CYP24A1: Difference between revisions

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== Function ==
== Function ==
CYP24A1 is an enzyme expressed in the [[mitochondrion]] of humans and other species. It catalyzes hydroxylation reactions which lead to the degradation of [[1,25-dihydroxyvitamin D3|1,25-dihydroxyvitamin D<sub>3</sub>]], the physiologically active form of [[vitamin D]]. Hydroxylation of the side chain produces [[calcitroic acid]] and other metabolites which are excreted in [[bile]].<ref name="entrez"/><ref name="Jones2014">{{cite journal | vauthors = Jones G, Prosser DE, Kaufmann M | title = Cytochrome P450-mediated metabolism of vitamin D | journal = Journal of Lipid Research | volume = 55 | issue = 1 | pages = 13–31 | date = January 2014 | pmid = 23564710 | doi = 10.1194/jlr.R031534 }}</ref>
CYP24A1 is an enzyme expressed in the [[mitochondrion]] of humans and other species. It catalyzes hydroxylation reactions which lead to the degradation of [[1,25-dihydroxyvitamin D3|1,25-dihydroxyvitamin D<sub>3</sub>]], the physiologically active form of [[vitamin D]]. Hydroxylation of the side chain produces [[calcitroic acid]] and other metabolites which are excreted in [[bile]].<ref name="entrez"/><ref name="Jones2014">{{cite journal | vauthors = Jones G, Prosser DE, Kaufmann M | title = Cytochrome P450-mediated metabolism of vitamin D | journal = Journal of Lipid Research | volume = 55 | issue = 1 | pages = 13–31 | date = January 2014 | pmid = 23564710 | doi = 10.1194/jlr.R031534 | pmc=3927478}}</ref>


CYP24A1 was identified in the early 1970s and was first thought to be involved in vitamin D metabolism as the renal 25-hydroxyvitamin D3-24-hydroxylase, modifying [[calcifediol]] (25-hydroxyvitamin D) to produce [[24,25-dihydroxycholecalciferol]] (24,25-dihydroxyvitamin D).  Subsequent studies using recombinant CYP24A1 showed that it could also catalyze multiple other hydroxylation reactions at the side chain carbons known as C-24 and C-23 in both 25-OH-D<sub>3</sub> and the active hormonal form, 1,25-(OH)<sub>2</sub>D<sub>3</sub>.  It is now considered responsible for the entire five-step, 24-oxidation pathway from 1,25-(OH)<sub>2</sub>D<sub>3</sub> producing calcitroic acid.<ref name="pmid15574355">{{cite journal | vauthors = Sakaki T, Kagawa N, Yamamoto K, Inouye K | title = Metabolism of vitamin D3 by cytochromes P450 | journal = Frontiers in Bioscience | volume = 10 | issue =  | pages = 119–34 | date = January 2005 | pmid = 15574355 | doi = 10.2741/1514 | url = http://www.bioscience.org/2005/v10/af/1514/fulltext.htm }}</ref><ref name="Jones2014"/>
CYP24A1 was identified in the early 1970s and was first thought to be involved in vitamin D metabolism as the renal 25-hydroxyvitamin D3-24-hydroxylase, modifying [[calcifediol]] (25-hydroxyvitamin D) to produce [[24,25-dihydroxycholecalciferol]] (24,25-dihydroxyvitamin D).  Subsequent studies using recombinant CYP24A1 showed that it could also catalyze multiple other hydroxylation reactions at the side chain carbons known as C-24 and C-23 in both 25-OH-D<sub>3</sub> and the active hormonal form, 1,25-(OH)<sub>2</sub>D<sub>3</sub>.  It is now considered responsible for the entire five-step, 24-oxidation pathway from 1,25-(OH)<sub>2</sub>D<sub>3</sub> producing calcitroic acid.<ref name="Jones2014"/>


