Blog
About

0
views
0
recommends
+1 Recommend
1 collections
    0
    shares
      • Record: found
      • Abstract: found
      • Article: found

      Distribution of Stanniocalcin 1 in Rat Kidney and Its Regulation by Vitamin D 3

      Read this article at

      ScienceOpenPublisherPubMed
      Bookmark
          There is no author summary for this article yet. Authors can add summaries to their articles on ScienceOpen to make them more accessible to a non-specialist audience.

          Abstract

          Stanniocalcin is a glycoprotein hormone first described in fish as a hypocalcemic factor, and recently its mammalian counterpart has been identified. Localization of stanniocalcin 1 and its regulation of expression were determined in control and 1α,25-dihydroxyvitamin D<sub>3</sub>-treated rats. Immunoreactivity for stanniocalcin 1 was detected in the loop of Henle, macula densa cells, distal convoluted tubule (DCT), and cortical collecting duct (CCD), and also faintly in the medullary collecting ducts. Pre-embedding electron-microscopic immunocytochemistry revealed stanniocalcin 1 in the apical membrane of cells of loop of Henle, DCT, and principal cells of CCD. The expression of stanniocalcin 1 was increased by elevated plasma calcium via 1α,25-dihydroxyvitamin D<sub>3</sub> treatment. In conclusion, stanniocalcin 1 was expressed in the apical membrane of distal nephron segments and enhanced by vitamin D<sub>3</sub>.

          Related collections

          Most cited references 3

          • Record: found
          • Abstract: found
          • Article: not found

          Human stanniocalcin: a possible hormonal regulator of mineral metabolism.

          We have isolated a human cDNA clone encoding the mammalian homolog of stanniocalcin (STC), a calcium- and phosphate-regulating hormone that was first described in fishes where it functions in preventing hypercalcemia. STC has a unique amino acid sequence and, until now, has remained one of the few polypeptide hormones never described in higher vertebrates. Human STC (hSTC) was found to be 247 amino acids long and to share 73% amino acid sequence similarity with fish STC. Polyclonal antibodies to recombinant hSTC localized to a distinct cell type in the nephron tubule, suggesting kidney as a possible site of synthesis. Recombinant hSTC inhibited the gill transport of calcium when administered to fish and stimulated renal phosphate reabsorption in the rat. The evidence suggests that mammalian STC, like its piscine counterpart, is a regulator of mineral homeostasis.
            Bookmark
            • Record: found
            • Abstract: found
            • Article: not found

            Calcium regulates stanniocalcin mRNA levels in primary cultured rainbow trout corpuscles of stannius.

            Stanniocalcin (STC) is an inhibitor of gill calcium transport produced by the corpuscles of Stannius (CS), endocrine glands in bony fishes. In previous studies we have described how STC secretion is regulated by calcium both in vitro and in vivo, using rainbow trout as a model system. In this report we have examined the effects of calcium on STC mRNA levels in primary cultured trout CS cells. The results show that message levels are positively regulated by extracellular calcium concentrations within the physiological range. The calcium response was also temporally-related as more prolonged exposures tended to have greater effects. Similar concentrations of magnesium had no effect on message levels. This represents another level at which calcium regulates the CS cell, in addition to its established effects on STC synthesis and secretion. The results are discussed in relation to the other known calciotropic hormones, calcitonin and parathyroid hormone.
              Bookmark
              • Record: found
              • Abstract: found
              • Article: not found

              Assignment of disulfide linkages in chum salmon stanniocalcin.

               H Kawauchi,  I Hulova (1999)
              Stanniocalcin (STC) is a hypocalcemic glycoprotein hormone secreted by the corpuscles of Stannius, endocrine glands unique to the bony fishes. Recently, two cDNAs encoding proteins, STC-1 and STC-2, homologous to fish STC have been identified in humans and rodents. The STC-1, but not STC-2, is identical to fish STC with respect to location of all Cys residues. The present study reports the localization of inter- and intra-molecular disulfide linkages in chum salmon STC. The chum salmon STC was deglycosylated and digested with several proteases in series. Six fragments, each of which consisted of two peptides connected by a single disulfide bond, were isolated by HPLC. Disulfide bonds were determined by sequence analysis after reduction and S-alkylation of each peptide fragment. Chum salmon STC is a homodimer connected by a single intermonomeric disulfide bond at Cys169. The monomer consists of 179 amino-acids, containing five intramonomeric disulfide bonds formed between Cys12-Cys26, Cys21-Cys41, Cys32-Cys81, Cys65-Cys95, and Cys102-Cys137. Copyright 1999 Academic Press.
                Bookmark

                Author and article information

                Journal
                EXN
                Nephron Exp Nephrol
                10.1159/issn.1660-2129
                Cardiorenal Medicine
                S. Karger AG
                1660-2129
                2001
                2001
                07 November 2001
                : 9
                : 6
                : 428-435
                Affiliations
                aDivision of Nephrology and Endocrinology, University of Tokyo, and bDepartment of Biological Sciences, Tokyo Institute of Technology, Yokohama, Japan
                Article
                52642 Exp Nephrol 2001;9:428–435
                10.1159/000052642
                11702003
                © 2001 S. Karger AG, Basel

                Copyright: All rights reserved. No part of this publication may be translated into other languages, reproduced or utilized in any form or by any means, electronic or mechanical, including photocopying, recording, microcopying, or by any information storage and retrieval system, without permission in writing from the publisher. Drug Dosage: The authors and the publisher have exerted every effort to ensure that drug selection and dosage set forth in this text are in accord with current recommendations and practice at the time of publication. However, in view of ongoing research, changes in government regulations, and the constant flow of information relating to drug therapy and drug reactions, the reader is urged to check the package insert for each drug for any changes in indications and dosage and for added warnings and precautions. This is particularly important when the recommended agent is a new and/or infrequently employed drug. Disclaimer: The statements, opinions and data contained in this publication are solely those of the individual authors and contributors and not of the publishers and the editor(s). The appearance of advertisements or/and product references in the publication is not a warranty, endorsement, or approval of the products or services advertised or of their effectiveness, quality or safety. The publisher and the editor(s) disclaim responsibility for any injury to persons or property resulting from any ideas, methods, instructions or products referred to in the content or advertisements.

                Page count
                Figures: 5, Tables: 1, References: 39, Pages: 8
                Product
                Self URI (application/pdf): https://www.karger.com/Article/Pdf/52642
                Categories
                Original Paper

                Comments

                Comment on this article