PubMed:26747426 JSON TXT

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Glycan-Motif

{"project":"Glycan-Motif","denotations":[{"id":"T1","span":{"begin":759,"end":768},"obj":"https://glytoucan.org/Structures/Glycans/G65889KE"},{"id":"T2","span":{"begin":759,"end":768},"obj":"https://glytoucan.org/Structures/Glycans/G68158BT"}],"text":"Urinary β-galactosidase stimulates Ca2+ transport by stabilizing TRPV5 at the plasma membrane.\nTranscellular Ca(2+) transport in the late distal convoluted tubule and connecting tubule (DCT2/CNT) of the kidney is a finely controlled process mediated by the transient receptor potential vanilloid type 5 (TRPV5) channel. A complex-type-N-glycan bound at the extracellular residue Asn358 of TRPV5 through post-translational glycosylation has been postulated to regulate the activity of TRPV5 channels. Using in vitro Ca(2+) transport assays, immunoblot analysis, immunohistochemistry, patch clamp electrophysiology and total internal reflection fluorescence microscopy, it is demonstrated that the glycosidase β-galactosidase (β-gal), an enzyme that hydrolyzes galactose, stimulates TRPV5 channel activity. However, the activity of the non-glycosylated TRPV(N358Q) mutant was not altered in the presence of β-gal, showing that the stimulation is dependent on the presence of the TRPV5 N-glycan. In addition, β-gal was found to stimulate transcellular Ca(2+) transport in isolated mouse primary DCT2/CNT cells. β-gal expression was detected in the apical membrane of the proximal tubules, and the protein was found in mouse urine. In summary, β-gal is present in the pro-urine from where it is thought to stimulate TRPV5 activity."}

GlyCosmos6-Glycan-Motif-Image

{"project":"GlyCosmos6-Glycan-Motif-Image","denotations":[{"id":"T1","span":{"begin":759,"end":768},"obj":"Glycan_Motif"}],"attributes":[{"id":"A1","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G68158BT"},{"id":"A2","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G65889KE"}],"text":"Urinary β-galactosidase stimulates Ca2+ transport by stabilizing TRPV5 at the plasma membrane.\nTranscellular Ca(2+) transport in the late distal convoluted tubule and connecting tubule (DCT2/CNT) of the kidney is a finely controlled process mediated by the transient receptor potential vanilloid type 5 (TRPV5) channel. A complex-type-N-glycan bound at the extracellular residue Asn358 of TRPV5 through post-translational glycosylation has been postulated to regulate the activity of TRPV5 channels. Using in vitro Ca(2+) transport assays, immunoblot analysis, immunohistochemistry, patch clamp electrophysiology and total internal reflection fluorescence microscopy, it is demonstrated that the glycosidase β-galactosidase (β-gal), an enzyme that hydrolyzes galactose, stimulates TRPV5 channel activity. However, the activity of the non-glycosylated TRPV(N358Q) mutant was not altered in the presence of β-gal, showing that the stimulation is dependent on the presence of the TRPV5 N-glycan. In addition, β-gal was found to stimulate transcellular Ca(2+) transport in isolated mouse primary DCT2/CNT cells. β-gal expression was detected in the apical membrane of the proximal tubules, and the protein was found in mouse urine. In summary, β-gal is present in the pro-urine from where it is thought to stimulate TRPV5 activity."}

GlyCosmos6-Glycan-Motif-Structure

{"project":"GlyCosmos6-Glycan-Motif-Structure","denotations":[{"id":"T1","span":{"begin":759,"end":768},"obj":"https://glytoucan.org/Structures/Glycans/G65889KE"},{"id":"T2","span":{"begin":759,"end":768},"obj":"https://glytoucan.org/Structures/Glycans/G68158BT"}],"text":"Urinary β-galactosidase stimulates Ca2+ transport by stabilizing TRPV5 at the plasma membrane.\nTranscellular Ca(2+) transport in the late distal convoluted tubule and connecting tubule (DCT2/CNT) of the kidney is a finely controlled process mediated by the transient receptor potential vanilloid type 5 (TRPV5) channel. A complex-type-N-glycan bound at the extracellular residue Asn358 of TRPV5 through post-translational glycosylation has been postulated to regulate the activity of TRPV5 channels. Using in vitro Ca(2+) transport assays, immunoblot analysis, immunohistochemistry, patch clamp electrophysiology and total internal reflection fluorescence microscopy, it is demonstrated that the glycosidase β-galactosidase (β-gal), an enzyme that hydrolyzes galactose, stimulates TRPV5 channel activity. However, the activity of the non-glycosylated TRPV(N358Q) mutant was not altered in the presence of β-gal, showing that the stimulation is dependent on the presence of the TRPV5 N-glycan. In addition, β-gal was found to stimulate transcellular Ca(2+) transport in isolated mouse primary DCT2/CNT cells. β-gal expression was detected in the apical membrane of the proximal tubules, and the protein was found in mouse urine. In summary, β-gal is present in the pro-urine from where it is thought to stimulate TRPV5 activity."}