CYP24A1 also is able to catalyse another pathway which starts with 23-hydroxylation of 1,25-(OH)<sub>2</sub>D<sub>3</sub> and culminates in 1,25-(OH)<sub>2</sub>D<sub>3</sub>-26,23-lactone.<ref name="pmid15574355"/><ref name="Jones2014"/>
CYP24A1 also is able to catalyse another pathway which starts with 23-hydroxylation of 1,25-(OH)<sub>2</sub>D<sub>3</sub> and culminates in 1,25-(OH)<sub>2</sub>D<sub>3</sub>-26,23-lactone.<ref name="Jones2014"/>


The side chains of the [[ergocalciferol]] (vitamin D<sub>2</sub>) derivatives, 25-OH-D<sub>2</sub> and 1,25-(OH)<sub>2</sub>D<sub>2</sub>, are also hydroxylated by CYP24A1.<ref name="Jones2014"/>
The side chains of the [[ergocalciferol]] (vitamin D<sub>2</sub>) derivatives, 25-OH-D<sub>2</sub> and 1,25-(OH)<sub>2</sub>D<sub>2</sub>, are also hydroxylated by CYP24A1.<ref name="Jones2014"/>
Line 14: Line 14:
The structure of CYP24A1 is highly conserved between different species although the balance of functions can differ.<ref name="Jones2014"/>  Alternatively spliced transcript variants encoding different isoforms have been found for this gene.
The structure of CYP24A1 is highly conserved between different species although the balance of functions can differ.<ref name="Jones2014"/>  Alternatively spliced transcript variants encoding different isoforms have been found for this gene.


This enzyme plays an important  role in [[calcium homeostasis]] and the vitamin D endocrine system through its regulation of the level of vitamin D<sub>3</sub>.<ref name="pmid15574355"/>
This enzyme plays an important  role in [[calcium homeostasis]] and the vitamin D endocrine system through its regulation of the level of vitamin D<sub>3</sub>.


===Interactive pathway map===
===Interactive pathway map===
Line 22: Line 22:
CYP24A1 is expressed in tissues which are considered targets for vitamin D, including kidney, intestine and bone.  Transcription of the CYP24A1 gene is markedly inducible by 1,25-(OH)<sub>2</sub>D<sub>3</sub> binding to the [[vitamin D receptor]].<ref name="Jones2014"/>  The gene has a strong, positive [[VDRE|vitamin D response element]] in the [[Promoter (genetics)|promoter]]. Through regulation of CYP24A1 expression, a [[negative feedback]] control system is created to limit the effects of 1,25-(OH)<sub>2</sub>D<sub>3</sub>.<ref name="Jones2014"/>
CYP24A1 is expressed in tissues which are considered targets for vitamin D, including kidney, intestine and bone.  Transcription of the CYP24A1 gene is markedly inducible by 1,25-(OH)<sub>2</sub>D<sub>3</sub> binding to the [[vitamin D receptor]].<ref name="Jones2014"/>  The gene has a strong, positive [[VDRE|vitamin D response element]] in the [[Promoter (genetics)|promoter]]. Through regulation of CYP24A1 expression, a [[negative feedback]] control system is created to limit the effects of 1,25-(OH)<sub>2</sub>D<sub>3</sub>.<ref name="Jones2014"/>


[[Parathyroid hormone|PTH]] and [[FGF23]] also regulate CYP24A1 gene expression.<ref name="Jones2014"/> Additionally, it is translationally regulated via [[Internal ribosome entry site|IRES]] within the [[Five prime untranslated region|5'UTR]], which is responsive to an inflammatory environment.<ref>{{cite journal | vauthors = Rübsamen D, Kunze MM, Buderus V, Brauß TF, Bajer MM, Brüne B, Schmid T | title = Inflammatory conditions induce IRES-dependent translation of cyp24a1 | journal = PLoS One | volume = 9 | issue = 1 | pages = e85314 | date = 2014-01-01 | pmid = 24416388 | pmc = 3885688 | doi = 10.1371/journal.pone.0085314 }}</ref>
[[Parathyroid hormone|PTH]] and [[FGF23]] also regulate CYP24A1 gene expression.<ref name="Jones2014"/> Additionally, it is translationally regulated via [[Internal ribosome entry site|IRES]] within the [[Five prime untranslated region|5'UTR]], which is responsive to an inflammatory environment.<ref>{{cite journal | vauthors = Rübsamen D, Kunze MM, Buderus V, Brauß TF, Bajer MM, Brüne B, Schmid T | title = Inflammatory conditions induce IRES-dependent translation of cyp24a1 | journal = PLOS ONE | volume = 9 | issue = 1 | pages = e85314 | date = 2014-01-01 | pmid = 24416388 | pmc = 3885688 | doi = 10.1371/journal.pone.0085314 }}</ref>


