Oxoguanine glycosylase: Difference between revisions

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{{Infobox_gene}}
{{PBB_Controls
{{Infobox protein family
| update_page = yes
| Symbol = OGG_N
| require_manual_inspection = no
| Name = 8-oxoguanine DNA glycosylase, N-terminal domain
| update_protein_box = yes
| image = PDB 2noh EBI.jpg
| update_summary = yes
| width =
| update_citations = yes
| caption = structure of catalytically inactive q315a human 8-oxoguanine glycosylase complexed to 8-oxoguanine dna
| Pfam = PF07934
| Pfam_clan = CL0407
| InterPro = IPR012904
| SMART =
| PROSITE =
| MEROPS =
| SCOP = 1ebm
| TCDB =  
| OPM family =  
| OPM protein =  
| CAZy =  
| CDD =  
}}
}}
'''8-Oxoguanine glycosylase''' also known as '''OGG1''' is a [[DNA glycosylase]] enzyme that, in humans, is encoded by the ''OGG1'' [[gene]]. It is involved in [[base excision repair]]. It is found in [[bacterial]], [[archaeal]] and [[eukaryotic]] [[species]].


<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
OGG1 is the primary enzyme responsible for the excision of [[8-oxoguanine]] (8-oxoG), a mutagenic base byproduct that occurs as a result of exposure to [[reactive oxygen species]] (ROS).  OGG1 is a bifunctional glycosylase, as it is able to both cleave the glycosidic bond of the mutagenic lesion and cause a strand break in the DNA backbone.  Alternative splicing of the C-terminal region of this gene classifies splice variants into two major groups, type 1 and type 2, depending on the last exon of the sequence.  Type 1 alternative splice variants end with exon 7 and type 2 end with exon 8.  One set of spliced forms are designated 1a, 1b, 2a to 2e.<ref name=Nishioka>{{cite journal |vauthors=Nishioka K, Ohtsubo T, Oda H, Fujiwara T, Kang D, Sugimachi K, Nakabeppu Y |title=Expression and differential intracellular localization of two major forms of human 8-oxoguanine DNA glycosylase encoded by alternatively spliced OGG1 mRNAs |journal=Mol. Biol. Cell |volume=10 |issue=5 |pages=1637–52 |year=1999 |pmid=10233168 |pmc=30487 |doi= 10.1091/mbc.10.5.1637|url=}}</ref> All variants have the N-terminal region in common. Many alternative splice variants for this gene have been described, but the full-length nature for every variant has not been determined.  In eukaryotes, the N-terminus of this gene contains a mitochondrial targeting signal, essential for mitochondrial localization.<ref>{{cite web | title = Entrez Gene: OGG1 8-oxoguanine DNA glycosylase| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4968| accessdate = }}</ref> However, OGG1-1a also has a nuclear location signal at its C-terminal end that suppresses mitochondrial targeting and causes OGG1-1a to localize to the nucleus.<ref name=Nishioka />  The main form of OGG1 that localizes to the mitochondria is OGG1-2a.<ref name=Nishioka /> A [[Conserved sequence|conserved]] N-terminal [[protein domain|domain]] contributes residues to the 8-oxoguanine [[Binding (molecular)|binding]] pocket. This domain is organised into a single copy of a [[TATA-binding protein|TBP]]-like [[protein folding|fold]].<ref name="pmid11902834">{{cite journal | vauthors = Bjørås M, Seeberg E, Luna L, Pearl LH, Barrett TE | title = Reciprocal "flipping" underlies substrate recognition and catalytic activation by the human 8-oxo-guanine DNA glycosylase | journal = J. Mol. Biol. | volume = 317 | issue = 2 | pages = 171–7  | date = March 2002 | pmid = 11902834 | doi = 10.1006/jmbi.2002.5400 }}</ref>
  | image = PBB_Protein_OGG1_image.jpg
 
  | image_source = [[Protein_Data_Bank|PDB]] rendering based on 1ebm.
Despite the presumed importance of this enzyme, mice lacking Ogg1 have been generated and found to have a normal lifespan,<ref name="pmid10557315">{{cite journal | vauthors = Klungland A, Rosewell I, Hollenbach S, Larsen E, Daly G, Epe B, Seeberg E, Lindahl T, Barnes DE | title = Accumulation of premutagenic DNA lesions in mice defective in removal of oxidative base damage | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 96 | issue = 23 | pages = 13300–5  | date = November 1999 | pmid = 10557315 | pmc = 23942 | doi = 10.1073/pnas.96.23.13300 }}</ref> and Ogg1 knockout mice have a higher probability to develop cancer, whereas Mth1 gene disruption concomitantly suppresses lung cancer development in Ogg1-/- mice.<ref name=Sakumi>{{cite journal |vauthors=Sakumi K, Tominaga Y, Furuichi M, Xu P, Tsuzuki T, Sekiguchi M, Nakabeppu Y |title=Ogg1 knockout-associated lung tumorigenesis and its suppression by Mth1 gene disruption |journal=Cancer Res. |volume=63 |issue=5 |pages=902–5 |year=2003 |pmid=12615700 |doi= |url=}}</ref>  Interestingly, mice lacking Ogg1 have been shown to be prone to increased body weight and obesity, as well as high-fat diet induced insulin resistance.<ref name="pmid23284747">{{cite journal | vauthors = Sampath H, Vartanian V, Rollins MR, Sakumi K, Nakabeppu Y, Lloyd RS | title = 8-Oxoguanine DNA glycosylase (OGG1) deficiency increases susceptibility to obesity and metabolic dysfunction | journal = PLoS ONE | volume = 7 | issue = 12 | pages = e51697  | date = December 2012 | pmid = 23284747 | pmc = 3524114 | doi = 10.1371/journal.pone.0051697 }}</ref> There is some controversy as to whether deletion of Ogg1 actually leads to increased 8-oxo-dG levels: the HPLC-EC assay suggests up to 6 fold higher levels of 8-oxo-dG in nuclear DNA and 20-fold higher in mitochondrial DNA whereas the Fapy-glycosylase assay indicates no change.{{Citation needed|date=July 2009}}
| PDB = {{PDB2|1ebm}}, {{PDB2|1fn7}}, {{PDB2|1hu0}}, {{PDB2|1ko9}}, {{PDB2|1lwv}}, {{PDB2|1lww}}, {{PDB2|1lwy}}, {{PDB2|1m3h}}, {{PDB2|1m3q}}, {{PDB2|1n39}}, {{PDB2|1n3a}}, {{PDB2|1n3c}}, {{PDB2|1yqk}}, {{PDB2|1yql}}, {{PDB2|1yqm}}, {{PDB2|1yqr}}, {{PDB2|2i5w}}, {{PDB2|2nob}}, {{PDB2|2noe}}, {{PDB2|2nof}}, {{PDB2|2noh}}, {{PDB2|2noi}}, {{PDB2|2nol}}, {{PDB2|2noz}}
 
