Proline oxidase: Difference between revisions

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Proline dehydrogenase, mitochondrial is an enzyme that in humans is encoded by the PRODH gene.^[1]^[2]^[3]

The protein encoded by this gene is a mitochondrial proline dehydrogenase which catalyzes the first step in proline catabolism. Deletion of this gene has been associated with type I hyperprolinemia. The gene is located on chromosome 22q11.21, a region which has also been associated with the contiguous gene deletion syndromes: DiGeorge syndrome and CATCH22 syndrome.^[3]

Function

Proline oxidase, or proline dehydrogenase, functions as the initiator of the proline cycle. Proline metabolism is especially important in nutrient stress because proline is readily available from the breakdown of extracellular matrix (ECM), and the degradation of proline through the proline cycle initiated by proline oxidase (PRODH), a mitochondrial inner membrane enzyme, can generate ATP. This degradative pathway generates glutamate and alpha-ketoglutarate, products that can play an anaplerotic role for the TCA cycle.The proline cycle is also in a metabolic interlock with the pentose phosphate pathway providing another bioenergetic mechanism. The induction of stress either by glucose withdrawal or by treatment with rapamycin, stimulated degradation of proline and increased PRODH catalytic activity. Under these conditions PRODH was responsible, at least in part, for maintenance of ATP levels. Activation of AMP-activated protein kinase (AMPK), the cellular energy sensor, by 5-aminoimidazole-4-carboxamide ribonucleoside (AICAR), also markedly upregulated PRODH and increased PRODH-dependent ATP levels, further supporting its role during stress. Glucose deprivation increased intracellular proline levels, and expression of PRODH activated the pentose phosphate pathway. Therefore, the induction of the proline cycle under conditions of nutrient stress may be a mechanism by which cells switch to a catabolic mode for maintaining cellular energy levels.^[4]

Clinical significance

Mutations in the PRODH gene are associated with Proline Dehydrogenase deficiency. Many case studies have reported on this genetic disorder. In one such case study, 4 unrelated patients with HPI and a severe neurologic phenotype were shown to have the following common features: psychomotor delay from birth, often associated with hypotonia, severe language delay, autistic features, behavioral problems, and seizures. One patient who was heterozygous for a 22q11 microdeletion also had dysmorphic features. Four previously reported patients with HPI and neurologic involvement had a similar phenotype. This case study showed that Hyperprolinemia, Type I (HPI) may not always be a benign condition, and that the severity of the clinical phenotype appears to correlate with the serum proline level.^[5] Still, in another case study, clinical features from 4 unrelated patients included early motor and cognitive developmental delay, speech delay, autistic features, hyperactivity, stereotypic behaviors, and seizures. All patients had increased plasma and urine proline levels. All patients had biallelic mutations in the PRODH gene, often with several variants on the same allele. Residual enzyme activity ranged from null in the most severely affected patient to 25 to 30% in those with a relatively milder phenotype.^[6]

References

↑ Campbell HD, Webb GC, Young IG (Nov 1997). "A human homologue of the Drosophila melanogaster sluggish-A (proline oxidase) gene maps to 22q11.2, and is a candidate gene for type-I hyperprolinaemia". Human Genetics. 101 (1): 69–74. doi:10.1007/s004390050589. PMID 9385373.
↑ Gogos JA, Santha M, Takacs Z, Beck KD, Luine V, Lucas LR, Nadler JV, Karayiorgou M (Apr 1999). "The gene encoding proline dehydrogenase modulates sensorimotor gating in mice". Nature Genetics. 21 (4): 434–9. doi:10.1038/7777. PMID 10192398.
↑ ^3.0 ^3.1 "Entrez Gene: PRODH proline dehydrogenase (oxidase) 1".
↑ Pandhare J, Donald SP, Cooper SK, Phang JM (Jul 2009). "Regulation and function of proline oxidase under nutrient stress". Journal of Cellular Biochemistry. 107 (4): 759–68. doi:10.1002/jcb.22174. PMC 2801574. PMID 19415679.
↑ Afenjar A, Moutard ML, Doummar D, Guët A, Rabier D, Vermersch AI, Mignot C, Burglen L, Heron D, Thioulouse E, de Villemeur TB, Campion D, Rodriguez D (Oct 2007). "Early neurological phenotype in 4 children with biallelic PRODH mutations". Brain & Development. 29 (9): 547–52. doi:10.1016/j.braindev.2007.01.008. PMID 17412540.
↑ Perry TL, Hardwick DF, Lowry RB, Hansen S (May 1968). "Hyperprolinaemia in two successive generations of a North American Indian family". Annals of Human Genetics. 31 (4): 401–7. doi:10.1111/j.1469-1809.1968.tb00573.x. PMID 4299764.

