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10.1074/jbc.M611117200

http://scihub22266oqcxt.onion/10.1074/jbc.M611117200
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17197439!ä!17197439

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suck abstract from ncbi


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pmid17197439      J+Biol+Chem 2007 ; 282 (10): 7656-67
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  • Hypomagnesemia with secondary hypocalcemia due to a missense mutation in the putative pore-forming region of TRPM6 #MMPMID17197439
  • Chubanov V; Schlingmann KP; Waring J; Heinzinger J; Kaske S; Waldegger S; Mederos y Schnitzler M; Gudermann T
  • J Biol Chem 2007[Mar]; 282 (10): 7656-67 PMID17197439show ga
  • Hypomagnesemia with secondary hypocalcemia is an autosomal recessive disorder caused by mutations in the TRPM6 gene. Current experimental evidence suggests that TRPM6 may function in a specific association with TRPM7 by means of heterooligomeric channel complex formation. Here, we report the identification and functional characterization of a new hypomagnesemia with secondary hypocalcemia missense mutation in TRPM6. The affected subject presented with profound hypomagnesemia and hypocalcemia caused by compound heterozygous mutation in the TRPM6 gene: 1208(-1)G > A affecting the acceptor splice site preceding exon 11, and 3050C > G resulting in the amino acid change (P1017R) in the putative pore-forming region of TRPM6. To assess the functional consequences of the P1017R mutation, TRPM6(P1017R) and wild-type TRPM6 were co-expressed with TRPM7 in Xenopus oocytes and HEK 293 cells, and currents were assessed by two-electrode voltage clamp and whole cell patch clamp measurements, respectively. Co-expression of wild-type TRPM6 and TRPM7 resulted in a significant increase in the amplitude of TRPM7-like currents. In contrast, TRPM6(P1017R) suppressed TRPM7 channel activity. In line with these observations, TRPM7, containing the corresponding mutation P1040R, displayed a dominant-negative effect upon co-expression with wild-type TRPM7. Confocal microscopy and fluorescence resonance energy transfer recordings demonstrated that the P1017R mutation neither affects assembly of TRPM6 with TRPM7, nor co-trafficking of heteromultimeric channel complexes to the cell surface. We conclude that a functional defect in the putative pore of TRPM6/7 channel complexes is sufficient to impair body magnesium homeostasis.
  • |*Mutation, Missense[MESH]
  • |Amino Acid Sequence[MESH]
  • |Animals[MESH]
  • |Cells, Cultured[MESH]
  • |Humans[MESH]
  • |Hypocalcemia/etiology/*genetics[MESH]
  • |Magnesium Deficiency/etiology/*genetics[MESH]
  • |Magnesium/blood[MESH]
  • |Molecular Sequence Data[MESH]
  • |Protein Serine-Threonine Kinases[MESH]
  • |TRPM Cation Channels/chemistry/*genetics/physiology[MESH]


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  • suck abstract from ncbi

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