==Clinical relevance==
==Clinical relevance==
Abnormal functioning CYP24A1 is thought to be one of the causes of severe infantile [[Hypercalcaemia|hypercalcemia]].<ref name="pmid22112808">{{cite journal | vauthors = Dauber A, Nguyen TT, Sochett E, Cole DE, Horst R, Abrams SA, Carpenter TO, Hirschhorn JN | title = Genetic defect in CYP24A1, the vitamin D 24-hydroxylase gene, in a patient with severe infantile hypercalcemia | journal = The Journal of Clinical Endocrinology and Metabolism | volume = 97 | issue = 2 | pages = E268-74 | date = February 2012 | pmid = 22112808 | pmc = 3275367 | doi = 10.1210/jc.2011-1972 }}</ref>  Patients with mutations of the CYP24A1 gene have elevated serum calcium concentrations, elevated serum 1,25-(OH)<sub>2</sub>D, suppressed PTH concentrations, hypercalciuria, nephrocalcinosis, nephrolithiasis, and sometimes reduced bone density. Variations in the gene may also be found in people with renal stones.<ref name="Tebben2016">{{cite journal | vauthors = Tebben PJ, Singh RJ, Kumar R | title = Vitamin D-Mediated Hypercalcemia: Mechanisms, Diagnosis, and Treatment | journal = Endocrine Reviews | volume = 37 | issue = 5 | pages = 521–547 | date = October 2016 | pmid = 27588937 | doi = 10.1210/er.2016-1070 }}</ref>
Abnormal functioning CYP24A1 is thought to be one of the causes of severe infantile [[Hypercalcaemia|hypercalcemia]].<ref name="pmid22112808">{{cite journal | vauthors = Dauber A, Nguyen TT, Sochett E, Cole DE, Horst R, Abrams SA, Carpenter TO, Hirschhorn JN | title = Genetic defect in CYP24A1, the vitamin D 24-hydroxylase gene, in a patient with severe infantile hypercalcemia | journal = The Journal of Clinical Endocrinology and Metabolism | volume = 97 | issue = 2 | pages = E268-74 | date = February 2012 | pmid = 22112808 | pmc = 3275367 | doi = 10.1210/jc.2011-1972 }}</ref>  Patients with mutations of the CYP24A1 gene have elevated serum calcium concentrations, elevated serum 1,25-(OH)<sub>2</sub>D, suppressed PTH concentrations, hypercalciuria, nephrocalcinosis, nephrolithiasis, and sometimes reduced bone density. Variations in the gene may also be found in people with renal stones.<ref name="Tebben2016">{{cite journal | vauthors = Tebben PJ, Singh RJ, Kumar R | title = Vitamin D-Mediated Hypercalcemia: Mechanisms, Diagnosis, and Treatment | journal = Endocrine Reviews | volume = 37 | issue = 5 | pages = 521–547 | date = October 2016 | pmid = 27588937 | doi = 10.1210/er.2016-1070 | pmc=5045493}}</ref>