External links

Proline+oxidase at the US National Library of Medicine Medical Subject Headings (MeSH)

[pmid9385373-1] Campbell HD, Webb GC, Young IG (Nov 1997). "A human homologue of the Drosophila melanogaster sluggish-A (proline oxidase) gene maps to 22q11.2, and is a candidate gene for type-I hyperprolinaemia". Human Genetics. 101 (1): 69–74. doi:10.1007/s004390050589. PMID 9385373.

[pmid10192398-2] Gogos JA, Santha M, Takacs Z, Beck KD, Luine V, Lucas LR, Nadler JV, Karayiorgou M (Apr 1999). "The gene encoding proline dehydrogenase modulates sensorimotor gating in mice". Nature Genetics. 21 (4): 434–9. doi:10.1038/7777. PMID 10192398.

[entrez-3] 3.0 ^3.1 "Entrez Gene: PRODH proline dehydrogenase (oxidase) 1".

[4] Pandhare J, Donald SP, Cooper SK, Phang JM (Jul 2009). "Regulation and function of proline oxidase under nutrient stress". Journal of Cellular Biochemistry. 107 (4): 759–68. doi:10.1002/jcb.22174. PMC 2801574. PMID 19415679.

[5] Afenjar A, Moutard ML, Doummar D, Guët A, Rabier D, Vermersch AI, Mignot C, Burglen L, Heron D, Thioulouse E, de Villemeur TB, Campion D, Rodriguez D (Oct 2007). "Early neurological phenotype in 4 children with biallelic PRODH mutations". Brain & Development. 29 (9): 547–52. doi:10.1016/j.braindev.2007.01.008. PMID 17412540.

[6] Perry TL, Hardwick DF, Lowry RB, Hansen S (May 1968). "Hyperprolinaemia in two successive generations of a North American Indian family". Annals of Human Genetics. 31 (4): 401–7. doi:10.1111/j.1469-1809.1968.tb00573.x. PMID 4299764.