Glycosmos6-MAT

{"project":"Glycosmos6-MAT","denotations":[{"id":"T1","span":{"begin":203,"end":209},"obj":"http://purl.obolibrary.org/obo/MAT_0000119"},{"id":"T2","span":{"begin":1145,"end":1151},"obj":"http://purl.obolibrary.org/obo/MAT_0000484"},{"id":"T3","span":{"begin":1168,"end":1176},"obj":"http://purl.obolibrary.org/obo/MAT_0000491"},{"id":"T4","span":{"begin":1221,"end":1226},"obj":"http://purl.obolibrary.org/obo/MAT_0000058"},{"id":"T5","span":{"begin":1268,"end":1273},"obj":"http://purl.obolibrary.org/obo/MAT_0000058"}],"text":"Urinary β-galactosidase stimulates Ca2+ transport by stabilizing TRPV5 at the plasma membrane.\nTranscellular Ca(2+) transport in the late distal convoluted tubule and connecting tubule (DCT2/CNT) of the kidney is a finely controlled process mediated by the transient receptor potential vanilloid type 5 (TRPV5) channel. A complex-type-N-glycan bound at the extracellular residue Asn358 of TRPV5 through post-translational glycosylation has been postulated to regulate the activity of TRPV5 channels. Using in vitro Ca(2+) transport assays, immunoblot analysis, immunohistochemistry, patch clamp electrophysiology and total internal reflection fluorescence microscopy, it is demonstrated that the glycosidase β-galactosidase (β-gal), an enzyme that hydrolyzes galactose, stimulates TRPV5 channel activity. However, the activity of the non-glycosylated TRPV(N358Q) mutant was not altered in the presence of β-gal, showing that the stimulation is dependent on the presence of the TRPV5 N-glycan. In addition, β-gal was found to stimulate transcellular Ca(2+) transport in isolated mouse primary DCT2/CNT cells. β-gal expression was detected in the apical membrane of the proximal tubules, and the protein was found in mouse urine. In summary, β-gal is present in the pro-urine from where it is thought to stimulate TRPV5 activity."}

sentences

{"project":"sentences","denotations":[{"id":"TextSentencer_T1","span":{"begin":0,"end":94},"obj":"Sentence"},{"id":"TextSentencer_T2","span":{"begin":95,"end":319},"obj":"Sentence"},{"id":"TextSentencer_T3","span":{"begin":320,"end":499},"obj":"Sentence"},{"id":"TextSentencer_T4","span":{"begin":500,"end":804},"obj":"Sentence"},{"id":"TextSentencer_T5","span":{"begin":805,"end":992},"obj":"Sentence"},{"id":"TextSentencer_T6","span":{"begin":993,"end":1227},"obj":"Sentence"},{"id":"TextSentencer_T7","span":{"begin":1228,"end":1327},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":94},"obj":"Sentence"},{"id":"T2","span":{"begin":95,"end":319},"obj":"Sentence"},{"id":"T3","span":{"begin":320,"end":499},"obj":"Sentence"},{"id":"T4","span":{"begin":500,"end":804},"obj":"Sentence"},{"id":"T5","span":{"begin":805,"end":992},"obj":"Sentence"},{"id":"T6","span":{"begin":993,"end":1227},"obj":"Sentence"},{"id":"T7","span":{"begin":1228,"end":1327},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":94},"obj":"Sentence"},{"id":"T2","span":{"begin":95,"end":319},"obj":"Sentence"},{"id":"T3","span":{"begin":320,"end":499},"obj":"Sentence"},{"id":"T4","span":{"begin":500,"end":804},"obj":"Sentence"},{"id":"T5","span":{"begin":805,"end":992},"obj":"Sentence"},{"id":"T6","span":{"begin":993,"end":1227},"obj":"Sentence"},{"id":"T7","span":{"begin":1228,"end":1327},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Urinary β-galactosidase stimulates Ca2+ transport by stabilizing TRPV5 at the plasma membrane.\nTranscellular Ca(2+) transport in the late distal convoluted tubule and connecting tubule (DCT2/CNT) of the kidney is a finely controlled process mediated by the transient receptor potential vanilloid type 5 (TRPV5) channel. A complex-type-N-glycan bound at the extracellular residue Asn358 of TRPV5 through post-translational glycosylation has been postulated to regulate the activity of TRPV5 channels. Using in vitro Ca(2+) transport assays, immunoblot analysis, immunohistochemistry, patch clamp electrophysiology and total internal reflection fluorescence microscopy, it is demonstrated that the glycosidase β-galactosidase (β-gal), an enzyme that hydrolyzes galactose, stimulates TRPV5 channel activity. However, the activity of the non-glycosylated TRPV(N358Q) mutant was not altered in the presence of β-gal, showing that the stimulation is dependent on the presence of the TRPV5 N-glycan. In addition, β-gal was found to stimulate transcellular Ca(2+) transport in isolated mouse primary DCT2/CNT cells. β-gal expression was detected in the apical membrane of the proximal tubules, and the protein was found in mouse urine. In summary, β-gal is present in the pro-urine from where it is thought to stimulate TRPV5 activity."}