== References ==
== References ==
Line 38: Line 38:
* {{cite journal | vauthors = 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 = Biochimica et Biophysica Acta | volume = 1263 | issue = 1 | pages = 1–9 | date = July 1995 | pmid = 7632726 | doi = 10.1016/0167-4781(95)00060-t }}
* {{cite journal | vauthors = 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 = Biochimica et Biophysica Acta | volume = 1263 | issue = 1 | pages = 1–9 | date = July 1995 | pmid = 7632726 | doi = 10.1016/0167-4781(95)00060-t }}
* {{cite journal | vauthors = Robertson NG, Khetarpal U, Gutiérrez-Espeleta GA, Bieber FR, Morton CC | 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 | date = September 1994 | pmid = 7829101 | doi = 10.1006/geno.1994.1457 }}
* {{cite journal | vauthors = Robertson NG, Khetarpal U, Gutiérrez-Espeleta GA, Bieber FR, Morton CC | 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 | date = September 1994 | pmid = 7829101 | doi = 10.1006/geno.1994.1457 }}
* {{cite journal | vauthors = Chen ML, Heinrich G, Ohyama YI, Okuda K, Omdahl JL, Chen TC, Holick MF | title = Expression of 25-hydroxyvitamin D3-24-hydroxylase mRNA in cultured human keratinocytes | journal = Proceedings of the Society for Experimental Biology and Medicine. Society for Experimental Biology and Medicine | volume = 207 | issue = 1 | pages = 57–61 | date = October 1994 | pmid = 7938037 | doi =  }}
* {{cite journal | vauthors = Chen ML, Heinrich G, Ohyama YI, Okuda K, Omdahl JL, Chen TC, Holick MF | title = Expression of 25-hydroxyvitamin D3-24-hydroxylase mRNA in cultured human keratinocytes | journal = Proceedings of the Society for Experimental Biology and Medicine. Society for Experimental Biology and Medicine | volume = 207 | issue = 1 | pages = 57–61 | date = October 1994 | pmid = 7938037 | doi =  10.3181/00379727-207-43791}}
* {{cite journal | vauthors = Labuda M, Lemieux N, Tihy F, Prinster C, Glorieux FH | title = Human 25-hydroxyvitamin D 24-hydroxylase cytochrome P450 subunit maps to a different chromosomal location than that of pseudovitamin D-deficient rickets | journal = Journal of Bone and Mineral Research | volume = 8 | issue = 11 | pages = 1397–406 | date = November 1993 | pmid = 8266831 | doi = 10.1002/jbmr.5650081114 }}
* {{cite journal | vauthors = Labuda M, Lemieux N, Tihy F, Prinster C, Glorieux FH | title = Human 25-hydroxyvitamin D 24-hydroxylase cytochrome P450 subunit maps to a different chromosomal location than that of pseudovitamin D-deficient rickets | journal = Journal of Bone and Mineral Research | volume = 8 | issue = 11 | pages = 1397–406 | date = November 1993 | pmid = 8266831 | doi = 10.1002/jbmr.5650081114 }}
* {{cite journal | vauthors = Hahn CN, Baker E, Laslo P, May BK, Omdahl JL, Sutherland GR | title = Localization of the human vitamin D 24-hydroxylase gene (CYP24) to chromosome 20q13.2-->q13.3 | journal = Cytogenetics and Cell Genetics | volume = 62 | issue = 4 | pages = 192–3 | year = 1993 | pmid = 8440135 | doi = 10.1159/000133473 }}
* {{cite journal | vauthors = Hahn CN, Baker E, Laslo P, May BK, Omdahl JL, Sutherland GR | title = Localization of the human vitamin D 24-hydroxylase gene (CYP24) to chromosome 20q13.2-->q13.3 | journal = Cytogenetics and Cell Genetics | volume = 62 | issue = 4 | pages = 192–3 | year = 1993 | pmid = 8440135 | doi = 10.1159/000133473 }}
Line 51: Line 51:
* {{cite journal | vauthors = Sawada N, Kusudo T, Sakaki T, Hatakeyama S, Hanada M, Abe D, Kamao M, Okano T, Ohta M, Inouye K | 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 | date = April 2004 | pmid = 15078099 | doi = 10.1021/bi030207f }}
* {{cite journal | vauthors = Sawada N, Kusudo T, Sakaki T, Hatakeyama S, Hanada M, Abe D, Kamao M, Okano T, Ohta M, Inouye K | 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 | date = April 2004 | pmid = 15078099 | doi = 10.1021/bi030207f }}
* {{cite journal | vauthors = Kusudo T, Sakaki T, Abe D, Fujishima T, Kittaka A, Takayama H, Hatakeyama S, Ohta M, Inouye K | title = Metabolism of A-ring diastereomers of 1alpha,25-dihydroxyvitamin D3 by CYP24A1 | journal = Biochemical and Biophysical Research Communications | volume = 321 | issue = 4 | pages = 774–82 | date = September 2004 | pmid = 15358094 | doi = 10.1016/j.bbrc.2004.07.040 }}
* {{cite journal | vauthors = Kusudo T, Sakaki T, Abe D, Fujishima T, Kittaka A, Takayama H, Hatakeyama S, Ohta M, Inouye K | title = Metabolism of A-ring diastereomers of 1alpha,25-dihydroxyvitamin D3 by CYP24A1 | journal = Biochemical and Biophysical Research Communications | volume = 321 | issue = 4 | pages = 774–82 | date = September 2004 | pmid = 15358094 | doi = 10.1016/j.bbrc.2004.07.040 }}
* {{cite journal | vauthors = Pascussi JM, Robert A, Nguyen M, Walrant-Debray O, Garabedian M, Martin P, Pineau T, Saric J, Navarro F, Maurel P, Vilarem MJ | title = Possible involvement of pregnane X receptor-enhanced CYP24 expression in drug-induced osteomalacia | journal = The Journal of Clinical Investigation | volume = 115 | issue = 1 | pages = 177–86 | date = January 2005 | pmid = 15630458 | pmc = 539191 | doi = 10.1172/JCI21867 }}
* {{cite journal | vauthors = Pascussi JM, Robert A, Nguyen M, Walrant-Debray O, Garabedian M, Martin P, Pineau T, Saric J, Navarro F, Maurel P, Vilarem MJ | title = Possible involvement of pregnane X receptor-enhanced CYP24 expression in drug-induced osteomalacia | journal = The Journal of Clinical Investigation | volume = 115 | issue = 1 | pages = 177–86 | date = January 2005 | pmid = 15630458 | pmc = 539191 | doi = 10.1172/JCI21867 | url = http://www.hal.inserm.fr/inserm-00086875/document }}
{{refend}}
{{refend}}