| Name = 8-oxoguanine DNA glycosylase
==''OGG1'' deficiency and increased [[8-Oxo-2'-deoxyguanosine|8-oxo-dG]] in mice==
| HGNCid = 8125
 
| Symbol = OGG1
[[File:Colonic epithelium mouse without tumorigenesis (A) and with tumorigenesis (B). Brown shows 8-oxo-dG.jpg|thumb|500px|Colonic epithelium from a mouse not undergoing colonic tumorigenesis (A), and a mouse that is undergoing colonic tumorigenesis (B). Cell nuclei are stained dark blue with hematoxylin (for nucleic acid) and immunostained brown for 8-oxo-dG. The level of 8-oxo-dG was graded in the nuclei of colonic crypt cells on a scale of 0-4. Mice not undergoing tumorigenesis had crypt 8-oxo-dG at levels 0 to 2 (panel A shows level 1) while mice progressing to colonic tumors had 8-oxo-dG in colonic crypts at levels 3 to 4 (panel B shows level 4)  Tumorigenesis was induced by adding deoxycholate to the mouse diet to give a level of deoxycholate in the mouse colon similar to the level in the colon of humans on a high fat diet.<ref name=Prasad>{{cite journal |vauthors=Prasad AR, Prasad S, Nguyen H, Facista A, Lewis C, Zaitlin B, Bernstein H, Bernstein C |title=Novel diet-related mouse model of colon cancer parallels human colon cancer |journal=World J Gastrointest Oncol |volume=6 |issue=7 |pages=225–43 |year=2014 |pmid=25024814 |pmc=4092339 |doi=10.4251/wjgo.v6.i7.225 |url=}}</ref>  The images were made from original photomicrographs.]]
| AltSymbols =; HMMH; HOGG1; MUTM; OGH1
 
| OMIM = 601982
Mice without a functional ''OGG1'' gene have about a 5-fold increased level of [[8-Oxo-2'-deoxyguanosine|8-oxo-dG]] in their livers compared to mice with wild-type ''OGG1''.<ref name=Sakumi>{{cite journal |vauthors=Sakumi K, Tominaga Y, Furuichi M, Xu P, Tsuzuki T, Sekiguchi M, Nakabeppu Y |title=Ogg1 knockout-associated lung tumorigenesis and its suppression by Mth1 gene disruption |journal=Cancer Res. |volume=63 |issue=5 |pages=902–5 |year=2003 |pmid=12615700 |doi= |url=}}</ref>  Mice defective in ''OGG1'' also have an increased risk for cancer.<ref name=Sakumi />  Kunisada et al.<ref name="pmid16024598">{{cite journal |vauthors=Kunisada M, Sakumi K, Tominaga Y, Budiyanto A, Ueda M, Ichihashi M, Nakabeppu Y, Nishigori C |title=8-Oxoguanine formation induced by chronic UVB exposure makes Ogg1 knockout mice susceptible to skin carcinogenesis |journal=Cancer Res. |volume=65 |issue=14 |pages=6006–10 |year=2005 |pmid=16024598 |doi=10.1158/0008-5472.CAN-05-0724 |url=}}</ref> irradiated mice without a functional ''OGG1'' gene (OGG1 knock-out mice) and wild-type mice three times a week for forty weeks with UVB light at a relatively low dose (not enough to cause skin redness).  Both types of mice had high levels of [[8-Oxo-2'-deoxyguanosine|8-oxo-dG]] in their epidermal cells three hours after irradiation.  However, 24 hours later, the majority of 8-oxo-dG was absent from the epidermal cells of the wild-type mice but 8-oxo-dG remained elevated in the epidermal cells of the ''OGG1'' knock-out mice.  The irradiated OGG1 knock-out mice had more than twice the level of skin tumors compared to irradiated wild-type mice, and the rate of malignancy within the tumors was higher in the OGG1 knock-out mice (73%) than in the wild-type mice (50%).
| ECnumber =
 
| Homologene = 1909
As reviewed by Valavanidis et al.,<ref name=Valavanidis>{{cite journal |vauthors=Valavanidis A, Vlachogianni T, Fiotakis K, Loridas S |title=Pulmonary oxidative stress, inflammation and cancer: respirable particulate matter, fibrous dusts and ozone as major causes of lung carcinogenesis through reactive oxygen species mechanisms |journal=Int J Environ Res Public Health |volume=10 |issue=9 |pages=3886–907 |year=2013 |pmid=23985773 |pmc=3799517 |doi=10.3390/ijerph10093886 |url=}}</ref> increased levels of 8-oxo-dG in a tissue can serve as a biomarker of oxidative stress.  They also noted that increased levels of 8-oxo-dG are frequently found during carcinogenesis.
| MGIid = 1097693
 
  | GeneAtlas_image1 = PBB_GE_OGG1_205301_s_at_tn.png
In the figure showing examples of mouse colonic epithelium, the colonic epithelium from a mouse on a normal diet was found to have a low level of 8-oxo-dG in its colonic crypts (panel A).  However, a mouse likely undergoing colonic tumorigenesis (due to [[Deoxycholic acid|deoxycholate]] added to its diet<ref name=Prasad />) was found to have a high level of 8-oxo-dG in its colonic epithelium (panel B). Deoxycholate increases intracellular production of reactive oxygen resulting in increased oxidative stress,<ref>Tsuei J, Chau T, Mills D, Wan YJ. Bile acid dysregulation, gut dysbiosis, and gastrointestinal cancer. Exp Biol Med (Maywood). 2014 Nov;239(11):1489-504. doi: 10.1177/1535370214538743. {{PMID|24951470}}</ref><ref>Ajouz H, Mukherji D, Shamseddine A. Secondary bile acids: an underrecognized cause of colon cancer. World J Surg Oncol. 2014 May 24;12:164. doi: 10.1186/1477-7819-12-164. Review. {{PMID|24884764}}</ref> and this can lead to tumorigenesis and carcinogenesis.
  | GeneAtlas_image2 = PBB_GE_OGG1_205760_s_at_tn.png
 
| Function = {{GNF_GO|id=GO:0003684 |text = damaged DNA binding}} {{GNF_GO|id=GO:0004519 |text = endonuclease activity}} {{GNF_GO|id=GO:0008534 |text = oxidized purine base lesion DNA N-glycosylase activity}} {{GNF_GO|id=GO:0016798 |text = hydrolase activity, acting on glycosyl bonds}} {{GNF_GO|id=GO:0016829 |text = lyase activity}}
==Epigenetic control==
  | Component = {{GNF_GO|id=GO:0005575 |text = cellular_component}} {{GNF_GO|id=GO:0005622 |text = intracellular}} {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005654 |text = nucleoplasm}} {{GNF_GO|id=GO:0005739 |text = mitochondrion}}  
 
