Receptor da vitamina D: Diferenzas entre revisións

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As dianas ''augas abaixo'' da ruta deste receptor nuclear de hormonas están implicadas principalmente no metabolismo mineral aínda que o receptor regula unha variedade doutras vías metabólicas, como os implicados na [[resposta inmunitaria]] e o [[cancro]].<ref name="pmid16848743">{{cite journal | vauthors = Adorini L, Daniel KC, Penna G | title = Vitamin D receptor agonists, cancer and the immune system: an intricate relationship | journal = Curr Top Med Chem | volume = 6 | issue = 12 | pages = 1297–301 | year = 2006 | pmid = 16848743 | doi = 10.2174/156802606777864890 }}</ref>
As dianas ''augas abaixo'' da ruta deste receptor nuclear de hormonas están implicadas principalmente no metabolismo mineral aínda que o receptor regula unha variedade doutras vías metabólicas, como os implicados na [[resposta inmunitaria]] e o [[cancro]].<ref name="pmid16848743">{{cite journal | vauthors = Adorini L, Daniel KC, Penna G | title = Vitamin D receptor agonists, cancer and the immune system: an intricate relationship | journal = Curr Top Med Chem | volume = 6 | issue = 12 | pages = 1297–301 | year = 2006 | pmid = 16848743 | doi = 10.2174/156802606777864890 }}</ref>
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Mutations in this gene are associated with type II vitamin D-resistant [[rickets]]. A single nucleotide polymorphism in the initiation codon results in an alternate translation start site three codons downstream. Alternative splicing results in multiple transcript variants encoding the same protein.<ref name="entrez">{{cite web | title = Entrez Gene: VDR vitamin D (1,25- dihydroxyvitamin D3) receptor| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7421| accessdate = }}</ref>


As [[mutación]]s neste xene están asociadas co [[raquitismo]] resistente a vitamina D tipo II. Un [[polimorfismo dun só nucleótido]] no [[codón]] de iniciación ten como resultado un sitio alternativo de inicio da [[tradución de proteínas|tradución]] situado tres codóns ''[[augas abaixo]]''. O [[empalme alternativo]] dá lugar a múltiples variantes de empalme ou splicing que codifican a mesma proteína.<ref name="entrez">{{cite web | title = Entrez Gene: VDR vitamin D (1,25- dihydroxyvitamin D3) receptor| url = http]] de iniciacióni.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7421| accessdate = }}</ref>
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The vitamin D receptor plays an important role in regulating the hair cycle. Loss of VDR is associated with hair loss in experimental animals.<ref name="pmid20138991">{{cite journal | vauthors = Luderer HF, Demay MB | title = The vitamin D receptor, the skin and stem cells | journal = J. Steroid Biochem. Mol. Biol. | volume = 121 | issue = 1–2 | pages = 314–6 | date = July 2010 | pmid = 20138991 | doi = 10.1016/j.jsbmb.2010.01.015 }}</ref>
The vitamin D receptor plays an important role in regulating the hair cycle. Loss of VDR is associated with hair loss in experimental animals.<ref name="pmid20138991">{{cite journal | vauthors = Luderer HF, Demay MB | title = The vitamin D receptor, the skin and stem cells | journal = J. Steroid Biochem. Mol. Biol. | volume = 121 | issue = 1–2 | pages = 314–6 | date = July 2010 | pmid = 20138991 | doi = 10.1016/j.jsbmb.2010.01.015 }}</ref>
Experimental studies have shown that the unliganded VDR interacts with regulatory regions in cWnt ([[wnt signaling pathway]]) and [[sonic hedgehog]] target genes and is required for the induction of these pathways during the postnatal hair cycle.<ref name="pmid25180455">{{cite journal | vauthors = Lisse TS, Saini V, Zhao H, Luderer HF, Gori F, Demay MB | title = The Vitamin D Receptor Is Required for Activation of cWnt and Hedgehog Signaling in Keratinocytes | journal = Mol. Endocrinol. | volume = 28 | issue = 10 | pages = 1698–1706 | date = September 2014 | pmid = 25180455 | doi = 10.1210/me.2014-1043 | pmc=4179637}}</ref>
Experimental studies have shown that the unliganded VDR interacts with regulatory regions in cWnt ([[wnt signaling pathway]]) and [[sonic hedgehog]] target genes and is required for the induction of these pathways during the postnatal hair cycle.<ref name="pmid25180455">{{cite journal | vauthors = Lisse TS, Saini V, Zhao H, Luderer HF, Gori F, Demay MB | title = The Vitamin D Receptor Is Required for Activation of cWnt and Hedgehog Signaling in Keratinocytes | journal = Mol. Endocrinol. | volume = 28 | issue = 10 | pages = 1698–1706 | date = September 2014 | pmid = 25180455 | doi = 10.1210/me.2014-1043 | pmc=4179637}}</ref>