{{Cytochrome P450}}
{{Cytochrome P450}}
{{Metabolism of vitamins, coenzymes, and cofactors}}
{{Metabolism of vitamins, coenzymes, and cofactors}}

Revision as of 13:20, 4 November 2018

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Identifiers
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External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Cytochrome P450 family 24 subfamily A member 1 (abbreviated CYP24A1) is a member of the cytochrome P450 superfamily of enzymes encoded by the CYP24A1 gene. It is a mitochondrial monooxygenase which catalyzes reactions including 24-hydroxylation of calcitriol (1,25-dihydroxyvitamin D3).[1] It has also been identified as vitamin D3 24-hydroxylase.(EC 1.14.15.16)

Function

CYP24A1 is an enzyme expressed in the mitochondrion of humans and other species. It catalyzes hydroxylation reactions which lead to the degradation of 1,25-dihydroxyvitamin D3, the physiologically active form of vitamin D. Hydroxylation of the side chain produces calcitroic acid and other metabolites which are excreted in bile.[1][2]

CYP24A1 was identified in the early 1970s and was first thought to be involved in vitamin D metabolism as the renal 25-hydroxyvitamin D3-24-hydroxylase, modifying calcifediol (25-hydroxyvitamin D) to produce 24,25-dihydroxycholecalciferol (24,25-dihydroxyvitamin D). Subsequent studies using recombinant CYP24A1 showed that it could also catalyze multiple other hydroxylation reactions at the side chain carbons known as C-24 and C-23 in both 25-OH-D3 and the active hormonal form, 1,25-(OH)2D3. It is now considered responsible for the entire five-step, 24-oxidation pathway from 1,25-(OH)2D3 producing calcitroic acid.[2]

CYP24A1 also is able to catalyse another pathway which starts with 23-hydroxylation of 1,25-(OH)2D3 and culminates in 1,25-(OH)2D3-26,23-lactone.[2]

The side chains of the ergocalciferol (vitamin D2) derivatives, 25-OH-D2 and 1,25-(OH)2D2, are also hydroxylated by CYP24A1.[2]

The structure of CYP24A1 is highly conserved between different species although the balance of functions can differ.[2] Alternatively spliced transcript variants encoding different isoforms have been found for this gene.