  | Process = {{GNF_GO|id=GO:0006284 |text = base-excision repair}} {{GNF_GO|id=GO:0008152 |text = metabolic process}}  
In a breast cancer study, the methylation level of the ''OGG1'' promoter was found to be anti-correlated with expression level of OGG1 messenger RNA.<ref name=Fleischer>{{cite journal |vauthors=Fleischer T, Edvardsen H, Solvang HK, Daviaud C, Naume B, Børresen-Dale AL, Kristensen VN, Tost J |title=Integrated analysis of high-resolution DNA methylation profiles, gene expression, germline genotypes and clinical end points in breast cancer patients |journal=Int. J. Cancer |volume=134 |issue=11 |pages=2615–25 |year=2014 |pmid=24395279 |doi=10.1002/ijc.28606 |url=}}</ref>  This means that hypermethylation was associated with low expression of ''OGG1'' and hypomethylation was correlated with over-expression of ''OGG1''.  Thus, ''OGG1'' expression is under [[Cancer epigenetics|epigenetic]] control.  Breast cancers with methylation levels of the ''OGG1'' promoter that were more than two standard deviations either above or below the normal were each associated with reduced patient survival.<ref name=Fleischer />
| Orthologs = {{GNF_Ortholog_box
 
    | Hs_EntrezGene = 4968
==In cancers==
    | Hs_Ensembl = ENSG00000114026
 
    | Hs_RefseqProtein = NP_002533
OGG1 is the primary enzyme responsible for the excision of [[8-oxo-2'-deoxyguanosine]] (8-oxo-dG).  Even when OGG1 expression is normal, the presence of 8-oxo-dG is mutagenic since OGG1 is not 100% effective.  Yasui et al.<ref name="pmid24559511">{{cite journal |vauthors=Yasui M, Kanemaru Y, Kamoshita N, Suzuki T, Arakawa T, Honma M |title=Tracing the fates of site-specifically introduced DNA adducts in the human genome |journal=DNA Repair (Amst.) |volume=15 |issue= |pages=11–20 |year=2014 |pmid=24559511 |doi=10.1016/j.dnarep.2014.01.003 |url=}}</ref> examined the fate of 8-oxo-dG when this oxidized derivative of [[deoxyguanosine]] was inserted into a specific gene in 800 cells in culture. After replication of the cells, 8-oxo-dG was restored to G in 86% of the clones, probably reflecting accurate OGG1 [[base excision repair]] or [[DNA repair#Translesion synthesis|translesion synthesis]] without mutation. G:C to T:A [[transversion]]s occurred in 5.9% of the clones, single base [[Deletion (genetics)|deletions]] in 2.1% and G:C to C:G transversions in 1.2%.  Together, these mutations were the most common, totalling 9.2% of the 14% of mutations generated at the site of the 8-oxo-dG insertion.  Among the other mutations in the 800 clones analyzed, there were also 3 larger deletions, of sizes 6, 33 and 135 base pairs.  Thus 8-oxo-dG can directly cause mutations, some of which may contribute to [[carcinogenesis]].
    | Hs_RefseqmRNA = NM_002542
 
    | Hs_GenLoc_db =   
If ''OGG1'' expression is reduced in cells, increased mutagenesis, and therefore increased [[Carcinogenesis#DNA damage and deficient DNA repair in carcinogenesis|carcinogenesis]] would be expected. The table, below, lists cancers with reduced expression of ''OGG1''.
    | Hs_GenLoc_chr = 3
 
    | Hs_GenLoc_start = 9765705
{| class="wikitable sortable"
    | Hs_GenLoc_end = 9783421
|+ Table 1. ''OGG1'' expression in sporadic cancers
    | Hs_Uniprot = O15527
! Cancer !!Expression !!Form of OGG1!!8-oxo-dG!!Evaluation method !!Ref.
    | Mm_EntrezGene = 18294
|-
    | Mm_Ensembl = ENSMUSG00000030271
![[Head and neck cancer]]||Under-expression ||OGG1-2a||-|| messenger RNA ||<ref name="pmid26785117">{{cite journal |vauthors=Mahjabeen I, Kayani MA |title=Loss of Mitochondrial Tumor Suppressor Genes Expression Is Associated with Unfavorable Clinical Outcome in Head and Neck Squamous Cell Carcinoma: Data from Retrospective Study |journal=PLoS ONE |volume=11 |issue=1 |pages=e0146948 |year=2016 |pmid=26785117 |pmc=4718451 |doi=10.1371/journal.pone.0146948 |url=}}</ref>
    | Mm_RefseqmRNA = NM_010957
|-
    | Mm_RefseqProtein = NP_035087
!Adenocarcinoma of [[Stomach#Sections|gastric cardia]]||Under-expression||cytoplasmic||increased||immunohistochemistry ||<ref name="pmid26980051">{{cite journal |vauthors=Kohno Y, Yamamoto H, Hirahashi M, Kumagae Y, Nakamura M, Oki E, Oda Y |title=Reduced MUTYH, MTH1, and OGG1 expression and TP53 mutation in diffuse-type adenocarcinoma of gastric cardia |journal=Hum. Pathol. |volume=52 |issue= |pages=145–52 |year=2016 |pmid=26980051 |doi=10.1016/j.humpath.2016.01.006 |url=}}</ref>
    | Mm_GenLoc_db =   
|-
    | Mm_GenLoc_chr = 6
![[Astrocytoma]]||Under-expression||total cell OGG1||-||messenger RNA||<ref name="pmid17034947">{{cite journal |vauthors=Jiang Z, Hu J, Li X, Jiang Y, Zhou W, Lu D |title=Expression analyses of 27 DNA repair genes in astrocytoma by TaqMan low-density array |journal=Neurosci. Lett. |volume=409 |issue=2 |pages=112–7 |year=2006 |pmid=17034947 |doi=10.1016/j.neulet.2006.09.038 |url=}}</ref>
    | Mm_GenLoc_start = 113292779
|-
    | Mm_GenLoc_end = 113299963
![[Esophageal cancer]]||48% Under-expression||nuclear||increased||immunohistochemistry||<ref name=Kubo>{{cite journal |vauthors=Kubo N, Morita M, Nakashima Y, Kitao H, Egashira A, Saeki H, Oki E, Kakeji Y, Oda Y, Maehara Y |title=Oxidative DNA damage in human esophageal cancer: clinicopathological analysis of 8-hydroxydeoxyguanosine and its repair enzyme |journal=Dis. Esophagus |volume=27 |issue=3 |pages=285–93 |year=2014 |pmid=23902537 |doi=10.1111/dote.12107 |url=}}</ref>
    | Mm_Uniprot = Q3UIL3
|-
  }}
!-||40% Under-expression||cytoplasm||increased||immunohistochemistry||<ref name=Kubo />
}}
|}
'''Oxoguanine glycosylase''' is a [[DNA glycosylase]] enzyme. It is involved in [[base excision repair]].
 
