PubMed:26747426 JSONTXT

{"target":"http://pubannotation.org/docs/sourcedb/PubMed/sourceid/26747426","sourcedb":"PubMed","sourceid":"26747426","source_url":"http://www.ncbi.nlm.nih.gov/pubmed/26747426","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 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