This enzyme plays an important role in calcium homeostasis and the vitamin D endocrine system through its regulation of the level of vitamin D3.

Interactive pathway map

Click on genes, proteins and metabolites below to link to respective articles. [§ 1]

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<imagemap> Image:VitaminDSynthesis WP1531.png
|{{{bSize}}}px|alt=Vitamin D Synthesis Pathway (view / edit)]]
Vitamin D Synthesis Pathway (view / edit)
  1. ↑ The interactive pathway map can be edited at WikiPathways: "VitaminDSynthesis_WP1531".

Regulation

CYP24A1 is expressed in tissues which are considered targets for vitamin D, including kidney, intestine and bone. Transcription of the CYP24A1 gene is markedly inducible by 1,25-(OH)2D3 binding to the vitamin D receptor.[2] The gene has a strong, positive vitamin D response element in the promoter. Through regulation of CYP24A1 expression, a negative feedback control system is created to limit the effects of 1,25-(OH)2D3.[2]

PTH and FGF23 also regulate CYP24A1 gene expression.[2] Additionally, it is translationally regulated via IRES within the 5'UTR, which is responsive to an inflammatory environment.[3]

Clinical relevance

Abnormal functioning CYP24A1 is thought to be one of the causes of severe infantile hypercalcemia.[4] Patients with mutations of the CYP24A1 gene have elevated serum calcium concentrations, elevated serum 1,25-(OH)2D, suppressed PTH concentrations, hypercalciuria, nephrocalcinosis, nephrolithiasis, and sometimes reduced bone density. Variations in the gene may also be found in people with renal stones.[5]

References

  1. ↑ 1.0 1.1 "Entrez Gene: CYP24A1 cytochrome P450, family 24, subfamily A, polypeptide 1".
  2. ↑ 2.0 2.1 2.2 2.3 2.4 2.5 2.6 2.7 Jones G, Prosser DE, Kaufmann M (January 2014). "Cytochrome P450-mediated metabolism of vitamin D". Journal of Lipid Research. 55 (1): 13–31. doi:10.1194/jlr.R031534. PMC 3927478. PMID 23564710.
  3. ↑ Rübsamen D, Kunze MM, Buderus V, Brauß TF, Bajer MM, Brüne B, Schmid T (2014-01-01). "Inflammatory conditions induce IRES-dependent translation of cyp24a1". PLOS ONE. 9 (1): e85314. doi:10.1371/journal.pone.0085314. PMC 3885688. PMID 24416388.
  4. ↑ Dauber A, Nguyen TT, Sochett E, Cole DE, Horst R, Abrams SA, Carpenter TO, Hirschhorn JN (February 2012). "Genetic defect in CYP24A1, the vitamin D 24-hydroxylase gene, in a patient with severe infantile hypercalcemia". The Journal of Clinical Endocrinology and Metabolism. 97 (2): E268–74. doi:10.1210/jc.2011-1972. PMC 3275367. PMID 22112808.
  5. ↑ Tebben PJ, Singh RJ, Kumar R (October 2016). "Vitamin D-Mediated Hypercalcemia: Mechanisms, Diagnosis, and Treatment". Endocrine Reviews. 37 (5): 521–547. doi:10.1210/er.2016-1070. PMC 5045493. PMID 27588937.