GlycoBiology-FMA

uniprot-human

{"project":"uniprot-human","denotations":[{"id":"T1","span":{"begin":8,"end":23},"obj":"http://www.uniprot.org/uniprot/P16278"},{"id":"T2","span":{"begin":708,"end":723},"obj":"http://www.uniprot.org/uniprot/P16278"},{"id":"T3","span":{"begin":65,"end":70},"obj":"http://www.uniprot.org/uniprot/Q9NQA5"},{"id":"T4","span":{"begin":304,"end":309},"obj":"http://www.uniprot.org/uniprot/Q9NQA5"},{"id":"T5","span":{"begin":389,"end":394},"obj":"http://www.uniprot.org/uniprot/Q9NQA5"},{"id":"T6","span":{"begin":484,"end":489},"obj":"http://www.uniprot.org/uniprot/Q9NQA5"},{"id":"T7","span":{"begin":781,"end":786},"obj":"http://www.uniprot.org/uniprot/Q9NQA5"},{"id":"T8","span":{"begin":977,"end":982},"obj":"http://www.uniprot.org/uniprot/Q9NQA5"},{"id":"T9","span":{"begin":1312,"end":1317},"obj":"http://www.uniprot.org/uniprot/Q9NQA5"},{"id":"T10","span":{"begin":257,"end":285},"obj":"http://www.uniprot.org/uniprot/Q7Z2W7"},{"id":"T11","span":{"begin":257,"end":285},"obj":"http://www.uniprot.org/uniprot/Q8NG64"}],"text":"Urinary β-galactosidase stimulates Ca2+ transport by stabilizing TRPV5 at the plasma membrane.\nTranscellular Ca(2+) transport in the late distal convoluted tubule and connecting tubule (DCT2/CNT) of the kidney is a finely controlled process mediated by the transient receptor potential vanilloid type 5 (TRPV5) channel. A complex-type-N-glycan bound at the extracellular residue Asn358 of TRPV5 through post-translational glycosylation has been postulated to regulate the activity of TRPV5 channels. Using in vitro Ca(2+) transport assays, immunoblot analysis, immunohistochemistry, patch clamp electrophysiology and total internal reflection fluorescence microscopy, it is demonstrated that the glycosidase β-galactosidase (β-gal), an enzyme that hydrolyzes galactose, stimulates TRPV5 channel activity. However, the activity of the non-glycosylated TRPV(N358Q) mutant was not altered in the presence of β-gal, showing that the stimulation is dependent on the presence of the TRPV5 N-glycan. In addition, β-gal was found to stimulate transcellular Ca(2+) transport in isolated mouse primary DCT2/CNT cells. β-gal expression was detected in the apical membrane of the proximal tubules, and the protein was found in mouse urine. In summary, β-gal is present in the pro-urine from where it is thought to stimulate TRPV5 activity."}

uniprot-mouse

{"project":"uniprot-mouse","denotations":[{"id":"T1","span":{"begin":8,"end":23},"obj":"http://www.uniprot.org/uniprot/P23780"},{"id":"T2","span":{"begin":708,"end":723},"obj":"http://www.uniprot.org/uniprot/P23780"},{"id":"T3","span":{"begin":35,"end":38},"obj":"http://www.uniprot.org/uniprot/P00920"},{"id":"T4","span":{"begin":727,"end":730},"obj":"http://www.uniprot.org/uniprot/P47212"},{"id":"T5","span":{"begin":907,"end":910},"obj":"http://www.uniprot.org/uniprot/P47212"},{"id":"T6","span":{"begin":1008,"end":1011},"obj":"http://www.uniprot.org/uniprot/P47212"},{"id":"T7","span":{"begin":1110,"end":1113},"obj":"http://www.uniprot.org/uniprot/P47212"},{"id":"T8","span":{"begin":1242,"end":1245},"obj":"http://www.uniprot.org/uniprot/P47212"},{"id":"T9","span":{"begin":1145,"end":1151},"obj":"http://www.uniprot.org/uniprot/P28352"},{"id":"T10","span":{"begin":1264,"end":1267},"obj":"http://www.uniprot.org/uniprot/Q08761"}],"text":"Urinary β-galactosidase stimulates Ca2+ transport by stabilizing TRPV5 at the plasma membrane.\nTranscellular Ca(2+) transport in the late distal convoluted tubule and connecting tubule (DCT2/CNT) of the kidney is a finely controlled process mediated by the transient receptor potential vanilloid type 5 (TRPV5) channel. A complex-type-N-glycan bound at the extracellular residue Asn358 of TRPV5 through post-translational glycosylation has been postulated to regulate the activity of TRPV5 channels. Using in vitro Ca(2+) transport assays, immunoblot analysis, immunohistochemistry, patch clamp electrophysiology and total internal reflection fluorescence microscopy, it is demonstrated that the glycosidase β-galactosidase (β-gal), an enzyme that hydrolyzes galactose, stimulates TRPV5 channel activity. However, the activity of the non-glycosylated TRPV(N358Q) mutant was not altered in the presence of β-gal, showing that the stimulation is dependent on the presence of the TRPV5 N-glycan. In addition, β-gal was found to stimulate transcellular Ca(2+) transport in isolated mouse primary DCT2/CNT cells. β-gal expression was detected in the apical membrane of the proximal tubules, and the protein was found in mouse urine. In summary, β-gal is present in the pro-urine from where it is thought to stimulate TRPV5 activity."}