==OGG1 or OGG activity in blood, and cancer==
 
''OGG1'' methylation levels in blood cells were measured in a prospective study of 582 US Veterans, median age 72, and followed for 13 years. High ''OGG1'' methylation at a particular promoter region was associated with increased risk for any cancer, and in particular for risk of prostate cancer.<ref name="pmid27186424">{{cite journal |vauthors=Gao T, Joyce BT, Liu L, Zheng Y, Dai Q, Zhang Z, Zhang W, Shrubsole MJ, Tao MH, Schwartz J, Baccarelli A, Hou L |title=DNA methylation of oxidative stress genes and cancer risk in the Normative Aging Study |journal=Am J Cancer Res |volume=6 |issue=2 |pages=553–61 |year=2016 |pmid=27186424 |pmc=4859680 |doi= |url=}}</ref>
 
Enzymatic activity excising [[8-oxoguanine]] from DNA ('''OGG activity''') was reduced in [[peripheral blood mononuclear cell]]s (PBMCs), and in paired lung tissue, from patients with [[Non-small-cell lung carcinoma|non–small cell lung cancer]].<ref name="pmid12953085">{{cite journal |vauthors=Paz-Elizur T, Krupsky M, Blumenstein S, Elinger D, Schechtman E, Livneh Z |title=DNA repair activity for oxidative damage and risk of lung cancer |journal=J. Natl. Cancer Inst. |volume=95 |issue=17 |pages=1312–9 |year=2003 |pmid=12953085 |doi= 10.1093/jnci/djg033|url=}}</ref> OGG activity was also reduced in PBMCs of patients with [[Head and neck cancer|head and neck squamous cell carcinoma]] (HNSCC).<ref name="pmid17178863">{{cite journal |vauthors=Paz-Elizur T, Ben-Yosef R, Elinger D, Vexler A, Krupsky M, Berrebi A, Shani A, Schechtman E, Freedman L, Livneh Z |title=Reduced repair of the oxidative 8-oxoguanine DNA damage and risk of head and neck cancer |journal=Cancer Res. |volume=66 |issue=24 |pages=11683–9 |year=2006 |pmid=17178863 |doi=10.1158/0008-5472.CAN-06-2294 |url=}}</ref>
 
== Interactions ==
 
Oxoguanine glycosylase has been shown to [[Protein-protein interaction|interact]] with [[XRCC1]]<ref name="pmid12933815">{{cite journal | vauthors = Marsin S, Vidal AE, Sossou M, Ménissier-de Murcia J, Le Page F, Boiteux S, de Murcia G, Radicella JP | title = Role of XRCC1 in the coordination and stimulation of oxidative DNA damage repair initiated by the DNA glycosylase hOGG1 | journal = J. Biol. Chem. | volume = 278 | issue = 45 | pages = 44068–74 | date = November 2003 | pmid = 12933815 | doi = 10.1074/jbc.M306160200 }}</ref> and [[PKC alpha]].<ref name="pmid12034821">{{cite journal | vauthors = Dantzer F, Luna L, Bjørås M, Seeberg E | title = Human OGG1 undergoes serine phosphorylation and associates with the nuclear matrix and mitotic chromatin in vivo | journal = Nucleic Acids Res. | volume = 30 | issue = 11 | pages = 2349–57 | date = June 2002 | pmid = 12034821 | pmc = 117190 | doi = 10.1093/nar/30.11.2349 }}</ref>
 
== Pathology ==
*OGG1 may be associated with cancer risk in [[BRCA1]] and [[BRCA2]] mutation carriers.<ref>{{cite journal | vauthors = Osorio A, Milne RL, Kuchenbaecker K, Vaclová T, Pita G, Alonso R, Peterlongo P, Blanco I, de la Hoya M, Duran M, Díez O, Ramón Y, Cajal T, Konstantopoulou I, Martínez-Bouzas C, Andrés Conejero R, Soucy P, McGuffog L, Barrowdale D, Lee A, Arver B, Rantala J, Loman N, Ehrencrona H, Olopade OI, Beattie MS, Domchek SM, Nathanson K, Rebbeck TR, Arun BK, Karlan BY, Walsh C, Lester J, John EM, Whittemore AS, Daly MB, Southey M, Hopper J, Terry MB, Buys SS, Janavicius R, Dorfling CM, van Rensburg EJ, Steele L, Neuhausen SL, Ding YC, Hansen TV, Jønson L, Ejlertsen B, Gerdes AM, Infante M, Herráez B, Moreno LT, Weitzel JN, Herzog J, Weeman K, Manoukian S, Peissel B, Zaffaroni D, Scuvera G, Bonanni B, Mariette F, Volorio S, Viel A, Varesco L, Papi L, Ottini L, Tibiletti MG, Radice P, Yannoukakos D, Garber J, Ellis S, Frost D, Platte R, Fineberg E, Evans G, Lalloo F, Izatt L, Eeles R, Adlard J, Davidson R, Cole T, Eccles D, Cook J, Hodgson S, Brewer C, Tischkowitz M, Douglas F, Porteous M, Side L, Walker L, Morrison P, Donaldson A, Kennedy J, Foo C, Godwin AK, Schmutzler RK, Wappenschmidt B, Rhiem K, Engel C, Meindl A, Ditsch N, Arnold N, Plendl HJ, Niederacher D, Sutter C, Wang-Gohrke S, Steinemann D, Preisler-Adams S, Kast K, Varon-Mateeva R, Gehrig A, Stoppa-Lyonnet D, Sinilnikova OM, Mazoyer S, Damiola F, Poppe B, Claes K, Piedmonte M, Tucker K, Backes F, Rodríguez G, Brewster W, Wakeley K, Rutherford T, Caldés T, Nevanlinna H, Aittomäki K, Rookus MA, van Os TA, van der Kolk L, de Lange JL, Meijers-Heijboer HE, van der Hout AH, van Asperen CJ, Gómez Garcia EB, Hoogerbrugge N, Collée JM, van Deurzen CH, van der Luijt RB, Devilee P, Olah E, Lázaro C, Teulé A, Menéndez M, Jakubowska A, Cybulski C, Gronwald J, Lubinski J, Durda K, Jaworska-Bieniek K, Johannsson OT, Maugard C, Montagna M, Tognazzo S, Teixeira MR, Healey S, Investigators K, Olswold C, Guidugli L, Lindor N, Slager S, Szabo CI, Vijai J, Robson M, Kauff N, Zhang L, Rau-Murthy R, Fink-Retter A, Singer CF, Rappaport C, Geschwantler Kaulich D, Pfeiler G, Tea MK, Berger A, Phelan CM, Greene MH, Mai PL, Lejbkowicz F, Andrulis I, Mulligan AM, Glendon G, Toland AE, Bojesen A, Pedersen IS, Sunde L, Thomassen M, Kruse TA, Jensen UB, Friedman E, Laitman Y, Shimon SP, Simard J, Easton DF, Offit K, Couch FJ, Chenevix-Trench G, Antoniou AC, Benitez J | title = DNA glycosylases involved in base excision repair may be associated with cancer risk in BRCA1 and BRCA2 mutation carriers | journal = PLoS Genet. | volume = 10 | issue = 4 | pages = e1004256 | year = 2014 | pmid = 24698998 | pmc = 3974638 | doi = 10.1371/journal.pgen.1004256 }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== References ==
{{PBB_Summary
{{reflist}}
| section_title =  
| summary_text = This gene encodes the enzyme responsible for the excision of 8-oxoguanine, a mutagenic base byproduct which occurs as a result of exposure to reactive oxygen.  The action of this enzyme includes lyase activity for chain cleavage.  Alternative splicing of the C-terminal region of this gene classifies splice variants into two major groups, type 1 and type 2, depending on the last exon of the sequence.  Type 1 alternative splice variants end with exon 7 and type 2 end with exon 8.  All variants share the N-terminal region in common.  Many alternative splice variants for this gene have been described, but the full-length nature for every variant has not been determined.  The N-terminus of this gene contains a mitochondrial targetting signal, essential for mitochondrial localization.<ref>{{cite web | title = Entrez Gene: OGG1 8-oxoguanine DNA glycosylase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4968| accessdate = }}</ref>
}}


