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Dominant isolated renal magnesium loss is caused by misrouting of the Na(+),K(+)-ATPase gamma-subunit 总被引:6,自引:0,他引:6
Meij IC Koenderink JB van Bokhoven H Assink KF Groenestege WT de Pont JJ Bindels RJ Monnens LA van den Heuvel LP Knoers NV 《Nature genetics》2000,26(3):265-266
Primary hypomagnesaemia is composed of a heterogeneous group of disorders characterized by renal or intestinal Mg(2+) wasting, often associated with disturbances in Ca(2+) excretion. We identified a putative dominant-negative mutation in the gene encoding the Na(+), K(+)-ATPase gamma-subunit (FXYD2), leading to defective routing of the protein in a family with dominant renal hypomagnesaemia. 相似文献
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Boros S Xi Q Dimke H van der Kemp AW Tudpor K Verkaart S Lee KP Bindels RJ Hoenderop JG 《Cellular and molecular life sciences : CMLS》2012,69(6):981-992
Tissue transglutaminase (tTG) is a multifunctional Ca2+-dependent enzyme, catalyzing protein crosslinking. The transient receptor potential vanilloid (TRPV) family of cation channels
was recently shown to contribute to the regulation of TG activities in keratinocytes and hence skin barrier formation. In
kidney, where active transcellular Ca2+ transport via TRPV5 predominates, the potential effect of tTG remains unknown. A multitude of factors regulate TRPV5, many
secreted into the pro-urine and acting from the extracellular side. We detected tTG in mouse urine and in the apical medium
of polarized cultures of rabbit connecting tubule and cortical collecting duct (CNT/CCD) cells. Extracellular application
of tTG significantly reduced TRPV5 activity in human embryonic kidney cells transiently expressing the channel. Similarly,
a strong inhibition of transepithelial Ca2+ transport was observed after apical application of purified tTG to polarized rabbit CNT/CCD cells. Furthermore, tTG promoted
the aggregation of the plasma membrane-associated fraction of TRPV5. Using patch clamp analysis, we observed a reduction in
the pore diameter after tTG treatment, suggesting distinct structural changes in TRPV5 upon crosslinking by tTG. As N-linked
glycosylation of TRPV5 is a key step in regulating channel function, we determined the effect of tTG in the N-glycosylation-deficient
TRPV5 mutant. In the absence of N-linked glycosylation, TRPV5 was insensitive to tTG. Taken together, these observations imply
that tTG is a novel extracellular enzyme inhibiting the activity of TRPV5. The inhibition of TRPV5 occurs in an N-glycosylation-dependent
manner, signifying a common final pathway by which distinct extracellular factors regulate channel activity. 相似文献
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