GlycoBiology-NCBITAXON

{"project":"GlycoBiology-NCBITAXON","denotations":[{"id":"T1","span":{"begin":133,"end":137},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/8186"},{"id":"T2","span":{"begin":145,"end":155},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/31269"},{"id":"T3","span":{"begin":286,"end":295},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/158333"},{"id":"T4","span":{"begin":834,"end":837},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/604139"},{"id":"T5","span":{"begin":1101,"end":1106},"obj":"http://purl.bioontology.org/ontology/STY/T025"}],"text":"Urinary β-galactosidase stimulates Ca2+ transport by stabilizing TRPV5 at the plasma membrane.\nTranscellular Ca(2+) transport in the late distal convoluted tubule and connecting tubule (DCT2/CNT) of the kidney is a finely controlled process mediated by the transient receptor potential vanilloid type 5 (TRPV5) channel. A complex-type-N-glycan bound at the extracellular residue Asn358 of TRPV5 through post-translational glycosylation has been postulated to regulate the activity of TRPV5 channels. Using in vitro Ca(2+) transport assays, immunoblot analysis, immunohistochemistry, patch clamp electrophysiology and total internal reflection fluorescence microscopy, it is demonstrated that the glycosidase β-galactosidase (β-gal), an enzyme that hydrolyzes galactose, stimulates TRPV5 channel activity. However, the activity of the non-glycosylated TRPV(N358Q) mutant was not altered in the presence of β-gal, showing that the stimulation is dependent on the presence of the TRPV5 N-glycan. In addition, β-gal was found to stimulate transcellular Ca(2+) transport in isolated mouse primary DCT2/CNT cells. β-gal expression was detected in the apical membrane of the proximal tubules, and the protein was found in mouse urine. In summary, β-gal is present in the pro-urine from where it is thought to stimulate TRPV5 activity."}

GO-BP

{"project":"GO-BP","denotations":[{"id":"T1","span":{"begin":40,"end":49},"obj":"http://purl.obolibrary.org/obo/GO_0006810"},{"id":"T2","span":{"begin":116,"end":125},"obj":"http://purl.obolibrary.org/obo/GO_0006810"},{"id":"T3","span":{"begin":522,"end":531},"obj":"http://purl.obolibrary.org/obo/GO_0006810"},{"id":"T4","span":{"begin":1056,"end":1065},"obj":"http://purl.obolibrary.org/obo/GO_0006810"},{"id":"T5","span":{"begin":109,"end":111},"obj":"http://purl.obolibrary.org/obo/GO_0033968"},{"id":"T6","span":{"begin":515,"end":517},"obj":"http://purl.obolibrary.org/obo/GO_0033968"},{"id":"T7","span":{"begin":1049,"end":1051},"obj":"http://purl.obolibrary.org/obo/GO_0033968"},{"id":"T8","span":{"begin":408,"end":421},"obj":"http://purl.obolibrary.org/obo/GO_0006412"},{"id":"T9","span":{"begin":422,"end":435},"obj":"http://purl.obolibrary.org/obo/GO_0070085"},{"id":"T10","span":{"begin":838,"end":850},"obj":"http://purl.obolibrary.org/obo/GO_0070085"},{"id":"T11","span":{"begin":459,"end":467},"obj":"http://purl.obolibrary.org/obo/GO_0065007"},{"id":"T12","span":{"begin":787,"end":803},"obj":"http://purl.obolibrary.org/obo/GO_0015267"},{"id":"T13","span":{"begin":1221,"end":1226},"obj":"http://purl.obolibrary.org/obo/GO_0060073"},{"id":"T14","span":{"begin":1268,"end":1273},"obj":"http://purl.obolibrary.org/obo/GO_0060073"}],"text":"Urinary β-galactosidase stimulates Ca2+ transport by stabilizing TRPV5 at the plasma membrane.\nTranscellular Ca(2+) transport in the late distal convoluted tubule and connecting tubule (DCT2/CNT) of the kidney is a finely controlled process mediated by the transient receptor potential vanilloid type 5 (TRPV5) channel. A complex-type-N-glycan bound at the extracellular residue Asn358 of TRPV5 through post-translational glycosylation has been postulated to regulate the activity of TRPV5 channels. Using in vitro Ca(2+) transport assays, immunoblot analysis, immunohistochemistry, patch clamp electrophysiology and total internal reflection fluorescence microscopy, it is demonstrated that the glycosidase β-galactosidase (β-gal), an enzyme that hydrolyzes galactose, stimulates TRPV5 channel activity. However, the activity of the non-glycosylated TRPV(N358Q) mutant was not altered in the presence of β-gal, showing that the stimulation is dependent on the presence of the TRPV5 N-glycan. In addition, β-gal was found to stimulate transcellular Ca(2+) transport in isolated mouse primary DCT2/CNT cells. β-gal expression was detected in the apical membrane of the proximal tubules, and the protein was found in mouse urine. In summary, β-gal is present in the pro-urine from where it is thought to stimulate TRPV5 activity."}