==References==
== Further reading ==
{{reflist|2}}
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{cite journal | vauthors = Boiteux S, Radicella JP | title = The human OGG1 gene: structure, functions, and its implication in the process of carcinogenesis | journal = Arch. Biochem. Biophys. | volume = 377 | issue = 1 | pages = 1–8 | year = 2000 | pmid = 10775435 | doi = 10.1006/abbi.2000.1773 }}
| citations =
* {{cite journal | vauthors = Park J, Chen L, Tockman MS, Elahi A, Lazarus P | title = The human 8-oxoguanine DNA N-glycosylase 1 (hOGG1) DNA repair enzyme and its association with lung cancer risk | journal = Pharmacogenetics | volume = 14 | issue = 2 | pages = 103–9 | year = 2004 | pmid = 15077011 | doi = 10.1097/00008571-200402000-00004 }}
*{{cite journal | author=Boiteux S, Radicella JP |title=The human OGG1 gene: structure, functions, and its implication in the process of carcinogenesis. |journal=Arch. Biochem. Biophys. |volume=377 |issue= 1 |pages= 1-8 |year= 2000 |pmid= 10775435 |doi= 10.1006/abbi.2000.1773 }}
* {{cite journal | vauthors = Hung RJ, Hall J, Brennan P, Boffetta P | title = Genetic polymorphisms in the base excision repair pathway and cancer risk: a HuGE review | journal = Am. J. Epidemiol. | volume = 162 | issue = 10 | pages = 925–42 | year = 2005 | pmid = 16221808 | doi = 10.1093/aje/kwi318 }}
*{{cite journal | author=Park J, Chen L, Tockman MS, ''et al.'' |title=The human 8-oxoguanine DNA N-glycosylase 1 (hOGG1) DNA repair enzyme and its association with lung cancer risk. |journal=Pharmacogenetics |volume=14 |issue= 2 |pages= 103-9 |year= 2004 |pmid= 15077011 |doi= }}
* {{cite journal | vauthors = Mirbahai L, Kershaw RM, Green RM, Hayden RE, Meldrum RA, Hodges NJ | title = Use of a molecular beacon to track the activity of base excision repair protein OGG1 in live cells | journal = DNA Repair (Amst.) | volume = 9 | issue = 2 | pages = 144–52 | year = 2010 | pmid = 20042377 | doi = 10.1016/j.dnarep.2009.11.009 }}
*{{cite journal | author=Hung RJ, Hall J, Brennan P, Boffetta P |title=Genetic polymorphisms in the base excision repair pathway and cancer risk: a HuGE review. |journal=Am. J. Epidemiol. |volume=162 |issue= 10 |pages= 925-42 |year= 2006 |pmid= 16221808 |doi= 10.1093/aje/kwi318 }}
}}
{{refend}}
{{refend}}


==External links==
== External links ==
* {{MeshName|oxoguanine+glycosylase+1,+human}}
* {{MeshName|oxoguanine+glycosylase+1,+human}}


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[[Category:Protein families]]

Revision as of 01:13, 1 November 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
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UniProt

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RefSeq (mRNA)

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View/Edit Human
8-oxoguanine DNA glycosylase, N-terminal domain
File:PDB 2noh EBI.jpg
structure of catalytically inactive q315a human 8-oxoguanine glycosylase complexed to 8-oxoguanine dna
Identifiers
SymbolOGG_N
PfamPF07934
Pfam clanCL0407
InterProIPR012904
SCOP1ebm
SUPERFAMILY1ebm

8-Oxoguanine glycosylase also known as OGG1 is a DNA glycosylase enzyme that, in humans, is encoded by the OGG1 gene. It is involved in base excision repair. It is found in bacterial, archaeal and eukaryotic species.

