Parathyroid function is controlled by the regulation of hormone secretion as well as degradation, through the action of calcium and vitamin D derivatives. In order to clarify the relationship between vitamin D metabolism and parathyroid degradation system, parathyroid hormone (PTH)-degrading activities of the kidney were measured in vitamin D repleted and depleted rats given various derivatives of vitamin D. Kidney calcium content rose markedly in animals given 10 microgram/kg 1 alpha(OH) vitamin D3 and 1,000 microgram/kg dihydrotachysterol and PTH-degrading activity rose only in these animals, indicating a parallelism between kidney calcium content and PTH-degrading activity of the kidney tissue. These vitamin D derivatives also increased the PTH-degrading activity of kidney tissue when they were added in vitro.
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http://dx.doi.org/10.1159/000385987 | DOI Listing |
Biol Chem Hoppe Seyler
December 1994
Department of Medicine, Kobe University School of Medicine, Japan.
Meprin (EC 3.4.24.
View Article and Find Full Text PDFBiochim Biophys Acta
February 1989
Department of Medicine, Kobe University School of Medicine, Japan.
Parathyroid hormone (PTH) -degrading activity was studied using osteoblast-like UMR-106 cells. PTH-degrading activity was assessed by the amount of PTH fragments produced in the medium after exposure of intact human PTH-(1-84) to UMR-106 cells. PTH immunoreactivity recovered in trichloroacetic acid-soluble products of the medium and in fractions eluted from reverse-phase high-performance liquid chromatography (HPLC) was measured by radioimmunoassay using an antibody specific for the mid-region and C-terminus of PTH.
View Article and Find Full Text PDFBiochem Biophys Res Commun
December 1988
Department of Medicine, Kobe University School of Medicine, Japan.
To clarify the possible role of protein kinase C in the control of parathyroid hormone (PTH)-degrading activity (PTHDA) in a PTH-responsive opossum kidney (OK) cell line, we investigated the effects of protein kinase C activators, 12-O-tetradecanoyl phorbol 13-acetate (TPA), 1-oleoyl-2-acetyl-glycerol (OAG), and 4 beta-phorbol 12, 13-didecanoate (4 beta-PDD). TPA, OAG, and 4 beta-PDD enhanced PTHDA in a dose-dependent fashion (10-50 ng/ml, 10-100 microgram/ml, and 10-50 nM, respectively), whereas 4 alpha-PDD, a non-activator of protein kinase C, did not affect it. HPLC analysis of TPA-treated samples revealed increase of all immunoreactive PTH fragments produced by OK cells.
View Article and Find Full Text PDFEndocrinology
December 1988
Department of Medicine, Kobe University School of Medicine, Japan.
Cathepsin-D has been previously reported to cleave intact PTH into PTH-(1-34) and -(35-84) in membranous fractions of rat and bovine kidney. Whether PTH degradation occurs by intact kidney cells, however, has not been examined in detail. We have, therefore, examined this possibility using an opossum kidney (OK) cell line which possesses the characteristics of proximal renal tubules and responds to PTH.
View Article and Find Full Text PDFBone Miner
January 1988
Department of Medicine, Kobe University School of Medicine, Japan.
A possible new enzyme, a cytosolic neutral PTH-degrading enzyme previously described by us, was purified by ammonium sulfate fractionation, Sephadex G-200 column chromatography and DEAE cellulose column chromatography from the 100,000 x g supernatant of rat kidney. Three active peaks (designated P-I, P-II and P-III) were obtained through a DEAE cellulose chromatographic column. These three activity peaks were interchangeable on rechromatography.
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