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@@ Line 1: / Line 1: @@
-{{PBB|geneid=5625}}
+{{Infobox_gene}}
-{{SI}}
+'''Proline dehydrogenase, mitochondrial''' is an [[enzyme]] that in humans is encoded by the ''PRODH'' [[gene]].<ref name="pmid9385373">{{cite journal | vauthors = Campbell HD, Webb GC, Young IG | title = A human homologue of the Drosophila melanogaster sluggish-A (proline oxidase) gene maps to 22q11.2, and is a candidate gene for type-I hyperprolinaemia | journal = Human Genetics | volume = 101 | issue = 1 | pages = 69–74 | date = Nov 1997 | pmid = 9385373 | pmc =  | doi = 10.1007/s004390050589 }}</ref><ref name="pmid10192398">{{cite journal | vauthors = Gogos JA, Santha M, Takacs Z, Beck KD, Luine V, Lucas LR, Nadler JV, Karayiorgou M | title = The gene encoding proline dehydrogenase modulates sensorimotor gating in mice | journal = Nature Genetics | volume = 21 | issue = 4 | pages = 434–9 | date = Apr 1999 | pmid = 10192398 | pmc =  | doi = 10.1038/7777 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: PRODH proline dehydrogenase (oxidase) 1| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5625| accessdate = }}</ref>
-{{EH}}
-'''Proline dehydrogenase (oxidase) 1''', also known as '''PRODH''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PRODH proline dehydrogenase (oxidase) 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5625| accessdate = }}</ref>
+The protein encoded by this gene is a [[mitochondria]]l proline [[dehydrogenase]] which catalyzes the first step in [[proline]] catabolism. Deletion of this gene has been associated with type I [[hyperprolinemia]]. The gene is located on [[chromosome 22]]q11.21, a region which has also been associated with the contiguous gene deletion syndromes: [[DiGeorge syndrome]] and [[CATCH22 syndrome]].<ref name="entrez"/>
-<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
+== Function ==
-{{PBB_Summary
-| section_title =
-| summary_text = The protein encoded by this gene is a mitochondrial proline dehydrogenase which catalyzes the first step in proline catabolism. Deletion of this gene has been associated with type I hyperprolinemia. The gene is located on chromosome 22q11.21, a region which has also been associated with the contiguous gene deletion syndromes DiGeorge syndrome and CATCH22 syndrome.<ref name="entrez">{{cite web | title = Entrez Gene: PRODH proline dehydrogenase (oxidase) 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5625| accessdate = }}</ref>
-}}
-==References==
+Proline oxidase, or proline dehydrogenase, functions as the initiator of the proline cycle. [[Proline]] metabolism is especially important in nutrient stress because proline is readily available from the breakdown of extracellular matrix (ECM), and the degradation of proline through the proline cycle initiated by proline oxidase (PRODH), a [[mitochondrial inner membrane]] enzyme, can generate [[Adenosine triphosphate|ATP]]. This degradative pathway generates [[glutamate]] and [[alpha-ketoglutarate]], products that can play an anaplerotic role for the [[TCA cycle]].The proline cycle is also in a metabolic interlock with the pentose phosphate pathway providing another bioenergetic mechanism. The induction of stress either by glucose withdrawal or by treatment with [[rapamycin]], stimulated degradation of proline and increased PRODH catalytic activity. Under these conditions PRODH was responsible, at least in part, for maintenance of ATP levels. Activation of AMP-activated protein kinase ([[AMPK]]), the cellular energy sensor, by 5-aminoimidazole-4-carboxamide ribonucleoside (AICAR), also markedly upregulated PRODH and increased PRODH-dependent ATP levels, further supporting its role during stress. Glucose deprivation increased intracellular proline levels, and expression of PRODH activated the [[pentose phosphate pathway]]. Therefore, the induction of the proline cycle under conditions of nutrient stress may be a mechanism by which cells switch to a catabolic mode for maintaining cellular energy levels.<ref>{{cite journal | vauthors = Pandhare J, Donald SP, Cooper SK, Phang JM | title = Regulation and function of proline oxidase under nutrient stress | journal = Journal of Cellular Biochemistry | volume = 107 | issue = 4 | pages = 759–68 | date = Jul 2009 | pmid = 19415679 | doi = 10.1002/jcb.22174 | pmc=2801574}}</ref>
