{{cs1 config|name-list-style=vanc|display-authors=6}} {{short description|DNA glycosylase enzyme}} {{Infobox_gene}} {{Infobox protein family | Symbol = OGG_N | Name = 8-oxoguanine DNA glycosylase, N-terminal domain | image = PDB 2noh EBI.jpg | width = | 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.
== 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.<ref name="Nishioka" /> 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 name="entrez" /> 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 N-terminal domain contributes residues to the 8-oxoguanine binding pocket. This domain is organised into a single copy of a TBP-like fold.<ref name="pmid11902834" />
Despite the presumed importance of this enzyme, mice lacking Ogg1 have been generated and found to have a normal lifespan,<ref name="pmid10557315" /> 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" /> 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" /> There is some controversy as to whether deletion of Ogg1 actually leads to increased 8-Oxo-2'-deoxyguanosine (8-oxo-dG) levels: high performance liquid chromatography with electrochemical detection (HPLC-ECD) assay suggests the deletion can lead to an up to 6 fold higher level of 8-oxo-dG in nuclear DNA and a 20-fold higher level in mitochondrial DNA, whereas DNA-fapy glycosylase assay indicates no change in 8-oxo-dG levels.{{Citation needed|date=July 2009}}
Increased oxidant stress temporarily inactivates OGG1, which recruits transcription factors such as NFkB and thereby activates expression of inflammatory genes.<ref>{{cite journal | vauthors = Pan L, Zhu B, Hao W, Zeng X, Vlahopoulos SA, Hazra TK, Hegde ML, Radak Z, Bacsi A, Brasier AR, Ba X, Boldogh I | title = Oxidized Guanine Base Lesions Function in 8-Oxoguanine DNA Glycosylase-1-mediated Epigenetic Regulation of Nuclear Factor κB-driven Gene Expression | journal = The Journal of Biological Chemistry | volume = 291 | issue = 49 | pages = 25553–25566 | date = December 2016 | pmid = 27756845 | pmc = 5207254 | doi = 10.1074/jbc.M116.751453 | doi-access = free }}</ref>
==''OGG1'' deficiency and increased 8-oxo-dG in mice==
thumb|250px|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" /> 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''.<ref name="Sakumi" /> Mice defective in ''OGG1'' also have an increased risk for cancer.<ref name="Sakumi" /> Kunisada et al.<ref name="pmid16024598" /> irradiated mice without a functional ''OGG1'' gene (OGG1 knock-out mice) and wild-type mice three times a week for 40 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. After 24 hours, over half of the initial amount 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 went on to develop more than twice the incidence 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.,<ref name="Valavanidis" /> 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<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 name="pmid24951470" /><ref name="pmid24884764" /> 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 negatively correlated with expression level of OGG1 messenger RNA.<ref name="Fleischer" /> 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.<ref name="Fleischer" />
==In cancers== OGG1 is the primary enzyme responsible for the excision of 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" /> 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 some cancers associated with reduced expression of ''OGG1''.
{| class="wikitable sortable" |+ 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 ||<ref name="pmid26785117" /> |- !Adenocarcinoma of gastric cardia||Under-expression||cytoplasmic||increased||immunohistochemistry ||<ref name="pmid26980051" /> |- !Astrocytoma||Under-expression||total cell OGG1||-||messenger RNA||<ref name="pmid17034947" /> |- !Esophageal cancer||48% Under-expression||nuclear||increased||immunohistochemistry||<ref name="Kubo" /> |- !-||40% Under-expression||cytoplasm||increased||immunohistochemistry||<ref name="Kubo" /> |}
==OGG1 or OGG activity in blood, and cancer==
''OGG1'' methylation levels in blood cells were measured in a prospective study of 582 US military 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" />