Revisión como estaba o 23 de xaneiro de 2018 ás 22:10

O receptor da vitamina D (VDR) ou receptor do calcitriol, tamén chamado NR1I1 (receptor nuclear familia 1, grupo I, membro 1), é un membro da familia do receptor nuclear de factores de transcrición.[1] O calcitriol, é a forma activa da vitamina D, e únese ao VDR, que despois forma un heterodímero co receptor X retinoide. Este despois únese aos elementos de resposta a hormonas do ADN, o que resulta na expresión ou transrepresión de produtos xénicos específicos. O VDR non só regulasas respostas transcricionais pero tamén implica mecanismos postranscricionais dirixidos por microARN.[2] En humanos, o receptor da vitamina D está codificado polo xene VDR situado no cromosoma 12 humano.[3]

Os glicocorticoides diminúen a expresión do VDR, que se expresa na maioría dos tecidos do corpo e regula o transporte intestinal de calcio, ferro e outros minerais.[4]

Función

Este xene codifica o receptor nuclear de hormonas para a vitamina D3 (calcitriol). Este receptor tamén funciona como receptor para o ácido biliar secundario ácido litocólico. O receptor pertence á familia dos factores reguladores transcricionais que actúas en trans e mostran unha similitude de secuencia cos receptores de hormonas tiroides e esteroides.[5]

As dianas augas abaixo da ruta deste receptor nuclear de hormonas están implicadas principalmente no metabolismo mineral aínda que o receptor regula unha variedade doutras vías metabólicas, como os implicados na resposta inmunitaria e o cancro.[6]

As mutacións neste xene están asociadas co raquitismo resistente a vitamina D tipo II. Un polimorfismo dun só nucleótido no codón de iniciación ten como resultado un sitio alternativo de inicio da tradución situado tres codóns augas abaixo. O empalme alternativo dá lugar a múltiples variantes de empalme ou splicing que codifican a mesma proteína.[7]

Interaccións

O receptor do calcitriol presenta interaccións con:

Notas

  1. ↑ Moore DD, Kato S, Xie W, Mangelsdorf DJ, Schmidt DR, Xiao R, Kliewer SA (December 2006). "International Union of Pharmacology. LXII. The NR1H and NR1I receptors: constitutive androstane receptor, pregnene X receptor, farnesoid X receptor alpha, farnesoid X receptor beta, liver X receptor alpha, liver X receptor beta, and vitamin D receptor". Pharmacol. Rev. 58 (4): 742–59. PMID 17132852. doi:10.1124/pr.58.4.6. 
  2. ↑ Lisse TS, Chun RF, Rieger S, Adams JS, Hewison M (June 2013). "Vitamin D activation of functionally distinct regulatory miRNAs in primary human osteoblasts". J Bone Miner Res. 28 (6): 1478–14788. PMID 23362149. doi:10.1002/jbmr.1882. 
  3. ↑ Szpirer J, Szpirer C, Riviere M, Levan G, Marynen P, Cassiman JJ, Wiese R, DeLuca HF (September 1991). "The Sp1 transcription factor gene (SP1) and the 1,25-dihydroxyvitamin D3 receptor gene (VDR) are colocalized on human chromosome arm 12q and rat chromosome 7". Genomics 11 (1): 168–73. PMID 1662663. doi:10.1016/0888-7543(91)90114-T. 
  4. ↑ Fleet JC, Schoch RD (August 2010). "Molecular Mechanisms for Regulation of Intestinal Calcium Absorption by Vitamin D and Other Factors". Crit Rev Clin Lab Sci 47 (4): 181–195. PMC 3235806. PMID 21182397. doi:10.3109/10408363.2010.536429. 
  5. ↑ Germain P, Staels B, Dacquet C, Spedding M, Laudet V (December 2006). "Overview of nomenclature of nuclear receptors". Pharmacol. Rev. 58 (4): 685–704. PMID 17132848. doi:10.1124/pr.58.4.2. 
  6. ↑ Adorini L, Daniel KC, Penna G (2006). "Vitamin D receptor agonists, cancer and the immune system: an intricate relationship". Curr Top Med Chem 6 (12): 1297–301. PMID 16848743. doi:10.2174/156802606777864890. 
  7. ↑ [http]] de iniciacióni.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7421 "Entrez Gene: VDR vitamin D (1,25- dihydroxyvitamin D3) receptor"] |url= incorrecto (Axuda). 
  8. ↑ Guzey M, Takayama S, Reed JC (December 2000). "BAG1L enhances trans-activation function of the vitamin D receptor". J. Biol. Chem. 275 (52): 40749–56. PMID 10967105. doi:10.1074/jbc.M004977200. 
  9. ↑ 9,0 9,1 9,2 9,3 9,4 Kitagawa H, Fujiki R, Yoshimura K, Mezaki Y, Uematsu Y, Matsui D, Ogawa S, Unno K, Okubo M, Tokita A, Nakagawa T, Ito T, Ishimi Y, Nagasawa H, Matsumoto T, Yanagisawa J, Kato S (June 2003). "The chromatin-remodeling complex WINAC targets a nuclear receptor to promoters and is impaired in Williams syndrome". Cell 113 (7): 905–17. PMID 12837248. doi:10.1016/S0092-8674(03)00436-7. 
  10. ↑ Zhao G, Simpson RU (2010). "Membrane Localization, Caveolin-3 Association and Rapid Actions of Vitamin D Receptor in Cardiac Myocytes". Steroids 75 (8–9): 555–9. PMC 2885558. PMID 20015453. doi:10.1016/j.steroids.2009.12.001. 
  11. ↑ 11,0 11,1 11,2 Ito M, Yuan CX, Malik S, Gu W, Fondell JD, Yamamura S, Fu ZY, Zhang X, Qin J, Roeder RG (March 1999). "Identity between TRAP and SMCC complexes indicates novel pathways for the function of nuclear receptors and diverse mammalian activators". Mol. Cell 3 (3): 361–70. PMID 10198638. doi:10.1016/S1097-2765(00)80463-3. 
  12. ↑ 12,0 12,1 Tagami T, Lutz WH, Kumar R, Jameson JL (December 1998). "The interaction of the vitamin D receptor with nuclear receptor corepressors and coactivators". Biochem. Biophys. Res. Commun. 253 (2): 358–63. PMID 9878542. doi:10.1006/bbrc.1998.9799. 
  13. ↑ 13,0 13,1 13,2 13,3 Puccetti E, Obradovic D, Beissert T, Bianchini A, Washburn B, Chiaradonna F, Boehrer S, Hoelzer D, Ottmann OG, Pelicci PG, Nervi C, Ruthardt M (December 2002). "AML-associated translocation products block vitamin D(3)-induced differentiation by sequestering the vitamin D(3) receptor". Cancer Res. 62 (23): 7050–8. PMID 12460926. 
  14. ↑ Herdick M, Steinmeyer A, Carlberg C (June 2000). "Antagonistic action of a 25-carboxylic ester analogue of 1alpha, 25-dihydroxyvitamin D3 is mediated by a lack of ligand-induced vitamin D receptor interaction with coactivators". J. Biol. Chem. 275 (22): 16506–12. PMID 10748178. doi:10.1074/jbc.M910000199. 
  15. ↑ 15,0 15,1 15,2 Zhang C, Baudino TA, Dowd DR, Tokumaru H, Wang W, MacDonald PN (November 2001). "Ternary complexes and cooperative interplay between NCoA-62/Ski-interacting protein and steroid receptor coactivators in vitamin D receptor-mediated transcription". J. Biol. Chem. 276 (44): 40614–20. PMID 11514567. doi:10.1074/jbc.M106263200. 
  16. ↑ He B, Wilson EM (March 2003). "Electrostatic Modulation in Steroid Receptor Recruitment of LXXLL and FXXLF Motifs". Mol. Cell. Biol. 23 (6): 2135–50. PMC 149467. PMID 12612084. doi:10.1128/MCB.23.6.2135-2150.2003. 
  17. ↑ 17,0 17,1 Baudino TA, Kraichely DM, Jefcoat SC, Winchester SK, Partridge NC, MacDonald PN (June 1998). "Isolation and characterization of a novel coactivator protein, NCoA-62, involved in vitamin D-mediated transcription". J. Biol. Chem. 273 (26): 16434–41. PMID 9632709. doi:10.1074/jbc.273.26.16434. 
  18. ↑ Vidal M, Ramana CV, Dusso AS (April 2002). "Stat1-Vitamin D Receptor Interactions Antagonize 1,25-Dihydroxyvitamin D Transcriptional Activity and Enhance Stat1-Mediated Transcription". Mol. Cell. Biol. 22 (8): 2777–87. PMC 133712. PMID 11909970. doi:10.1128/MCB.22.8.2777-2787.2002. 
  19. ↑ Ward JO, McConnell MJ, Carlile GW, Pandolfi PP, Licht JD, Freedman LP (December 2001). "The acute promyelocytic leukemia-associated protein, promyelocytic leukemia zinc finger, regulates 1,25-dihydroxyvitamin D(3)-induced monocytic differentiation of U937 cells through a physical interaction with vitamin D(3) receptor". Blood 98 (12): 3290–300. PMID 11719366. doi:10.1182/blood.V98.12.3290. 

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Ligazóns externas

Este artigo incorpora textos en dominio público da United States National Library of Medicine.

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