-{{reflist|2}}
-==Further reading==
+==Clinical significance==
-{{refbegin | 2}}
+Mutations in the PRODH gene are associated with Proline Dehydrogenase deficiency. Many case studies have reported on this genetic disorder. In one such case study, 4 unrelated patients with HPI and a severe neurologic phenotype were shown to have the following common features: psychomotor delay from birth, often associated with hypotonia, severe language delay, autistic features, behavioral problems, and seizures. One patient who was heterozygous for a 22q11 microdeletion also had dysmorphic features. Four previously reported patients with HPI and neurologic involvement had a similar phenotype. This case study showed that [[Hyperprolinemia]], Type I (HPI) may not always be a benign condition, and that the severity of the clinical phenotype appears to correlate with the serum proline level.<ref>{{cite journal | vauthors = Afenjar A, Moutard ML, Doummar D, Guët A, Rabier D, Vermersch AI, Mignot C, Burglen L, Heron D, Thioulouse E, de Villemeur TB, Campion D, Rodriguez D | title = Early neurological phenotype in 4 children with biallelic PRODH mutations | journal = Brain & Development | volume = 29 | issue = 9 | pages = 547–52 | date = Oct 2007 | pmid = 17412540 | doi = 10.1016/j.braindev.2007.01.008 }}</ref> Still, in another case study, clinical features from 4 unrelated patients included early motor and cognitive developmental delay, speech delay, autistic features, hyperactivity, stereotypic behaviors, and seizures. All patients had increased plasma and urine proline levels. All patients had biallelic mutations in the PRODH gene, often with several variants on the same allele. Residual enzyme activity ranged from null in the most severely affected patient to 25 to 30% in those with a relatively milder phenotype.<ref>{{cite journal | vauthors = Perry TL, Hardwick DF, Lowry RB, Hansen S | title = Hyperprolinaemia in two successive generations of a North American Indian family | journal = Annals of Human Genetics | volume = 31 | issue = 4 | pages = 401–7 | date = May 1968 | pmid = 4299764 | doi=10.1111/j.1469-1809.1968.tb00573.x}}</ref>
-{{PBB_Further_reading
-| citations =
+== References ==
-*{{cite journal  | author=Polyak K, Xia Y, Zweier JL, ''et al.'' |title=A model for p53-induced apoptosis. |journal=Nature |volume=389 |issue= 6648 |pages= 300-5 |year= 1997 |pmid= 9305847 |doi= 10.1038/38525 }}
+{{reflist|33em}}
-*{{cite journal  | author=Campbell HD, Webb GC, Young IG |title=A human homologue of the Drosophila melanogaster sluggish-A (proline oxidase) gene maps to 22q11.2, and is a candidate gene for type-I hyperprolinaemia. |journal=Hum. Genet. |volume=101 |issue= 1 |pages= 69-74 |year= 1997 |pmid= 9385373 |doi=  }}
-*{{cite journal  | author=Gogos JA, Santha M, Takacs Z, ''et al.'' |title=The gene encoding proline dehydrogenase modulates sensorimotor gating in mice. |journal=Nat. Genet. |volume=21 |issue= 4 |pages= 434-9 |year= 1999 |pmid= 10192398 |doi= 10.1038/7777 }}
+== Further reading ==
-*{{cite journal  | author=Donald SP, Sun XY, Hu CA, ''et al.'' |title=Proline oxidase, encoded by p53-induced gene-6, catalyzes the generation of proline-dependent reactive oxygen species. |journal=Cancer Res. |volume=61 |issue= 5 |pages= 1810-5 |year= 2001 |pmid= 11280728 |doi=  }}
