CYP24A1

CYP24A1

Cytochrome P450, family 24, subfamily A, polypeptide 1, also known as CYP24A1, is a human gene.cite web | title = Entrez Gene: CYP24A1 cytochrome P450, family 24, subfamily A, polypeptide 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1591| accessdate = ]

PBB_Summary
section_title =
summary_text = This gene encodes a member of the cytochrome P450 superfamily of enzymes. The cytochrome P450 proteins are monooxygenases which catalyze many reactions involved in drug metabolism and synthesis of cholesterol, steroids and other lipids. This mitochondrial protein initiates the degradation of 1,25-dihydroxyvitamin D3, the physiologically active form of vitamin D3, by hydroxylation of the side chain. In regulating the level of vitamin D3, this enzyme plays a role in calcium homeostasis and the vitamin D endocrine system.cite web | title = Entrez Gene: CYP24A1 cytochrome P450, family 24, subfamily A, polypeptide 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1591| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Okuda K, Usui E, Ohyama Y |title=Recent progress in enzymology and molecular biology of enzymes involved in vitamin D metabolism. |journal=J. Lipid Res. |volume=36 |issue= 8 |pages= 1641–52 |year= 1995 |pmid= 7595086 |doi=
*cite journal | author=Chen KS, DeLuca HF |title=Cloning of the human 1 alpha,25-dihydroxyvitamin D-3 24-hydroxylase gene promoter and identification of two vitamin D-responsive elements. |journal=Biochim. Biophys. Acta |volume=1263 |issue= 1 |pages= 1–9 |year= 1995 |pmid= 7632726 |doi=
*cite journal | author=Robertson NG, Khetarpal U, Gutiérrez-Espeleta GA, "et al." |title=Isolation of novel and known genes from a human fetal cochlear cDNA library using subtractive hybridization and differential screening. |journal=Genomics |volume=23 |issue= 1 |pages= 42–50 |year= 1995 |pmid= 7829101 |doi= 10.1006/geno.1994.1457
*cite journal | author=Chen ML, Heinrich G, Ohyama YI, "et al." |title=Expression of 25-hydroxyvitamin D3-24-hydroxylase mRNA in cultured human keratinocytes. |journal=Proc. Soc. Exp. Biol. Med. |volume=207 |issue= 1 |pages= 57–61 |year= 1994 |pmid= 7938037 |doi=
*cite journal | author=Labuda M, Lemieux N, Tihy F, "et al." |title=Human 25-hydroxyvitamin D 24-hydroxylase cytochrome P450 subunit maps to a different chromosomal location than that of pseudovitamin D-deficient rickets. |journal=J. Bone Miner. Res. |volume=8 |issue= 11 |pages= 1397–406 |year= 1994 |pmid= 8266831 |doi=
*cite journal | author=Hahn CN, Baker E, Laslo P, "et al." |title=Localization of the human vitamin D 24-hydroxylase gene (CYP24) to chromosome 20q13.2-->q13.3. |journal=Cytogenet. Cell Genet. |volume=62 |issue= 4 |pages= 192–3 |year= 1993 |pmid= 8440135 |doi=
*cite journal | author=Chen KS, Prahl JM, DeLuca HF |title=Isolation and expression of human 1,25-dihydroxyvitamin D3 24-hydroxylase cDNA. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=90 |issue= 10 |pages= 4543–7 |year= 1993 |pmid= 8506296 |doi=
*cite journal | author=Bland R, Walker EA, Hughes SV, "et al." |title=Constitutive expression of 25-hydroxyvitamin D3-1alpha-hydroxylase in a transformed human proximal tubule cell line: evidence for direct regulation of vitamin D metabolism by calcium. |journal=Endocrinology |volume=140 |issue= 5 |pages= 2027–34 |year= 1999 |pmid= 10218951 |doi=
*cite journal | author=Taniguchi T, Eto TA, Shiotsuki H, "et al." |title=Newly established assay method for 25-hydroxyvitamin D3 24-hydroxylase revealed much lower Km for 25-hydroxyvitamin D3 than for 1alpha,25-dihydroxyvitamin D3. |journal=J. Bone Miner. Res. |volume=16 |issue= 1 |pages= 57–62 |year= 2001 |pmid= 11149490 |doi=
*cite journal | author=Deloukas P, Matthews LH, Ashurst J, "et al." |title=The DNA sequence and comparative analysis of human chromosome 20. |journal=Nature |volume=414 |issue= 6866 |pages= 865–71 |year= 2002 |pmid= 11780052 |doi= 10.1038/414865a
*cite journal | author=Strausberg RL, Feingold EA, Grouse LH, "et al." |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899
*cite journal | author=Farhan H, Cross HS |title=Transcriptional inhibition of CYP24 by genistein. |journal=Ann. N. Y. Acad. Sci. |volume=973 |issue= |pages= 459–62 |year= 2003 |pmid= 12485911 |doi=
*cite journal | author=Theodoropoulos C, Demers C, Delvin E, "et al." |title=Calcitriol regulates the expression of the genes encoding the three key vitamin D3 hydroxylases and the drug-metabolizing enzyme CYP3A4 in the human fetal intestine. |journal=Clin. Endocrinol. (Oxf) |volume=58 |issue= 4 |pages= 489–99 |year= 2003 |pmid= 12641633 |doi=
*cite journal | author=Fritsche J, Mondal K, Ehrnsperger A, "et al." |title=Regulation of 25-hydroxyvitamin D3-1 alpha-hydroxylase and production of 1 alpha,25-dihydroxyvitamin D3 by human dendritic cells. |journal=Blood |volume=102 |issue= 9 |pages= 3314–6 |year= 2004 |pmid= 12855575 |doi= 10.1182/blood-2002-11-3521
*cite journal | author=Nguyen TM, Lieberherr M, Fritsch J, "et al." |title=The rapid effects of 1,25-dihydroxyvitamin D3 require the vitamin D receptor and influence 24-hydroxylase activity: studies in human skin fibroblasts bearing vitamin D receptor mutations. |journal=J. Biol. Chem. |volume=279 |issue= 9 |pages= 7591–7 |year= 2004 |pmid= 14665637 |doi= 10.1074/jbc.M309517200
*cite journal | author=Mimori K, Tanaka Y, Yoshinaga K, "et al." |title=Clinical significance of the overexpression of the candidate oncogene CYP24 in esophageal cancer. |journal=Ann. Oncol. |volume=15 |issue= 2 |pages= 236–41 |year= 2004 |pmid= 14760115 |doi=
*cite journal | author=Sawada N, Kusudo T, Sakaki T, "et al." |title=Novel metabolism of 1 alpha,25-dihydroxyvitamin D3 with C24-C25 bond cleavage catalyzed by human CYP24A1. |journal=Biochemistry |volume=43 |issue= 15 |pages= 4530–7 |year= 2004 |pmid= 15078099 |doi= 10.1021/bi030207f
*cite journal | author=Kusudo T, Sakaki T, Abe D, "et al." |title=Metabolism of A-ring diastereomers of 1alpha,25-dihydroxyvitamin D3 by CYP24A1. |journal=Biochem. Biophys. Res. Commun. |volume=321 |issue= 4 |pages= 774–82 |year= 2004 |pmid= 15358094 |doi= 10.1016/j.bbrc.2004.07.040
*cite journal | author=Pascussi JM, Robert A, Nguyen M, "et al." |title=Possible involvement of pregnane X receptor-enhanced CYP24 expression in drug-induced osteomalacia. |journal=J. Clin. Invest. |volume=115 |issue= 1 |pages= 177–86 |year= 2005 |pmid= 15630458 |doi= 10.1172/JCI200521867

