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

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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 D3-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 D3 treatment. In conclusion, stanniocalcin 1 was expressed in the apical membrane of distal nephron segments and enhanced by vitamin D3.

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Human stanniocalcin: a possible hormonal regulator of mineral metabolism.

Raymond Rosen, B L Vozzolo, Bradley Wagner … (1996)

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.

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

Graham F. Wagner, Ewa Jaworski (1994)

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.

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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.

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Journal ID (publisher-id): EXN

Journal ID (nlm-ta): Nephron Exp Nephrol

Journal ID (doi): 10.1159/issn.1660-2129

Title: Cardiorenal Medicine

Publisher: S. Karger AG

ISSN (Electronic): 1660-2129

Publication date Subscription-year: 2001

Publication date (Print): 2001

Publication date (Electronic): 07 November 2001

Volume: 9

Issue: 6

Pages: 428-435

Affiliations

^aDivision of Nephrology and Endocrinology, University of Tokyo, and ^bDepartment of Biological Sciences, Tokyo Institute of Technology, Yokohama, Japan

Article

Publisher ID: 52642 Other ID: Exp Nephrol 2001;9:428–435

DOI: 10.1159/000052642

PubMed ID: 11702003

SO-VID: 04caad70-0ed1-4026-af25-c0b696a5cf27

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

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Karger: Nephrology

Most cited references 3

Human stanniocalcin: a possible hormonal regulator of mineral metabolism.

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

Assignment of disulfide linkages in chum salmon stanniocalcin.

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