+{{refbegin|33em}}
-*{{cite journal  | author=Liu H, Heath SC, Sobin C, ''et al.'' |title=Genetic variation at the 22q11 PRODH2/DGCR6 locus presents an unusual pattern and increases susceptibility to schizophrenia. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 6 |pages= 3717-22 |year= 2002 |pmid= 11891283 |doi= 10.1073/pnas.042700699 }}
+* {{cite journal | vauthors = Kempf L, Nicodemus KK, Kolachana B, Vakkalanka R, Verchinski BA, Egan MF, Straub RE, Mattay VA, Callicott JH, Weinberger DR, Meyer-Lindenberg A | title = Functional polymorphisms in PRODH are associated with risk and protection for schizophrenia and fronto-striatal structure and function | journal = PLoS Genetics | volume = 4 | issue = 11 | pages = e1000252 | date = Nov 2008 | pmid = 18989458 | pmc = 2573019 | doi = 10.1371/journal.pgen.1000252 | editor1-last = Katsanis | editor1-first = Nicholas }}
-*{{cite journal  | author=Jacquet H, Raux G, Thibaut F, ''et al.'' |title=PRODH mutations and hyperprolinemia in a subset of schizophrenic patients. |journal=Hum. Mol. Genet. |volume=11 |issue= 19 |pages= 2243-9 |year= 2003 |pmid= 12217952 |doi=  }}
+* {{cite journal | vauthors = Polyak K, Xia Y, Zweier JL, Kinzler KW, Vogelstein B | title = A model for p53-induced apoptosis | journal = Nature | volume = 389 | issue = 6648 | pages = 300–5 | date = Sep 1997 | pmid = 9305847 | doi = 10.1038/38525 }}
-*{{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 | vauthors = Donald SP, Sun XY, Hu CA, Yu J, Mei JM, Valle D, Phang JM | title = Proline oxidase, encoded by p53-induced gene-6, catalyzes the generation of proline-dependent reactive oxygen species | journal = Cancer Research | volume = 61 | issue = 5 | pages = 1810–5 | date = Mar 2001 | pmid = 11280728 | doi =  }}
-*{{cite journal  | author=Maxwell SA, Rivera A |title=Proline oxidase induces apoptosis in tumor cells, and its expression is frequently absent or reduced in renal carcinomas. |journal=J. Biol. Chem. |volume=278 |issue= 11 |pages= 9784-9 |year= 2003 |pmid= 12514185 |doi= 10.1074/jbc.M210012200 }}
+* {{cite journal | vauthors = Liu H, Heath SC, Sobin C, Roos JL, Galke BL, Blundell ML, Lenane M, Robertson B, Wijsman EM, Rapoport JL, Gogos JA, Karayiorgou M | title = Genetic variation at the 22q11 PRODH2/DGCR6 locus presents an unusual pattern and increases susceptibility to schizophrenia | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 99 | issue = 6 | pages = 3717–22 | date = Mar 2002 | pmid = 11891283 | pmc = 122590 | doi = 10.1073/pnas.042700699 }}
-*{{cite journal  | author=Jacquet H, Berthelot J, Bonnemains C, ''et al.'' |title=The severe form of type I hyperprolinaemia results from homozygous inactivation of the PRODH gene. |journal=J. Med. Genet. |volume=40 |issue= 1 |pages= e7 |year= 2003 |pmid= 12525555 |doi=  }}
+* {{cite journal | vauthors = Jacquet H, Raux G, Thibaut F, Hecketsweiler B, Houy E, Demilly C, Haouzir S, Allio G, Fouldrin G, Drouin V, Bou J, Petit M, Campion D, Frébourg T | title = PRODH mutations and hyperprolinemia in a subset of schizophrenic patients | journal = Human Molecular Genetics | volume = 11 | issue = 19 | pages = 2243–9 | date = Sep 2002 | pmid = 12217952 | doi = 10.1093/hmg/11.19.2243 }}
-*{{cite journal  | author=Williams HJ, Williams N, Spurlock G, ''et al.'' |title=Detailed analysis of PRODH and PsPRODH reveals no association with schizophrenia. |journal=Am. J. Med. Genet. B Neuropsychiatr. Genet. |volume=120 |issue= 1 |pages= 42-6 |year= 2004 |pmid= 12815738 |doi= 10.1002/ajmg.b.20049 }}
+* {{cite journal | vauthors = Maxwell SA, Rivera A | title = Proline oxidase induces apoptosis in tumor cells, and its expression is frequently absent or reduced in renal carcinomas | journal = The Journal of Biological Chemistry | volume = 278 | issue = 11 | pages = 9784–9 | date = Mar 2003 | pmid = 12514185 | doi = 10.1074/jbc.M210012200 }}