GO-CC

{"project":"GO-CC","denotations":[{"id":"T1","span":{"begin":78,"end":93},"obj":"http://purl.obolibrary.org/obo/GO_0005886"},{"id":"T2","span":{"begin":85,"end":93},"obj":"http://purl.obolibrary.org/obo/GO_0016020"},{"id":"T3","span":{"begin":1152,"end":1160},"obj":"http://purl.obolibrary.org/obo/GO_0016020"},{"id":"T4","span":{"begin":156,"end":162},"obj":"http://purl.obolibrary.org/obo/GO_0097649"},{"id":"T5","span":{"begin":178,"end":184},"obj":"http://purl.obolibrary.org/obo/GO_0097649"},{"id":"T6","span":{"begin":1177,"end":1184},"obj":"http://purl.obolibrary.org/obo/GO_0097649"},{"id":"T7","span":{"begin":357,"end":370},"obj":"http://purl.obolibrary.org/obo/GO_0005576"},{"id":"T8","span":{"begin":1101,"end":1106},"obj":"http://purl.obolibrary.org/obo/GO_0005623"}],"text":"Urinary β-galactosidase stimulates Ca2+ transport by stabilizing TRPV5 at the plasma membrane.\nTranscellular Ca(2+) transport in the late distal convoluted tubule and connecting tubule (DCT2/CNT) of the kidney is a finely controlled process mediated by the transient receptor potential vanilloid type 5 (TRPV5) channel. A complex-type-N-glycan bound at the extracellular residue Asn358 of TRPV5 through post-translational glycosylation has been postulated to regulate the activity of TRPV5 channels. Using in vitro Ca(2+) transport assays, immunoblot analysis, immunohistochemistry, patch clamp electrophysiology and total internal reflection fluorescence microscopy, it is demonstrated that the glycosidase β-galactosidase (β-gal), an enzyme that hydrolyzes galactose, stimulates TRPV5 channel activity. However, the activity of the non-glycosylated TRPV(N358Q) mutant was not altered in the presence of β-gal, showing that the stimulation is dependent on the presence of the TRPV5 N-glycan. In addition, β-gal was found to stimulate transcellular Ca(2+) transport in isolated mouse primary DCT2/CNT cells. β-gal expression was detected in the apical membrane of the proximal tubules, and the protein was found in mouse urine. In summary, β-gal is present in the pro-urine from where it is thought to stimulate TRPV5 activity."}

UBERON-AE

{"project":"UBERON-AE","denotations":[{"id":"T1","span":{"begin":133,"end":162},"obj":"http://purl.obolibrary.org/obo/UBERON_0005102"},{"id":"T2","span":{"begin":138,"end":162},"obj":"http://purl.obolibrary.org/obo/UBERON_0001292"},{"id":"T3","span":{"begin":203,"end":209},"obj":"http://purl.obolibrary.org/obo/UBERON_0002113"},{"id":"T4","span":{"begin":1168,"end":1184},"obj":"http://purl.obolibrary.org/obo/UBERON_0004134"},{"id":"T5","span":{"begin":1221,"end":1226},"obj":"http://purl.obolibrary.org/obo/UBERON_0001088"},{"id":"T6","span":{"begin":1268,"end":1273},"obj":"http://purl.obolibrary.org/obo/UBERON_0001088"}],"text":"Urinary β-galactosidase stimulates Ca2+ transport by stabilizing TRPV5 at the plasma membrane.\nTranscellular Ca(2+) transport in the late distal convoluted tubule and connecting tubule (DCT2/CNT) of the kidney is a finely controlled process mediated by the transient receptor potential vanilloid type 5 (TRPV5) channel. A complex-type-N-glycan bound at the extracellular residue Asn358 of TRPV5 through post-translational glycosylation has been postulated to regulate the activity of TRPV5 channels. Using in vitro Ca(2+) transport assays, immunoblot analysis, immunohistochemistry, patch clamp electrophysiology and total internal reflection fluorescence microscopy, it is demonstrated that the glycosidase β-galactosidase (β-gal), an enzyme that hydrolyzes galactose, stimulates TRPV5 channel activity. However, the activity of the non-glycosylated TRPV(N358Q) mutant was not altered in the presence of β-gal, showing that the stimulation is dependent on the presence of the TRPV5 N-glycan. In addition, β-gal was found to stimulate transcellular Ca(2+) transport in isolated mouse primary DCT2/CNT cells. β-gal expression was detected in the apical membrane of the proximal tubules, and the protein was found in mouse urine. In summary, β-gal is present in the pro-urine from where it is thought to stimulate TRPV5 activity."}