Function

OGG1 is the primary enzyme responsible for the excision of 8-oxoguanine (8-oxoG), a mutagenic base byproduct that occurs as a result of exposure to reactive oxygen species (ROS). OGG1 is a bifunctional glycosylase, as it is able to both cleave the glycosidic bond of the mutagenic lesion and cause a strand break in the DNA backbone. Alternative splicing of the C-terminal region of this gene classifies splice variants into two major groups, type 1 and type 2, depending on the last exon of the sequence. Type 1 alternative splice variants end with exon 7 and type 2 end with exon 8. One set of spliced forms are designated 1a, 1b, 2a to 2e.[1] All variants have the N-terminal region in common. Many alternative splice variants for this gene have been described, but the full-length nature for every variant has not been determined. In eukaryotes, the N-terminus of this gene contains a mitochondrial targeting signal, essential for mitochondrial localization.[2] However, OGG1-1a also has a nuclear location signal at its C-terminal end that suppresses mitochondrial targeting and causes OGG1-1a to localize to the nucleus.[1] The main form of OGG1 that localizes to the mitochondria is OGG1-2a.[1] A conserved N-terminal domain contributes residues to the 8-oxoguanine binding pocket. This domain is organised into a single copy of a TBP-like fold.[3]

Despite the presumed importance of this enzyme, mice lacking Ogg1 have been generated and found to have a normal lifespan,[4] and Ogg1 knockout mice have a higher probability to develop cancer, whereas Mth1 gene disruption concomitantly suppresses lung cancer development in Ogg1-/- mice.[5] Interestingly, mice lacking Ogg1 have been shown to be prone to increased body weight and obesity, as well as high-fat diet induced insulin resistance.[6] There is some controversy as to whether deletion of Ogg1 actually leads to increased 8-oxo-dG levels: the HPLC-EC assay suggests up to 6 fold higher levels of 8-oxo-dG in nuclear DNA and 20-fold higher in mitochondrial DNA whereas the Fapy-glycosylase assay indicates no change.[citation needed]

OGG1 deficiency and increased 8-oxo-dG in mice

File:Colonic epithelium mouse without tumorigenesis (A) and with tumorigenesis (B). Brown shows 8-oxo-dG.jpg
Colonic epithelium from a mouse not undergoing colonic tumorigenesis (A), and a mouse that is undergoing colonic tumorigenesis (B). Cell nuclei are stained dark blue with hematoxylin (for nucleic acid) and immunostained brown for 8-oxo-dG. The level of 8-oxo-dG was graded in the nuclei of colonic crypt cells on a scale of 0-4. Mice not undergoing tumorigenesis had crypt 8-oxo-dG at levels 0 to 2 (panel A shows level 1) while mice progressing to colonic tumors had 8-oxo-dG in colonic crypts at levels 3 to 4 (panel B shows level 4) Tumorigenesis was induced by adding deoxycholate to the mouse diet to give a level of deoxycholate in the mouse colon similar to the level in the colon of humans on a high fat diet.[7] The images were made from original photomicrographs.

Mice without a functional OGG1 gene have about a 5-fold increased level of 8-oxo-dG in their livers compared to mice with wild-type OGG1.[5] Mice defective in OGG1 also have an increased risk for cancer.[5] Kunisada et al.[8] irradiated mice without a functional OGG1 gene (OGG1 knock-out mice) and wild-type mice three times a week for forty weeks with UVB light at a relatively low dose (not enough to cause skin redness). Both types of mice had high levels of 8-oxo-dG in their epidermal cells three hours after irradiation. However, 24 hours later, the majority of 8-oxo-dG was absent from the epidermal cells of the wild-type mice but 8-oxo-dG remained elevated in the epidermal cells of the OGG1 knock-out mice. The irradiated OGG1 knock-out mice had more than twice the level of skin tumors compared to irradiated wild-type mice, and the rate of malignancy within the tumors was higher in the OGG1 knock-out mice (73%) than in the wild-type mice (50%).

As reviewed by Valavanidis et al.,[9] increased levels of 8-oxo-dG in a tissue can serve as a biomarker of oxidative stress. They also noted that increased levels of 8-oxo-dG are frequently found during carcinogenesis.

In the figure showing examples of mouse colonic epithelium, the colonic epithelium from a mouse on a normal diet was found to have a low level of 8-oxo-dG in its colonic crypts (panel A). However, a mouse likely undergoing colonic tumorigenesis (due to deoxycholate added to its diet[7]) was found to have a high level of 8-oxo-dG in its colonic epithelium (panel B). Deoxycholate increases intracellular production of reactive oxygen resulting in increased oxidative stress,[10][11] and this can lead to tumorigenesis and carcinogenesis.

Epigenetic control

In a breast cancer study, the methylation level of the OGG1 promoter was found to be anti-correlated with expression level of OGG1 messenger RNA.[12] This means that hypermethylation was associated with low expression of OGG1 and hypomethylation was correlated with over-expression of OGG1. Thus, OGG1 expression is under epigenetic control. Breast cancers with methylation levels of the OGG1 promoter that were more than two standard deviations either above or below the normal were each associated with reduced patient survival.[12]

In cancers

OGG1 is the primary enzyme responsible for the excision of 8-oxo-2'-deoxyguanosine (8-oxo-dG). Even when OGG1 expression is normal, the presence of 8-oxo-dG is mutagenic since OGG1 is not 100% effective. Yasui et al.[13] examined the fate of 8-oxo-dG when this oxidized derivative of deoxyguanosine was inserted into a specific gene in 800 cells in culture. After replication of the cells, 8-oxo-dG was restored to G in 86% of the clones, probably reflecting accurate OGG1 base excision repair or translesion synthesis without mutation. G:C to T:A transversions occurred in 5.9% of the clones, single base deletions in 2.1% and G:C to C:G transversions in 1.2%. Together, these mutations were the most common, totalling 9.2% of the 14% of mutations generated at the site of the 8-oxo-dG insertion. Among the other mutations in the 800 clones analyzed, there were also 3 larger deletions, of sizes 6, 33 and 135 base pairs. Thus 8-oxo-dG can directly cause mutations, some of which may contribute to carcinogenesis.

If OGG1 expression is reduced in cells, increased mutagenesis, and therefore increased carcinogenesis would be expected. The table, below, lists cancers with reduced expression of OGG1.

Table 1. OGG1 expression in sporadic cancers
Cancer Expression Form of OGG1 8-oxo-dG Evaluation method Ref.
Head and neck cancer Under-expression OGG1-2a - messenger RNA [14]
Adenocarcinoma of gastric cardia Under-expression cytoplasmic increased immunohistochemistry [15]
Astrocytoma Under-expression total cell OGG1 - messenger RNA [16]
Esophageal cancer 48% Under-expression nuclear increased immunohistochemistry [17]
- 40% Under-expression cytoplasm increased immunohistochemistry [17]

OGG1 or OGG activity in blood, and cancer

OGG1 methylation levels in blood cells were measured in a prospective study of 582 US Veterans, median age 72, and followed for 13 years. High OGG1 methylation at a particular promoter region was associated with increased risk for any cancer, and in particular for risk of prostate cancer.[18]

Enzymatic activity excising 8-oxoguanine from DNA (OGG activity) was reduced in peripheral blood mononuclear cells (PBMCs), and in paired lung tissue, from patients with non–small cell lung cancer.[19] OGG activity was also reduced in PBMCs of patients with head and neck squamous cell carcinoma (HNSCC).[20]

Interactions

Oxoguanine glycosylase has been shown to interact with XRCC1[21] and PKC alpha.[22]

