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      mRNAs Coding for the Calcium–Sensing Receptor along the Rat Nephron: Effect of a Low–Phosphate Diet


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          We investigated the localization of mRNA encoding the calcium–sensing receptor (CaSR) along the rat nephron. For this purpose, we combined microdissection of nephron segments and RT–PCR techniques. The results indicate that mRNA encoding rat CaSR is present in rat glomeruli and distal segments (medullary thick ascending limb, cortical thick ascending limb, distal convoluted tubule and cortical collecting duct), whereas it was not detected in proximal convoluted tubules or proximal straight tubules. We also studied whether the CaSR transcription in kidney cortex was modified in response to low dietary phosphate. No significant changes were detected. Given the fact that a low–phosphate diet increased Ca<sup>2+</sup> excretion by more than 50–fold, the results suggest that if the CaSR regulates Ca<sup>2+</sup> reabsorption, it does so through receptor occupancy by Ca<sup>2+</sup> rather than by changes in receptor expression.

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          Cloning and characterization of an extracellular Ca(2+)-sensing receptor from bovine parathyroid.

          Maintenance of a stable internal environment within complex organisms requires specialized cells that sense changes in the extracellular concentration of specific ions (such as Ca2+). Although the molecular nature of such ion sensors is unknown, parathyroid cells possess a cell surface Ca(2+)-sensing mechanism that also recognizes trivalent and polyvalent cations (such as neomycin) and couples by changes in phosphoinositide turnover and cytosolic Ca2+ to regulation of parathyroid hormone secretion. The latter restores normocalcaemia by acting on kidney and bone. We now report the cloning of complementary DNA encoding an extracellular Ca(2+)-sensing receptor from bovine parathyroid with pharmacological and functional properties nearly identical to those of the native receptor. The novel approximately 120K receptor shares limited similarity with the metabotropic glutamate receptors and features a large extracellular domain, containing clusters of acidic amino-acid residues possibly involved in calcium binding, coupled to a seven-membrane-spanning domain like those in the G-protein-coupled receptor superfamily.
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            Relationship between Extra- and Intracellular Calcium in Distal Segments of the Renal Tubule. Role of the Ca 2+ Receptor RaKCaR


              Author and article information

              Kidney Blood Press Res
              Kidney and Blood Pressure Research
              S. Karger AG
              12 November 1998
              : 21
              : 5
              : 305-309
              aDepartment of Biochemistry and Molecular Biology, and bRenal Pathophysiology Laboratory, Mayo Clinic, Rochester, Minn., USA
              25886 Kidney Blood Press Res 1998;21:305–309
              © 1998 S. Karger AG, Basel

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              Page count
              Figures: 3, Tables: 1, References: 18, Pages: 5
              Self URI (application/pdf): https://www.karger.com/Article/Pdf/25886
              Self URI (text/html): https://www.karger.com/Article/FullText/25886
              Self URI (journal page): https://www.karger.com/SubjectArea/Nephrology
              Original Paper

              Cardiovascular Medicine,Nephrology
              Microdissection,Glomeruli,Rat kidney,Ca2 receptor,Extracellular Ca2 ,Ca2 reabsorption


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