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.<ref name="pmid12953085" /> OGG activity was also reduced in PBMCs of patients with head and neck squamous cell carcinoma (HNSCC).<ref name="pmid17178863" />
An important effect on cancer is expected to derive from the drastic enhancement of gene expression for certain immunity genes, which OGG1 regulates.<ref name="pmid38201575">{{cite journal | vauthors = Vlahopoulos S, Pan L, Varisli L, Dancik GM, Karantanos T, Boldogh I | title = OGG1 as an Epigenetic Reader Affects NFκB: What This Means for Cancer | journal = Cancers | volume = 16 | issue = 1 | page = 148 | date = December 2023 | pmid = 38201575 | pmc = 10778025 | doi = 10.3390/cancers16010148 | doi-access = free }}</ref>
== Interactions ==
Oxoguanine glycosylase has been shown to interact with XRCC1<ref name="pmid12933815" /> and PKC alpha.<ref name="pmid12034821" />
== Pathology == *OGG1 may be associated with cancer risk in BRCA1 and BRCA2 mutation carriers.<ref name="pmid24698998" />
== As a treatment target == Several small molecule inhibitors of OGG1 have been reported as starting points for treatments against cancer and inflammatory diseases.<ref>{{cite journal | vauthors = Tahara YK, Auld D, Ji D, Beharry AA, Kietrys AM, Wilson DL, Jimenez M, King D, Nguyen Z, Kool ET | title = Potent and Selective Inhibitors of 8-Oxoguanine DNA Glycosylase | journal = Journal of the American Chemical Society | volume = 140 | issue = 6 | pages = 2105–2114 | date = February 2018 | pmid = 29376367 | pmc = 5823510 | doi = 10.1021/jacs.7b09316 | bibcode = 2018JAChS.140.2105T }}</ref><ref>{{cite journal | vauthors = Visnes T, Cázares-Körner A, Hao W, Wallner O, Masuyer G, Loseva O, Mortusewicz O, Wiita E, Sarno A, Manoilov A, Astorga-Wells J, Jemth AS, Pan L, Sanjiv K, Karsten S, Gokturk C, Grube M, Homan EJ, Hanna BM, Paulin CB, Pham T, Rasti A, Berglund UW, von Nicolai C, Benitez-Buelga C, Koolmeister T, Ivanic D, Iliev P, Scobie M, Krokan HE, Baranczewski P, Artursson P, Altun M, Jensen AJ, Kalderén C, Ba X, Zubarev RA, Stenmark P, Boldogh I, Helleday T | title = Small-molecule inhibitor of OGG1 suppresses proinflammatory gene expression and inflammation | journal = Science | volume = 362 | issue = 6416 | pages = 834–839 | date = November 2018 | pmid = 30442810 | pmc = 6645780 | doi = 10.1126/science.aar8048 | bibcode = 2018Sci...362..834V }}</ref><ref>{{cite journal | vauthors = Luttens A, Vo DD, Scaletti ER, Wiita E, Almlöf I, Wallner O, Davies J, Košenina S, Meng L, Long M, Mortusewicz O, Masuyer G, Ballante F, Michel M, Homan E, Scobie M, Kalderén C, Warpman Berglund U, Tarnovskiy AV, Radchenko DS, Moroz YS, Kihlberg J, Stenmark P, Helleday T, Carlsson J | title = Virtual fragment screening for DNA repair inhibitors in vast chemical space | journal = Nature Communications | volume = 16 | issue = 1 | page = 1741 | date = February 2025 | pmid = 39966348 | pmc = 11836371 | doi = 10.1038/s41467-025-56893-9 | bibcode = 2025NatCo..16.1741L }}</ref>
== See also ==
== References == {{reflist|1=32em|refs= <ref name="entrez">{{EntrezGene|4968}} "OGG1 8-oxoguanine DNA glycosylase"</ref> <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 = International Journal of Cancer | volume = 134 | issue = 11 | pages = 2615–2625 | date = June 2014 | pmid = 24395279 | doi = 10.1002/ijc.28606 | s2cid = 32537522 | doi-access = free }}</ref> <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 = Diseases of the Esophagus | volume = 27 | issue = 3 | pages = 285–293 | date = April 2014 | pmid = 23902537 | doi = 10.1111/dote.12107 | hdl-access = free | hdl = 2324/1441070 }}</ref> <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 = Molecular Biology of the Cell | volume = 10 | issue = 5 | pages = 1637–1652 | date = May 1999 | pmid = 10233168 | pmc = 30487 | doi = 10.1091/mbc.10.5.1637 }}</ref> <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 = Proceedings of the National Academy of Sciences of the United States of America | volume = 96 | issue = 23 | pages = 13300–13305 | date = November 1999 | pmid = 10557315 | pmc = 23942 | doi = 10.1073/pnas.96.23.13300 | doi-access = free | bibcode = 1999PNAS...9613300K }}</ref> <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 = Journal of Molecular Biology | volume = 317 | issue = 2 | pages = 171–177 | date = March 2002 | pmid = 11902834 | doi = 10.1006/jmbi.2002.5400 }}</ref> <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 Research | volume = 30 | issue = 11 | pages = 2349–2357 | date = June 2002 | pmid = 12034821 | pmc = 117190 | doi = 10.1093/nar/30.11.2349 }}</ref> <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 = The Journal of Biological Chemistry | volume = 278 | issue = 45 | pages = 44068–44074 | date = November 2003 | pmid = 12933815 | doi = 10.1074/jbc.M306160200 | doi-access = free | hdl = 10261/343816 | hdl-access = free }}</ref> <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 = Journal of the National Cancer Institute | volume = 95 | issue = 17 | pages = 1312–1319 | date = September 2003 | pmid = 12953085 | doi = 10.1093/jnci/djg033 | citeseerx = 10.1.1.335.8063 | doi-access = free }}</ref> <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 Research | volume = 65 | issue = 14 | pages = 6006–6010 | date = July 2005 | pmid = 16024598 | doi = 10.1158/0008-5472.CAN-05-0724 | doi-access = }}</ref> <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 = Neuroscience Letters | volume = 409 | issue = 2 | pages = 112–117 | date = December 2006 | pmid = 17034947 | doi = 10.1016/j.neulet.2006.09.038 | s2cid = 54278905 }}</ref> <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 Research | volume = 66 | 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M, Oki E, Oda Y | title = Reduced MUTYH, MTH1, and OGG1 expression and TP53 mutation in diffuse-type adenocarcinoma of gastric cardia | journal = Human Pathology | volume = 52 | pages = 145–152 | date = June 2016 | pmid = 26980051 | doi = 10.1016/j.humpath.2016.01.006 }}</ref> <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 = American Journal of Cancer Research | volume = 6 | issue = 2 | pages = 553–561 | year = 2016 | pmid = 27186424 | pmc = 4859680 }}</ref> <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 Journal of Gastrointestinal Oncology | volume = 6 | issue = 7 | pages = 225–243 | date = July 2014 | pmid = 25024814 | pmc = 4092339 | doi = 10.4251/wjgo.v6.i7.225 | doi-access = free }}</ref> <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 Research | volume = 63 | issue = 5 | pages = 902–905 | date = March 2003 | pmid = 12615700 }}</ref> <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 = International Journal of Environmental Research and Public Health | volume = 10 | issue = 9 | pages = 3886–3907 | date = August 2013 | pmid = 23985773 | pmc = 3799517 | doi = 10.3390/ijerph10093886 | doi-access = free }}</ref> }}
== Further reading == {{refbegin|32em}} * {{cite journal | vauthors = Boiteux S, Radicella JP | title = The human OGG1 gene: structure, functions, and its implication in the process of carcinogenesis | journal = Archives of Biochemistry and Biophysics | volume = 377 | issue = 1 | pages = 1–8 | date = May 2000 | pmid = 10775435 | doi = 10.1006/abbi.2000.1773 }} * {{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 = 103–109 | date = February 2004 | pmid = 15077011 | doi = 10.1097/00008571-200402000-00004 }} * {{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 = American Journal of Epidemiology | volume = 162 | issue = 10 | pages = 925–942 | date = November 2005 | pmid = 16221808 | doi = 10.1093/aje/kwi318 | doi-access = free }} * {{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 | volume = 9 | issue = 2 | pages = 144–152 | date = February 2010 | pmid = 20042377 | doi = 10.1016/j.dnarep.2009.11.009 }} * {{cite journal | vauthors = Wang R, Hao W, Pan L, Boldogh I, Ba X | title = The roles of base excision repair enzyme OGG1 in gene expression | journal = Cellular and Molecular Life Sciences | volume = 75 | issue = 20 | pages = 3741–3750 | date = October 2018 | pmid = 30043138 | pmc = 6154017 | doi = 10.1007/s00018-018-2887-8 }} * {{cite journal | vauthors = Vlahopoulos S, Adamaki M, Khoury N, Zoumpourlis V, Boldogh I | title = Roles of DNA repair enzyme OGG1 in innate immunity and its significance for lung cancer | journal = Pharmacology & Therapeutics | volume = 194 | pages = 59–72 | date = February 2019 | pmid = 30240635 | pmc = 6504182 | doi = 10.1016/j.pharmthera.2018.09.004 }} {{refend}}
== External links == * {{MeshName|oxoguanine+glycosylase+1,+human}}
{{PDB Gallery|geneid=4968}} {{Sugar hydrolases}}
{{InterPro content|IPR012904}}
Category:Protein families