-*{{cite journal  | author=Ota T, Suzuki Y, Nishikawa T, ''et al.'' |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40-5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
+* {{cite journal | vauthors = Jacquet H, Berthelot J, Bonnemains C, Simard G, Saugier-Veber P, Raux G, Campion D, Bonneau D, Frebourg T | title = The severe form of type I hyperprolinaemia results from homozygous inactivation of the PRODH gene | journal = Journal of Medical Genetics | volume = 40 | issue = 1 | pages = e7 | date = Jan 2003 | pmid = 12525555 | pmc = 1735267 | doi = 10.1136/jmg.40.1.e7 }}
-*{{cite journal  | author=Li T, Ma X, Sham PC, ''et al.'' |title=Evidence for association between novel polymorphisms in the PRODH gene and schizophrenia in a Chinese population. |journal=Am. J. Med. Genet. B Neuropsychiatr. Genet. |volume=129 |issue= 1 |pages= 13-5 |year= 2005 |pmid= 15274030 |doi= 10.1002/ajmg.b.30049 }}
+* {{cite journal | vauthors = Williams HJ, Williams N, Spurlock G, Norton N, Zammit S, Kirov G, Owen MJ, O'Donovan MC | title = Detailed analysis of PRODH and PsPRODH reveals no association with schizophrenia | journal = American Journal of Medical Genetics Part B | volume = 120B | issue = 1 | pages = 42–6 | date = Jul 2003 | pmid = 12815738 | doi = 10.1002/ajmg.b.20049 }}
-*{{cite journal  | author=Zhang M, White TA, Schuermann JP, ''et al.'' |title=Structures of the Escherichia coli PutA proline dehydrogenase domain in complex with competitive inhibitors. |journal=Biochemistry |volume=43 |issue= 39 |pages= 12539-48 |year= 2004 |pmid= 15449943 |doi= 10.1021/bi048737e }}
+* {{cite journal | vauthors = Li T, Ma X, Sham PC, Sun X, Hu X, Wang Q, Meng H, Deng W, Liu X, Murray RM, Collier DA | title = Evidence for association between novel polymorphisms in the PRODH gene and schizophrenia in a Chinese population | journal = American Journal of Medical Genetics Part B | volume = 129B | issue = 1 | pages = 13–5 | date = Aug 2004 | pmid = 15274030 | doi = 10.1002/ajmg.b.30049 }}
-*{{cite journal  | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121-7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 }}
+* {{cite journal | vauthors = Zhang M, White TA, Schuermann JP, Baban BA, Becker DF, Tanner JJ | title = Structures of the Escherichia coli PutA proline dehydrogenase domain in complex with competitive inhibitors | journal = Biochemistry | volume = 43 | issue = 39 | pages = 12539–48 | date = Oct 2004 | pmid = 15449943 | doi = 10.1021/bi048737e }}
-*{{cite journal  | author=Jacquet H, Demily C, Houy E, ''et al.'' |title=Hyperprolinemia is a risk factor for schizoaffective disorder. |journal=Mol. Psychiatry |volume=10 |issue= 5 |pages= 479-85 |year= 2005 |pmid= 15494707 |doi= 10.1038/sj.mp.4001597 }}
+* {{cite journal | vauthors = Jacquet H, Demily C, Houy E, Hecketsweiler B, Bou J, Raux G, Lerond J, Allio G, Haouzir S, Tillaux A, Bellegou C, Fouldrin G, Delamillieure P, Ménard JF, Dollfus S, D'Amato T, Petit M, Thibaut F, Frébourg T, Campion D | title = Hyperprolinemia is a risk factor for schizoaffective disorder | journal = Molecular Psychiatry | volume = 10 | issue = 5 | pages = 479–85 | date = May 2005 | pmid = 15494707 | doi = 10.1038/sj.mp.4001597 }}
-*{{cite journal  | author=Bender HU, Almashanu S, Steel G, ''et al.'' |title=Functional consequences of PRODH missense mutations. |journal=Am. J. Hum. Genet. |volume=76 |issue= 3 |pages= 409-20 |year= 2005 |pmid= 15662599 |doi= 10.1086/428142 }}
+* {{cite journal | vauthors = Bender HU, Almashanu S, Steel G, Hu CA, Lin WW, Willis A, Pulver A, Valle D | title = Functional consequences of PRODH missense mutations | journal = American Journal of Human Genetics | volume = 76 | issue = 3 | pages = 409–20 | date = Mar 2005 | pmid = 15662599 | pmc = 1196393 | doi = 10.1086/428142 }}
