasis.\nUNLABELLED: Cadherin-11 (CDH11) is a member of the cadherin superfamily mainly expressed in osteoblasts but not in epithelial cells. However, prostate cancer cells with a propensity for bone metastasis express high levels of cadherin-11 and reduced levels of E-cadherin. Downregulation of cadherin-11 inhibits interaction of prostate cancer cells with osteoblasts in vitro and homing of prostate cancer cells to bone in an animal model of metastasis. These findings indicate that targeting cadherin-11 may prevent prostate cancer bone metastasis. To explore this possibility, a panel of 21 monoclonal antibodies (mAb) was generated against the extracellular (EC) domain of cadherin-11. Two antibodies, mAbs 2C7 and 1A5, inhibited cadherin-11-mediated cell-cell aggregation in vitro using L-cells transfected with cadherin-11. Both antibodies demonstrated specificity to cadherin-11, and neither antibody recognized E-cadherin or N-cadherin on C4-2B or PC3 cells, respectively. Furthermore, mAb 2C7 inhibited cadherin-11-mediated aggregation between the highly metastatic PC3-mm2 cells and MC3T3-E1 osteoblasts. Mechanistically, a series of deletion mutants revealed a unique motif, aa 343-348, in the cadherin-11 EC3 domain that is recognized by mAb 2C7 and that this motif coordinated cell-cell adhesion. Importantly, administration of mAb 2C7 in a prophylactic setting effectively prevented metastasis of PC3-mm2 cells to bone in an in vivo mouse model. These results show that targeting the extracellular domain of cadherin-11 can limit cellular adhesion and metastatic dissemination of prostate cancer cells.\nIMPLICATIONS: Monotherapy using a cadherin-11 antibody is a suitable option for the prevention of bone metastases."}

{"project":"DisGeNET5_gene_disease","denotations":[{"id":"23913163-0#33#44#gene1009","span":{"begin":33,"end":44},"obj":"gene1009"},{"id":"23913163-0#62#77#diseaseC0153690","span":{"begin":62,"end":77},"obj":"diseaseC0153690"},{"id":"23913163-11#62#73#gene1009","span":{"begin":1597,"end":1608},"obj":"gene1009"},{"id":"23913163-11#134#149#diseaseC0376358","span":{"begin":1669,"end":1684},"obj":"diseaseC0376358"},{"id":"23913163-11#134#149#diseaseC0600139","span":{"begin":1669,"end":1684},"obj":"diseaseC0600139"},{"id":"23913163-3#18#29#gene1009","span":{"begin":368,"end":379},"obj":"gene1009"},{"id":"23913163-3#168#178#diseaseC0027627","span":{"begin":518,"end":528},"obj":"diseaseC0027627"}],"relations":[{"id":"33#44#gene100962#77#diseaseC0153690","pred":"associated_with","subj":"23913163-0#33#44#gene1009","obj":"23913163-0#62#77#diseaseC0153690"},{"id":"62#73#gene1009134#149#diseaseC0376358","pred":"associated_with","subj":"23913163-11#62#73#gene1009","obj":"23913163-11#134#149#diseaseC0376358"},{"id":"62#73#gene1009134#149#diseaseC0600139","pred":"associated_with","subj":"23913163-11#62#73#gene1009","obj":"23913163-11#134#149#diseaseC0600139"},{"id":"18#29#gene1009168#178#diseaseC0027627","pred":"associated_with","subj":"23913163-3#18#29#gene1009","obj":"23913163-3#168#178#diseaseC0027627"}],"text":"Inhibition of cell adhesion by a cadherin-11 antibody thwarts bone metastasis.