GlycoBiology-MAT

{"project":"GlycoBiology-MAT","denotations":[{"id":"T1","span":{"begin":203,"end":209},"obj":"http://purl.obolibrary.org/obo/MAT_0000119"},{"id":"T2","span":{"begin":1145,"end":1151},"obj":"http://purl.obolibrary.org/obo/MAT_0000484"},{"id":"T3","span":{"begin":1168,"end":1176},"obj":"http://purl.obolibrary.org/obo/MAT_0000491"},{"id":"T4","span":{"begin":1221,"end":1226},"obj":"http://purl.obolibrary.org/obo/MAT_0000058"},{"id":"T5","span":{"begin":1268,"end":1273},"obj":"http://purl.obolibrary.org/obo/MAT_0000058"}],"text":"Urinary β-galactosidase stimulates Ca2+ transport by stabilizing TRPV5 at the plasma membrane.\nTranscellular Ca(2+) transport in the late distal convoluted tubule and connecting tubule (DCT2/CNT) of the kidney is a finely controlled process mediated by the transient receptor potential vanilloid type 5 (TRPV5) channel. A complex-type-N-glycan bound at the extracellular residue Asn358 of TRPV5 through post-translational glycosylation has been postulated to regulate the activity of TRPV5 channels. Using in vitro Ca(2+) transport assays, immunoblot analysis, immunohistochemistry, patch clamp electrophysiology and total internal reflection fluorescence microscopy, it is demonstrated that the glycosidase β-galactosidase (β-gal), an enzyme that hydrolyzes galactose, stimulates TRPV5 channel activity. However, the activity of the non-glycosylated TRPV(N358Q) mutant was not altered in the presence of β-gal, showing that the stimulation is dependent on the presence of the TRPV5 N-glycan. In addition, β-gal was found to stimulate transcellular Ca(2+) transport in isolated mouse primary DCT2/CNT cells. β-gal expression was detected in the apical membrane of the proximal tubules, and the protein was found in mouse urine. In summary, β-gal is present in the pro-urine from where it is thought to stimulate TRPV5 activity."}

performance-test

{"project":"performance-test","denotations":[{"id":"PD-UBERON-AE-B_T1","span":{"begin":203,"end":209},"obj":"http://purl.obolibrary.org/obo/UBERON_0002113"},{"id":"PD-UBERON-AE-B_T2","span":{"begin":133,"end":162},"obj":"http://purl.obolibrary.org/obo/UBERON_0005102"},{"id":"PD-UBERON-AE-B_T3","span":{"begin":138,"end":162},"obj":"http://purl.obolibrary.org/obo/UBERON_0001292"},{"id":"PD-UBERON-AE-B_T4","span":{"begin":1168,"end":1184},"obj":"http://purl.obolibrary.org/obo/UBERON_0004134"},{"id":"PD-UBERON-AE-B_T5","span":{"begin":1221,"end":1226},"obj":"http://purl.obolibrary.org/obo/UBERON_0001088"},{"id":"PD-UBERON-AE-B_T6","span":{"begin":1268,"end":1273},"obj":"http://purl.obolibrary.org/obo/UBERON_0001088"}],"text":"Urinary β-galactosidase stimulates Ca2+ transport by stabilizing TRPV5 at the plasma membrane.\nTranscellular Ca(2+) transport in the late distal convoluted tubule and connecting tubule (DCT2/CNT) of the kidney is a finely controlled process mediated by the transient receptor potential vanilloid type 5 (TRPV5) channel. A complex-type-N-glycan bound at the extracellular residue Asn358 of TRPV5 through post-translational glycosylation has been postulated to regulate the activity of TRPV5 channels. Using in vitro Ca(2+) transport assays, immunoblot analysis, immunohistochemistry, patch clamp electrophysiology and total internal reflection fluorescence microscopy, it is demonstrated that the glycosidase β-galactosidase (β-gal), an enzyme that hydrolyzes galactose, stimulates TRPV5 channel activity. However, the activity of the non-glycosylated TRPV(N358Q) mutant was not altered in the presence of β-gal, showing that the stimulation is dependent on the presence of the TRPV5 N-glycan. In addition, β-gal was found to stimulate transcellular Ca(2+) transport in isolated mouse primary DCT2/CNT cells. β-gal expression was detected in the apical membrane of the proximal tubules, and the protein was found in mouse urine. In summary, β-gal is present in the pro-urine from where it is thought to stimulate TRPV5 activity."}