Pathology

  • OGG1 may be associated with cancer risk in BRCA1 and BRCA2 mutation carriers.[23]

References

  1. ↑ 1.0 1.1 1.2 Nishioka K, Ohtsubo T, Oda H, Fujiwara T, Kang D, Sugimachi K, Nakabeppu Y (1999). "Expression and differential intracellular localization of two major forms of human 8-oxoguanine DNA glycosylase encoded by alternatively spliced OGG1 mRNAs". Mol. Biol. Cell. 10 (5): 1637–52. doi:10.1091/mbc.10.5.1637. PMC 30487. PMID 10233168.
  2. ↑ "Entrez Gene: OGG1 8-oxoguanine DNA glycosylase".
  3. ↑ Bjørås M, Seeberg E, Luna L, Pearl LH, Barrett TE (March 2002). "Reciprocal "flipping" underlies substrate recognition and catalytic activation by the human 8-oxo-guanine DNA glycosylase". J. Mol. Biol. 317 (2): 171–7. doi:10.1006/jmbi.2002.5400. PMID 11902834.
  4. ↑ Klungland A, Rosewell I, Hollenbach S, Larsen E, Daly G, Epe B, Seeberg E, Lindahl T, Barnes DE (November 1999). "Accumulation of premutagenic DNA lesions in mice defective in removal of oxidative base damage". Proc. Natl. Acad. Sci. U.S.A. 96 (23): 13300–5. doi:10.1073/pnas.96.23.13300. PMC 23942. PMID 10557315.
  5. ↑ 5.0 5.1 5.2 Sakumi K, Tominaga Y, Furuichi M, Xu P, Tsuzuki T, Sekiguchi M, Nakabeppu Y (2003). "Ogg1 knockout-associated lung tumorigenesis and its suppression by Mth1 gene disruption". Cancer Res. 63 (5): 902–5. PMID 12615700.
  6. ↑ Sampath H, Vartanian V, Rollins MR, Sakumi K, Nakabeppu Y, Lloyd RS (December 2012). "8-Oxoguanine DNA glycosylase (OGG1) deficiency increases susceptibility to obesity and metabolic dysfunction". PLoS ONE. 7 (12): e51697. doi:10.1371/journal.pone.0051697. PMC 3524114. PMID 23284747.
  7. ↑ 7.0 7.1 Prasad AR, Prasad S, Nguyen H, Facista A, Lewis C, Zaitlin B, Bernstein H, Bernstein C (2014). "Novel diet-related mouse model of colon cancer parallels human colon cancer". World J Gastrointest Oncol. 6 (7): 225–43. doi:10.4251/wjgo.v6.i7.225. PMC 4092339. PMID 25024814.
  8. ↑ Kunisada M, Sakumi K, Tominaga Y, Budiyanto A, Ueda M, Ichihashi M, Nakabeppu Y, Nishigori C (2005). "8-Oxoguanine formation induced by chronic UVB exposure makes Ogg1 knockout mice susceptible to skin carcinogenesis". Cancer Res. 65 (14): 6006–10. doi:10.1158/0008-5472.CAN-05-0724. PMID 16024598.
  9. ↑ Valavanidis A, Vlachogianni T, Fiotakis K, Loridas S (2013). "Pulmonary oxidative stress, inflammation and cancer: respirable particulate matter, fibrous dusts and ozone as major causes of lung carcinogenesis through reactive oxygen species mechanisms". Int J Environ Res Public Health. 10 (9): 3886–907. doi:10.3390/ijerph10093886. PMC 3799517. PMID 23985773.
  10. ↑ Tsuei J, Chau T, Mills D, Wan YJ. Bile acid dysregulation, gut dysbiosis, and gastrointestinal cancer. Exp Biol Med (Maywood). 2014 Nov;239(11):1489-504. doi: 10.1177/1535370214538743. PMID 24951470
  11. ↑ Ajouz H, Mukherji D, Shamseddine A. Secondary bile acids: an underrecognized cause of colon cancer. World J Surg Oncol. 2014 May 24;12:164. doi: 10.1186/1477-7819-12-164. Review. PMID 24884764
  12. ↑ 12.0 12.1 Fleischer T, Edvardsen H, Solvang HK, Daviaud C, Naume B, Børresen-Dale AL, Kristensen VN, Tost J (2014). "Integrated analysis of high-resolution DNA methylation profiles, gene expression, germline genotypes and clinical end points in breast cancer patients". Int. J. Cancer. 134 (11): 2615–25. doi:10.1002/ijc.28606. PMID 24395279.
  13. ↑ Yasui M, Kanemaru Y, Kamoshita N, Suzuki T, Arakawa T, Honma M (2014). "Tracing the fates of site-specifically introduced DNA adducts in the human genome". DNA Repair (Amst.). 15: 11–20. doi:10.1016/j.dnarep.2014.01.003. PMID 24559511.
  14. ↑ Mahjabeen I, Kayani MA (2016). "Loss of Mitochondrial Tumor Suppressor Genes Expression Is Associated with Unfavorable Clinical Outcome in Head and Neck Squamous Cell Carcinoma: Data from Retrospective Study". PLoS ONE. 11 (1): e0146948. doi:10.1371/journal.pone.0146948. PMC 4718451. PMID 26785117.
  15. ↑ Kohno Y, Yamamoto H, Hirahashi M, Kumagae Y, Nakamura M, Oki E, Oda Y (2016). "Reduced MUTYH, MTH1, and OGG1 expression and TP53 mutation in diffuse-type adenocarcinoma of gastric cardia". Hum. Pathol. 52: 145–52. doi:10.1016/j.humpath.2016.01.006. PMID 26980051.
  16. ↑ Jiang Z, Hu J, Li X, Jiang Y, Zhou W, Lu D (2006). "Expression analyses of 27 DNA repair genes in astrocytoma by TaqMan low-density array". Neurosci. Lett. 409 (2): 112–7. doi:10.1016/j.neulet.2006.09.038. PMID 17034947.
  17. ↑ 17.0 17.1 Kubo N, Morita M, Nakashima Y, Kitao H, Egashira A, Saeki H, Oki E, Kakeji Y, Oda Y, Maehara Y (2014). "Oxidative DNA damage in human esophageal cancer: clinicopathological analysis of 8-hydroxydeoxyguanosine and its repair enzyme". Dis. Esophagus. 27 (3): 285–93. doi:10.1111/dote.12107. PMID 23902537.
  18. ↑ Gao T, Joyce BT, Liu L, Zheng Y, Dai Q, Zhang Z, Zhang W, Shrubsole MJ, Tao MH, Schwartz J, Baccarelli A, Hou L (2016). "DNA methylation of oxidative stress genes and cancer risk in the Normative Aging Study". Am J Cancer Res. 6 (2): 553–61. PMC 4859680. PMID 27186424.
  19. ↑ Paz-Elizur T, Krupsky M, Blumenstein S, Elinger D, Schechtman E, Livneh Z (2003). "DNA repair activity for oxidative damage and risk of lung cancer". J. Natl. Cancer Inst. 95 (17): 1312–9. doi:10.1093/jnci/djg033. PMID 12953085.
  20. ↑ Paz-Elizur T, Ben-Yosef R, Elinger D, Vexler A, Krupsky M, Berrebi A, Shani A, Schechtman E, Freedman L, Livneh Z (2006). "Reduced repair of the oxidative 8-oxoguanine DNA damage and risk of head and neck cancer". Cancer Res. 66 (24): 11683–9. doi:10.1158/0008-5472.CAN-06-2294. PMID 17178863.
  21. ↑ Marsin S, Vidal AE, Sossou M, Ménissier-de Murcia J, Le Page F, Boiteux S, de Murcia G, Radicella JP (November 2003). "Role of XRCC1 in the coordination and stimulation of oxidative DNA damage repair initiated by the DNA glycosylase hOGG1". J. Biol. Chem. 278 (45): 44068–74. doi:10.1074/jbc.M306160200. PMID 12933815.
  22. ↑ Dantzer F, Luna L, Bjørås M, Seeberg E (June 2002). "Human OGG1 undergoes serine phosphorylation and associates with the nuclear matrix and mitotic chromatin in vivo". Nucleic Acids Res. 30 (11): 2349–57. doi:10.1093/nar/30.11.2349. PMC 117190. PMID 12034821.
  23. ↑ Osorio A, Milne RL, Kuchenbaecker K, Vaclová T, Pita G, Alonso R, Peterlongo P, Blanco I, de la Hoya M, Duran M, Díez O, Ramón Y, Cajal T, Konstantopoulou I, Martínez-Bouzas C, Andrés Conejero R, Soucy P, McGuffog L, Barrowdale D, Lee A, Arver B, Rantala J, Loman N, Ehrencrona H, Olopade OI, Beattie MS, Domchek SM, Nathanson K, Rebbeck TR, Arun BK, Karlan BY, Walsh C, Lester J, John EM, Whittemore AS, Daly MB, Southey M, Hopper J, Terry MB, Buys SS, Janavicius R, Dorfling CM, van Rensburg EJ, Steele L, Neuhausen SL, Ding YC, Hansen TV, Jønson L, Ejlertsen B, Gerdes AM, Infante M, Herráez B, Moreno LT, Weitzel JN, Herzog J, Weeman K, Manoukian S, Peissel B, Zaffaroni D, Scuvera G, Bonanni B, Mariette F, Volorio S, Viel A, Varesco L, Papi L, Ottini L, Tibiletti MG, Radice P, Yannoukakos D, Garber J, Ellis S, Frost D, Platte R, Fineberg E, Evans G, Lalloo F, Izatt L, Eeles R, Adlard J, Davidson R, Cole T, Eccles D, Cook J, Hodgson S, Brewer C, Tischkowitz M, Douglas F, Porteous M, Side L, Walker L, Morrison P, Donaldson A, Kennedy J, Foo C, Godwin AK, Schmutzler RK, Wappenschmidt B, Rhiem K, Engel C, Meindl A, Ditsch N, Arnold N, Plendl HJ, Niederacher D, Sutter C, Wang-Gohrke S, Steinemann D, Preisler-Adams S, Kast K, Varon-Mateeva R, Gehrig A, Stoppa-Lyonnet D, Sinilnikova OM, Mazoyer S, Damiola F, Poppe B, Claes K, Piedmonte M, Tucker K, Backes F, Rodríguez G, Brewster W, Wakeley K, Rutherford T, Caldés T, Nevanlinna H, Aittomäki K, Rookus MA, van Os TA, van der Kolk L, de Lange JL, Meijers-Heijboer HE, van der Hout AH, van Asperen CJ, Gómez Garcia EB, Hoogerbrugge N, Collée JM, van Deurzen CH, van der Luijt RB, Devilee P, Olah E, Lázaro C, Teulé A, Menéndez M, Jakubowska A, Cybulski C, Gronwald J, Lubinski J, Durda K, Jaworska-Bieniek K, Johannsson OT, Maugard C, Montagna M, Tognazzo S, Teixeira MR, Healey S, Investigators K, Olswold C, Guidugli L, Lindor N, Slager S, Szabo CI, Vijai J, Robson M, Kauff N, Zhang L, Rau-Murthy R, Fink-Retter A, Singer CF, Rappaport C, Geschwantler Kaulich D, Pfeiler G, Tea MK, Berger A, Phelan CM, Greene MH, Mai PL, Lejbkowicz F, Andrulis I, Mulligan AM, Glendon G, Toland AE, Bojesen A, Pedersen IS, Sunde L, Thomassen M, Kruse TA, Jensen UB, Friedman E, Laitman Y, Shimon SP, Simard J, Easton DF, Offit K, Couch FJ, Chenevix-Trench G, Antoniou AC, Benitez J (2014). "DNA glycosylases involved in base excision repair may be associated with cancer risk in BRCA1 and BRCA2 mutation carriers". PLoS Genet. 10 (4): e1004256. doi:10.1371/journal.pgen.1004256. PMC 3974638. PMID 24698998.

