Only bioactive forms of PTH (n-oxPTH and Met18(ox)-PTH) inhibit synthesis of sclerostin - evidence from in vitro and human studies
Sclerostin (SOST) is produced by osteocytes and is known as a negative regulator of bone homeostasis. Parathyroid hormone (PTH) regulates calcium, phosphate as well as vitamin D metabolism, and is a strong inhibitor of SOST synthesis in vitro and in vivo. PTH has two methionine amino acids (position...
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| Hauptverfasser: | , , , , , , , , , |
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| Dokumenttyp: | Article (Journal) |
| Sprache: | Englisch |
| Veröffentlicht: |
23 February 2024
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| In: |
Pflügers Archiv
Year: 2024, Jahrgang: 476, Heft: 6, Pages: 889-899 |
| ISSN: | 1432-2013 |
| DOI: | 10.1007/s00424-024-02928-x |
| Online-Zugang: | Verlag, kostenfrei, Volltext: https://doi.org/10.1007/s00424-024-02928-x
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| Verfasserangaben: | Mei Li, Ahmed A. Hasan, Chang Chu, Johann-Georg Hocher, Yvonne Liu, Xiaoli Zhang, Xin Chen, Benito Yard, Bernhard K. Krämer, Berthold Hocher |
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| 245 | 1 | 0 | |a Only bioactive forms of PTH (n-oxPTH and Met18(ox)-PTH) inhibit synthesis of sclerostin - evidence from in vitro and human studies |c Mei Li, Ahmed A. Hasan, Chang Chu, Johann-Georg Hocher, Yvonne Liu, Xiaoli Zhang, Xin Chen, Benito Yard, Bernhard K. Krämer, Berthold Hocher |
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| 520 | |a Sclerostin (SOST) is produced by osteocytes and is known as a negative regulator of bone homeostasis. Parathyroid hormone (PTH) regulates calcium, phosphate as well as vitamin D metabolism, and is a strong inhibitor of SOST synthesis in vitro and in vivo. PTH has two methionine amino acids (positions 8 and 18) which can be oxidized. PTH oxidized at Met18 (Met18(ox)-PTH) continues to be bioactive, whereas PTH oxidized at Met8 (Met8(ox)-PTH) or PTH oxidized at Met8 and Met18 (Met8, Met18(di-ox)-PTH) has minor bioactivity. How non-oxidized PTH (n-oxPTH) and oxidized forms of PTH act on sclerostin synthesis is unknown. The effects of n-oxPTH and oxidized forms of PTH on SOST gene expression were evaluated in UMR106 osteoblast-like cells. Moreover, we analyzed the relationship of SOST with n-oxPTH and all forms of oxPTH in 516 stable kidney transplant recipients using an assay system that can distinguish in clinical samples between n-oxPTH and the sum of all oxidized PTH forms (Met8(ox)-PTH, Met18(ox)-PTH, and Met8, Met18(di-ox)-PTH). We found that both n-oxPTH and Met18(ox)-PTH at doses of 1, 3, 20, and 30 nmol/L significantly inhibit SOST gene expression in vitro, whereas Met8(ox)-PTH and Met8, Met18(di-ox)-PTH only have a weak inhibitory effect on SOST gene expression. In the clinical cohort, multivariate linear regression showed that only n-oxPTH, but not intact PTH (iPTH) nor oxPTH, is independently associated with circulating SOST after adjusting for known confounding factors. In conclusion, only bioactive PTH forms such as n-oxPTH and Met18(ox)-PTH, inhibit SOST synthesis. | ||
| 650 | 4 | |a Adaptor Proteins, Signal Transducing | |
| 650 | 4 | |a Animals | |
| 650 | 4 | |a Bone Morphogenetic Proteins | |
| 650 | 4 | |a Cell Line | |
| 650 | 4 | |a Female | |
| 650 | 4 | |a Genetic Markers | |
| 650 | 4 | |a Humans | |
| 650 | 4 | |a KTRs | |
| 650 | 4 | |a Male | |
| 650 | 4 | |a Methionine | |
| 650 | 4 | |a Middle Aged | |
| 650 | 4 | |a Non-oxidized | |
| 650 | 4 | |a Osteoblasts | |
| 650 | 4 | |a Oxidation-Reduction | |
| 650 | 4 | |a Oxidized | |
| 650 | 4 | |a Parathyroid Hormone | |
| 650 | 4 | |a PTH | |
| 650 | 4 | |a Rats | |
| 650 | 4 | |a SOST | |
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