\nUNLABELLED: Cadherin-11 (CDH11) is a member of the cadherin superfamily mainly expressed in osteoblasts but not in epithelial cells. However, prostate cancer cells with a propensity for bone metastasis express high levels of cadherin-11 and reduced levels of E-cadherin. Downregulation of cadherin-11 inhibits interaction of prostate cancer cells with osteoblasts in vitro and homing of prostate cancer cells to bone in an animal model of metastasis. These findings indicate that targeting cadherin-11 may prevent prostate cancer bone metastasis. To explore this possibility, a panel of 21 monoclonal antibodies (mAb) was generated against the extracellular (EC) domain of cadherin-11. Two antibodies, mAbs 2C7 and 1A5, inhibited cadherin-11-mediated cell-cell aggregation in vitro using L-cells transfected with cadherin-11. Both antibodies demonstrated specificity to cadherin-11, and neither antibody recognized E-cadherin or N-cadherin on C4-2B or PC3 cells, respectively. Furthermore, mAb 2C7 inhibited cadherin-11-mediated aggregation between the highly metastatic PC3-mm2 cells and MC3T3-E1 osteoblasts. Mechanistically, a series of deletion mutants revealed a unique motif, aa 343-348, in the cadherin-11 EC3 domain that is recognized by mAb 2C7 and that this motif coordinated cell-cell adhesion. Importantly, administration of mAb 2C7 in a prophylactic setting effectively prevented metastasis of PC3-mm2 cells to bone in an in vivo mouse model. These results show that targeting the extracellular domain of cadherin-11 can limit cellular adhesion and metastatic dissemination of prostate cancer cells.\nIMPLICATIONS: Monotherapy using a cadherin-11 antibody is a suitable option for the prevention of bone metastases."}

{"project":"DisGeNet-2017-sample","denotations":[{"id":"T790","span":{"begin":368,"end":379},"obj":"gene:1009"},{"id":"T791","span":{"begin":518,"end":528},"obj":"disease:C0027627"}],"relations":[{"id":"R1","pred":"associated_with","subj":"T790","obj":"T791"}],"namespaces":[{"prefix":"gene","uri":"http://www.ncbi.nlm.nih.gov/gene/"},{"prefix":"disease","uri":"http://purl.bioontology.org/ontology/MEDLINEPLUS/"}],"text":"Inhibition of cell adhesion by a cadherin-11 antibody thwarts bone metastasis.\nUNLABELLED: Cadherin-11 (CDH11) is a member of the cadherin superfamily mainly expressed in osteoblasts but not in epithelial cells. However, prostate cancer cells with a propensity for bone metastasis express high levels of cadherin-11 and reduced levels of E-cadherin. Downregulation of cadherin-11 inhibits interaction of prostate cancer cells with osteoblasts in vitro and homing of prostate cancer cells to bone in an animal model of metastasis. These findings indicate that targeting cadherin-11 may prevent prostate cancer bone metastasis. To explore this possibility, a panel of 21 monoclonal antibodies (mAb) was generated against the extracellular (EC) domain of cadherin-11. Two antibodies, mAbs 2C7 and 1A5, inhibited cadherin-11-mediated cell-cell aggregation in vitro using L-cells transfected with cadherin-11. Both antibodies demonstrated specificity to cadherin-11, and neither antibody recognized E-cadherin or N-cadherin on C4-2B or PC3 cells, respectively. Furthermore, mAb 2C7 inhibited cadherin-11-mediated aggregation between the highly metastatic PC3-mm2 cells and MC3T3-E1 osteoblasts. Mechanistically, a series of deletion mutants revealed a unique motif, aa 343-348, in the cadherin-11 EC3 domain that is recognized by mAb 2C7 and that this motif coordinated cell-cell adhesion. Importantly, administration of mAb 2C7 in a prophylactic setting effectively prevented metastasis of PC3-mm2 cells to bone in an in vivo mouse model. These results show that targeting the extracellular domain of cadherin-11 can limit cellular adhesion and metastatic dissemination of prostate cancer cells.\nIMPLICATIONS: Monotherapy using a cadherin-11 antibody is a suitable option for the prevention of bone metastases."}