GlycoBiology-Motifs

{"project":"GlycoBiology-Motifs","denotations":[{"id":"T1","span":{"begin":335,"end":343},"obj":"http://rdf.glycoinfo.org/glycan/G00027MO"},{"id":"T2","span":{"begin":983,"end":991},"obj":"http://rdf.glycoinfo.org/glycan/G00027MO"}],"text":"Urinary β-galactosidase stimulates Ca2+ transport by stabilizing TRPV5 at the plasma membrane.\nTranscellular Ca(2+) transport in the late distal convoluted tubule and connecting tubule (DCT2/CNT) of the kidney is a finely controlled process mediated by the transient receptor potential vanilloid type 5 (TRPV5) channel. A complex-type-N-glycan bound at the extracellular residue Asn358 of TRPV5 through post-translational glycosylation has been postulated to regulate the activity of TRPV5 channels. Using in vitro Ca(2+) transport assays, immunoblot analysis, immunohistochemistry, patch clamp electrophysiology and total internal reflection fluorescence microscopy, it is demonstrated that the glycosidase β-galactosidase (β-gal), an enzyme that hydrolyzes galactose, stimulates TRPV5 channel activity. However, the activity of the non-glycosylated TRPV(N358Q) mutant was not altered in the presence of β-gal, showing that the stimulation is dependent on the presence of the TRPV5 N-glycan. In addition, β-gal was found to stimulate transcellular Ca(2+) transport in isolated mouse primary DCT2/CNT cells. β-gal expression was detected in the apical membrane of the proximal tubules, and the protein was found in mouse urine. In summary, β-gal is present in the pro-urine from where it is thought to stimulate TRPV5 activity."}

Lectin

{"project":"Lectin","denotations":[{"id":"Lectin_T1","span":{"begin":109,"end":111},"obj":"https://acgg.asia/db/lfdb/LfDB0227"},{"id":"Lectin_T2","span":{"begin":515,"end":517},"obj":"https://acgg.asia/db/lfdb/LfDB0227"},{"id":"Lectin_T3","span":{"begin":1049,"end":1051},"obj":"https://acgg.asia/db/lfdb/LfDB0227"}],"text":"Urinary β-galactosidase stimulates Ca2+ transport by stabilizing TRPV5 at the plasma membrane.\nTranscellular Ca(2+) transport in the late distal convoluted tubule and connecting tubule (DCT2/CNT) of the kidney is a finely controlled process mediated by the transient receptor potential vanilloid type 5 (TRPV5) channel. A complex-type-N-glycan bound at the extracellular residue Asn358 of TRPV5 through post-translational glycosylation has been postulated to regulate the activity of TRPV5 channels. Using in vitro Ca(2+) transport assays, immunoblot analysis, immunohistochemistry, patch clamp electrophysiology and total internal reflection fluorescence microscopy, it is demonstrated that the glycosidase β-galactosidase (β-gal), an enzyme that hydrolyzes galactose, stimulates TRPV5 channel activity. However, the activity of the non-glycosylated TRPV(N358Q) mutant was not altered in the presence of β-gal, showing that the stimulation is dependent on the presence of the TRPV5 N-glycan. In addition, β-gal was found to stimulate transcellular Ca(2+) transport in isolated mouse primary DCT2/CNT cells. β-gal expression was detected in the apical membrane of the proximal tubules, and the protein was found in mouse urine. In summary, β-gal is present in the pro-urine from where it is thought to stimulate TRPV5 activity."}

GlyTouCan-IUPAC

Anatomy-MAT

{"project":"Anatomy-MAT","denotations":[{"id":"T1","span":{"begin":203,"end":209},"obj":"Body_part"},{"id":"T2","span":{"begin":1145,"end":1151},"obj":"Body_part"},{"id":"T3","span":{"begin":1168,"end":1176},"obj":"Body_part"},{"id":"T4","span":{"begin":1221,"end":1226},"obj":"Body_part"},{"id":"T5","span":{"begin":1268,"end":1273},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"mat_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MAT_0000119"},{"id":"A2","pred":"mat_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/MAT_0000484"},{"id":"A3","pred":"mat_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/MAT_0000491"},{"id":"A4","pred":"mat_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/MAT_0000058"},{"id":"A5","pred":"mat_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/MAT_0000058"}],"text":"Urinary β-galactosidase stimulates Ca2+ transport by stabilizing TRPV5 at the plasma membrane.\nTranscellular Ca(2+) transport in the late distal convoluted tubule and connecting tubule (DCT2/CNT) of the kidney is a finely controlled process mediated by the transient receptor potential vanilloid type 5 (TRPV5) channel. A complex-type-N-glycan bound at the extracellular residue Asn358 of TRPV5 through post-translational glycosylation has been postulated to regulate the activity of TRPV5 channels. Using in vitro Ca(2+) transport assays, immunoblot analysis, immunohistochemistry, patch clamp electrophysiology and total internal reflection fluorescence microscopy, it is demonstrated that the glycosidase β-galactosidase (β-gal), an enzyme that hydrolyzes galactose, stimulates TRPV5 channel activity. However, the activity of the non-glycosylated TRPV(N358Q) mutant was not altered in the presence of β-gal, showing that the stimulation is dependent on the presence of the TRPV5 N-glycan. In addition, β-gal was found to stimulate transcellular Ca(2+) transport in isolated mouse primary DCT2/CNT cells. β-gal expression was detected in the apical membrane of the proximal tubules, and the protein was found in mouse urine. In summary, β-gal is present in the pro-urine from where it is thought to stimulate TRPV5 activity."}