External links

Further reading

  • Okuda K, Usui E, Ohyama Y (August 1995). "Recent progress in enzymology and molecular biology of enzymes involved in vitamin D metabolism". Journal of Lipid Research. 36 (8): 1641–52. PMID 7595086.
  • Chen KS, DeLuca HF (July 1995). "Cloning of the human 1 alpha,25-dihydroxyvitamin D-3 24-hydroxylase gene promoter and identification of two vitamin D-responsive elements". Biochimica et Biophysica Acta. 1263 (1): 1–9. doi:10.1016/0167-4781(95)00060-t. PMID 7632726.
  • Robertson NG, Khetarpal U, Gutiérrez-Espeleta GA, Bieber FR, Morton CC (September 1994). "Isolation of novel and known genes from a human fetal cochlear cDNA library using subtractive hybridization and differential screening". Genomics. 23 (1): 42–50. doi:10.1006/geno.1994.1457. PMID 7829101.
  • Chen ML, Heinrich G, Ohyama YI, Okuda K, Omdahl JL, Chen TC, Holick MF (October 1994). "Expression of 25-hydroxyvitamin D3-24-hydroxylase mRNA in cultured human keratinocytes". Proceedings of the Society for Experimental Biology and Medicine. Society for Experimental Biology and Medicine. 207 (1): 57–61. doi:10.3181/00379727-207-43791. PMID 7938037.
  • Labuda M, Lemieux N, Tihy F, Prinster C, Glorieux FH (November 1993). "Human 25-hydroxyvitamin D 24-hydroxylase cytochrome P450 subunit maps to a different chromosomal location than that of pseudovitamin D-deficient rickets". Journal of Bone and Mineral Research. 8 (11): 1397–406. doi:10.1002/jbmr.5650081114. PMID 8266831.
  • Hahn CN, Baker E, Laslo P, May BK, Omdahl JL, Sutherland GR (1993). "Localization of the human vitamin D 24-hydroxylase gene (CYP24) to chromosome 20q13.2-->q13.3". Cytogenetics and Cell Genetics. 62 (4): 192–3. doi:10.1159/000133473. PMID 8440135.
  • Chen KS, Prahl JM, DeLuca HF (May 1993). "Isolation and expression of human 1,25-dihydroxyvitamin D3 24-hydroxylase cDNA". Proceedings of the National Academy of Sciences of the United States of America. 90 (10): 4543–7. doi:10.1073/pnas.90.10.4543. PMC 46548. PMID 8506296.
  • Bland R, Walker EA, Hughes SV, Stewart PM, Hewison M (May 1999). "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". Endocrinology. 140 (5): 2027–34. doi:10.1210/en.140.5.2027. PMID 10218951.
  • Taniguchi T, Eto TA, Shiotsuki H, Sueta H, Higashi S, Iwamura T, Okuda KI, Setoguchi T (January 2001). "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 of Bone and Mineral Research. 16 (1): 57–62. doi:10.1359/jbmr.2001.16.1.57. PMID 11149490.
  • Farhan H, Cross HS (November 2002). "Transcriptional inhibition of CYP24 by genistein". Annals of the New York Academy of Sciences. 973: 459–62. doi:10.1111/j.1749-6632.2002.tb04683.x. PMID 12485911.
  • Theodoropoulos C, Demers C, Delvin E, Ménard D, Gascon-Barré M (April 2003). "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". Clinical Endocrinology. 58 (4): 489–99. doi:10.1046/j.1365-2265.2003.01743.x. PMID 12641633.
  • Fritsche J, Mondal K, Ehrnsperger A, Andreesen R, Kreutz M (November 2003). "Regulation of 25-hydroxyvitamin D3-1 alpha-hydroxylase and production of 1 alpha,25-dihydroxyvitamin D3 by human dendritic cells". Blood. 102 (9): 3314–6. doi:10.1182/blood-2002-11-3521. PMID 12855575.
  • Nguyen TM, Lieberherr M, Fritsch J, Guillozo H, Alvarez ML, Fitouri Z, Jehan F, Garabédian M (February 2004). "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". The Journal of Biological Chemistry. 279 (9): 7591–7. doi:10.1074/jbc.M309517200. PMID 14665637.
  • Mimori K, Tanaka Y, Yoshinaga K, Masuda T, Yamashita K, Okamoto M, Inoue H, Mori M (February 2004). "Clinical significance of the overexpression of the candidate oncogene CYP24 in esophageal cancer". Annals of Oncology. 15 (2): 236–41. doi:10.1093/annonc/mdh056. PMID 14760115.
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