-*{{cite journal  | author=Rivera A, Maxwell SA |title=The p53-induced gene-6 (proline oxidase) mediates apoptosis through a calcineurin-dependent pathway. |journal=J. Biol. Chem. |volume=280 |issue= 32 |pages= 29346-54 |year= 2005 |pmid= 15914462 |doi= 10.1074/jbc.M504852200 }}
+* {{cite journal | vauthors = Rivera A, Maxwell SA | title = The p53-induced gene-6 (proline oxidase) mediates apoptosis through a calcineurin-dependent pathway | journal = The Journal of Biological Chemistry | volume = 280 | issue = 32 | pages = 29346–54 | date = Aug 2005 | pmid = 15914462 | doi = 10.1074/jbc.M504852200 }}
-*{{cite journal  | author=Pandhare J, Cooper SK, Phang JM |title=Proline oxidase, a proapoptotic gene, is induced by troglitazone: evidence for both peroxisome proliferator-activated receptor gamma-dependent and -independent mechanisms. |journal=J. Biol. Chem. |volume=281 |issue= 4 |pages= 2044-52 |year= 2006 |pmid= 16303758 |doi= 10.1074/jbc.M507867200 }}
+* {{cite journal | vauthors = Pandhare J, Cooper SK, Phang JM | title = Proline oxidase, a proapoptotic gene, is induced by troglitazone: evidence for both peroxisome proliferator-activated receptor gamma-dependent and -independent mechanisms | journal = The Journal of Biological Chemistry | volume = 281 | issue = 4 | pages = 2044–52 | date = Jan 2006 | pmid = 16303758 | doi = 10.1074/jbc.M507867200 }}
-*{{cite journal  | author=Liu Y, Borchert GL, Surazynski A, ''et al.'' |title=Proline oxidase activates both intrinsic and extrinsic pathways for apoptosis: the role of ROS/superoxides, NFAT and MEK/ERK signaling. |journal=Oncogene |volume=25 |issue= 41 |pages= 5640-7 |year= 2006 |pmid= 16619034 |doi= 10.1038/sj.onc.1209564 }}
+* {{cite journal | vauthors = Liu Y, Borchert GL, Surazynski A, Hu CA, Phang JM | title = Proline oxidase activates both intrinsic and extrinsic pathways for apoptosis: the role of ROS/superoxides, NFAT and MEK/ERK signaling | journal = Oncogene | volume = 25 | issue = 41 | pages = 5640–7 | date = Sep 2006 | pmid = 16619034 | doi = 10.1038/sj.onc.1209564 }}
-*{{cite journal  | author=Li D, He L |title=Association study of the G-protein signaling 4 (RGS4) and proline dehydrogenase (PRODH) genes with schizophrenia: a meta-analysis. |journal=Eur. J. Hum. Genet. |volume=14 |issue= 10 |pages= 1130-5 |year= 2006 |pmid= 16791139 |doi= 10.1038/sj.ejhg.5201680 }}
+* {{cite journal | vauthors = Li D, He L | title = Association study of the G-protein signaling 4 (RGS4) and proline dehydrogenase (PRODH) genes with schizophrenia: a meta-analysis | journal = European Journal of Human Genetics | volume = 14 | issue = 10 | pages = 1130–5 | date = Oct 2006 | pmid = 16791139 | doi = 10.1038/sj.ejhg.5201680 }}
-}}
 {{refend}}
-==External links==
+== External links ==
 * {{MeshName|Proline+oxidase}}
-{{SIB}}
 {{CH-NH oxidoreductases}}
 {{Amino acid metabolism enzymes}}
-{{WH}}
-{{WS}}
-<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
-{{PBB_Controls
-| update_page = yes
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v t e Oxidoreductases: CH-NH (EC 1.5)
1.5.1: NAD or NADP acceptor	Dihydrofolate reductase Saccharopine dehydrogenase Methylenetetrahydrofolate reductase
1.5.3: oxygen acceptor	Dihydrobenzophenanthridine oxidase Sarcosine oxidase Proline oxidase
1.5.5: quinone acceptor	Electron-transferring-flavoprotein dehydrogenase
1.5.99	Sarcosine dehydrogenase Cytokinin dehydrogenase

Proline oxidase: Difference between revisions

Revision as of 15:02, 8 September 2017

Contents

Function

Clinical significance

References

Further reading

External links

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