NCBITAXON

{"project":"NCBITAXON","denotations":[{"id":"T1","span":{"begin":1078,"end":1083},"obj":"OrganismTaxon"},{"id":"T3","span":{"begin":1215,"end":1220},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"10088"},{"id":"A2","pred":"db_id","subj":"T1","obj":"10090"},{"id":"A3","pred":"db_id","subj":"T3","obj":"10088"},{"id":"A4","pred":"db_id","subj":"T3","obj":"10090"}],"text":"Urinary β-galactosidase stimulates Ca2+ transport by stabilizing TRPV5 at the plasma membrane.\nTranscellular Ca(2+) transport in the late distal convoluted tubule and connecting tubule (DCT2/CNT) of the kidney is a finely controlled process mediated by the transient receptor potential vanilloid type 5 (TRPV5) channel. A complex-type-N-glycan bound at the extracellular residue Asn358 of TRPV5 through post-translational glycosylation has been postulated to regulate the activity of TRPV5 channels. Using in vitro Ca(2+) transport assays, immunoblot analysis, immunohistochemistry, patch clamp electrophysiology and total internal reflection fluorescence microscopy, it is demonstrated that the glycosidase β-galactosidase (β-gal), an enzyme that hydrolyzes galactose, stimulates TRPV5 channel activity. However, the activity of the non-glycosylated TRPV(N358Q) mutant was not altered in the presence of β-gal, showing that the stimulation is dependent on the presence of the TRPV5 N-glycan. In addition, β-gal was found to stimulate transcellular Ca(2+) transport in isolated mouse primary DCT2/CNT cells. β-gal expression was detected in the apical membrane of the proximal tubules, and the protein was found in mouse urine. In summary, β-gal is present in the pro-urine from where it is thought to stimulate TRPV5 activity."}

Anatomy-UBERON

{"project":"Anatomy-UBERON","denotations":[{"id":"T1","span":{"begin":78,"end":93},"obj":"Body_part"},{"id":"T2","span":{"begin":133,"end":162},"obj":"Body_part"},{"id":"T3","span":{"begin":167,"end":184},"obj":"Body_part"},{"id":"T4","span":{"begin":203,"end":209},"obj":"Body_part"},{"id":"T5","span":{"begin":357,"end":370},"obj":"Body_part"},{"id":"T6","span":{"begin":1152,"end":1160},"obj":"Body_part"},{"id":"T9","span":{"begin":1168,"end":1184},"obj":"Body_part"},{"id":"T10","span":{"begin":1221,"end":1226},"obj":"Body_part"},{"id":"T11","span":{"begin":1268,"end":1273},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/GO_0005886"},{"id":"A2","pred":"uberon_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/UBERON_0005102"},{"id":"A3","pred":"uberon_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/UBERON_0005097"},{"id":"A4","pred":"uberon_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/UBERON_0002113"},{"id":"A5","pred":"uberon_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/GO_0005576"},{"id":"A6","pred":"uberon_id","subj":"T6","obj":"http://purl.obolibrary.org/obo/GO_0016020"},{"id":"A7","pred":"uberon_id","subj":"T6","obj":"http://purl.obolibrary.org/obo/UBERON_0000094"},{"id":"A8","pred":"uberon_id","subj":"T6","obj":"http://purl.obolibrary.org/obo/UBERON_0000158"},{"id":"A9","pred":"uberon_id","subj":"T9","obj":"http://purl.obolibrary.org/obo/UBERON_0004134"},{"id":"A10","pred":"uberon_id","subj":"T10","obj":"http://purl.obolibrary.org/obo/UBERON_0001088"},{"id":"A11","pred":"uberon_id","subj":"T11","obj":"http://purl.obolibrary.org/obo/UBERON_0001088"}],"text":"Urinary β-galactosidase stimulates Ca2+ transport by stabilizing TRPV5 at the plasma membrane.\nTranscellular Ca(2+) transport in the late distal convoluted tubule and connecting tubule (DCT2/CNT) of the kidney is a finely controlled process mediated by the transient receptor potential vanilloid type 5 (TRPV5) channel. A complex-type-N-glycan bound at the extracellular residue Asn358 of TRPV5 through post-translational glycosylation has been postulated to regulate the activity of TRPV5 channels. Using in vitro Ca(2+) transport assays, immunoblot analysis, immunohistochemistry, patch clamp electrophysiology and total internal reflection fluorescence microscopy, it is demonstrated that the glycosidase β-galactosidase (β-gal), an enzyme that hydrolyzes galactose, stimulates TRPV5 channel activity. However, the activity of the non-glycosylated TRPV(N358Q) mutant was not altered in the presence of β-gal, showing that the stimulation is dependent on the presence of the TRPV5 N-glycan. In addition, β-gal was found to stimulate transcellular Ca(2+) transport in isolated mouse primary DCT2/CNT cells. β-gal expression was detected in the apical membrane of the proximal tubules, and the protein was found in mouse urine. In summary, β-gal is present in the pro-urine from where it is thought to stimulate TRPV5 activity."}