PBB_Controls
update_page = yes
require_manual_inspection = no
update_protein_box = yes
update_summary = yes
update_citations = yes


Wikimedia Foundation. 2010.

Игры ⚽ Поможем написать курсовую

Look at other dictionaries:

  • CYP24A1 — Cytochrom P450 24A1 Größe 479 Aminosäuren Kofaktor Häm Bezeichner …   Deutsch Wikipedia

  • Cytochrom P450 24A1 — Masse/Länge Primärstruktur 479 Aminosäuren …   Deutsch Wikipedia

  • 24-Hydroxylase — Cytochrom P450 24A1 Größe 479 Aminosäuren Kofaktor Häm Bezeichner …   Deutsch Wikipedia

  • P450 24A1 — Cytochrom P450 24A1 Größe 479 Aminosäuren Kofaktor Häm Bezeichner …   Deutsch Wikipedia

  • Cholecalciferol — Strukturformel Allgemeines Trivialname Vitamin D3 …   Deutsch Wikipedia

  • Hypervitaminose D — Klassifikation nach ICD 10 E67.3 Hypervitaminose Vitamin D …   Deutsch Wikipedia

  • Metabolism — Cell metabolism redirects here. For the journal, see Cell Metabolism. Structure of adenosine triphosphate, a central intermediate in energy metabolism Metabolism (from Greek: μεταβολή metabolē , change or Greek: μεταβολισμός metabolismos,… …   Wikipedia

  • Dihydrofolate reductase — Ribbon diagram of human dihydrofolate reductase in complex with folate (blue). From PDB 1DRF …   Wikipedia

  • Cytochrome P450 — Oxidase (CYP2C9) Identifiers Symbol p450 Pfam …   Wikipedia

  • Methylenetetrahydrofolate reductase — methylene tetrahydrofolate reductase [NAD(P)H] Ribbon diagram of the active site of E. coli MTHFR. The flavin cofactor (top) is shown interacting with the bound substrate NADH.[1] …   Wikipedia

Share the article and excerpts

Direct link
Do a right-click on the link above
and select “Copy Link”