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Titolo:
Parathyroid hormone regulates 25-hydroxyvitamin D-3-24-hydroxylase mRNA byaltering its stability
Autore:
Zierold, C; Mings, JA; DeLuca, HF;
Indirizzi:
Univ Wisconsin, Dept Biochem, Madison, WI 53706 USA Univ Wisconsin Madison WI USA 53706 , Dept Biochem, Madison, WI 53706 USA
Titolo Testata:
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
fascicolo: 24, volume: 98, anno: 2001,
pagine: 13572 - 13576
SICI:
0027-8424(20011120)98:24<13572:PHR2DM>2.0.ZU;2-S
Fonte:
ISI
Lingua:
ENG
Soggetto:
RECEPTOR MESSENGER-RNA; VITAMIN-D; 24-HYDROXYLASE GENE; ELEMENT; REGION; IDENTIFICATION; CELLS; DESTABILIZATION; SEQUENCES; TURNOVER;
Keywords:
calcium metabolism; vitamin D endocrine system;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
19
Recensione:
Indirizzi per estratti:
Indirizzo: DeLuca, HF Univ Wisconsin, Dept Biochem, 433 Babcock Dr, Madison, WI 53706USA Univ Wisconsin 433 Babcock Dr Madison WI USA 53706 WI 53706 USA
Citazione:
C. Zierold et al., "Parathyroid hormone regulates 25-hydroxyvitamin D-3-24-hydroxylase mRNA byaltering its stability", P NAS US, 98(24), 2001, pp. 13572-13576

Abstract

The up-regulation of the 25-hydroxyvitamin D-3-24-hydroxylase by 1,25-dihydroxyvitamin D-3 [1,25(OH)(2)D-3] is well established and occurs at the transcriptional level through two vitamin D response elements in the promoter of the gene. However, the mechanism of down-regulation of the 24-hydroxylase by parathyroid hormone (PTH) has not yet been elucidated. To study the mechanism of PTH action, we used AOK-B50 cells, a porcine kidney-cell line with stably transfected opossum PTH receptor in which both the 24-hydroxylasemRNA and activity are down-regulated by PTH. Cells dosed with 1,25(OH)(2)D-3 at 0 h, and subsequently at 0, 1, 2, or 4 h with 100 nM of PTH, showed levels of 24-hydroxylase mRNA equivalent to 72.6, 65.3, 57.2, and 37.1%, respectively, of the levels found in cells dosed with 1,25(OH)2D3 only. All cells were collected 7 h after the initial 1,25(OH)(2)D-3 dose. This pattern of expression indicated that PTH does not act by repressing transcription but rather by making the mRNA for 24-hydroxylase susceptible to degradation. At least 1 h is required for PTH to act. Further RNA and protein synthesesare required for PTH to act. However, the sites and mechanism whereby PTH causes 24-hydroxylase mRNA degradation are unknown. Because the untranslated regions of genes can determine the stability of its transcripts, we studied the 5' untranslated region and the 3' untranslated region of the rat 24-hydroxylase gene by using reporter-gene strategy to identify possible PTH sites of action. None was found, suggesting that the destabilization site iselsewhere in the coding region.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 19/01/20 alle ore 15:17:07