Further reading

  • Boiteux S, Radicella JP (2000). "The human OGG1 gene: structure, functions, and its implication in the process of carcinogenesis". Arch. Biochem. Biophys. 377 (1): 1–8. doi:10.1006/abbi.2000.1773. PMID 10775435.
  • Park J, Chen L, Tockman MS, Elahi A, Lazarus P (2004). "The human 8-oxoguanine DNA N-glycosylase 1 (hOGG1) DNA repair enzyme and its association with lung cancer risk". Pharmacogenetics. 14 (2): 103–9. doi:10.1097/00008571-200402000-00004. PMID 15077011.
  • Hung RJ, Hall J, Brennan P, Boffetta P (2005). "Genetic polymorphisms in the base excision repair pathway and cancer risk: a HuGE review". Am. J. Epidemiol. 162 (10): 925–42. doi:10.1093/aje/kwi318. PMID 16221808.
  • Mirbahai L, Kershaw RM, Green RM, Hayden RE, Meldrum RA, Hodges NJ (2010). "Use of a molecular beacon to track the activity of base excision repair protein OGG1 in live cells". DNA Repair (Amst.). 9 (2): 144–52. doi:10.1016/j.dnarep.2009.11.009. PMID 20042377.

External links

This article incorporates text from the public domain Pfam and InterPro: IPR012904
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