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Article: Inflammation-mediated cytosine damage: a mechanistic link between inflammation and the epigenetic alterations in human cancers.

Valinluck, Victoria / Sowers, Lawrence C

2007 Volume 67, Issue 12, Page(s) 5583–5586

Abstract: Aberrant methylation patterns have long been known to exist in the promoter regions of key regulatory genes in the DNA of tumor cells. However, the mechanisms by which these methylation patterns become altered during the transformation of normal cells to ...

Abstract	Aberrant methylation patterns have long been known to exist in the promoter regions of key regulatory genes in the DNA of tumor cells. However, the mechanisms by which these methylation patterns become altered during the transformation of normal cells to tumor cells have remained elusive. We have recently shown in in vitro studies that inflammation-mediated halogenated cytosine damage products can mimic 5-methylcytosine in directing enzymatic DNA methylation and in enhancing the binding of methyl-binding proteins whereas certain oxidative damage products inhibit both. We have therefore proposed that cytosine damage products could potentially interfere with normal epigenetic control by altering DNA-protein interactions critical for gene regulation and the heritable transmission of methylation patterns. These inflammation-mediated cytosine damage products may provide, in some cases, a mechanistic link between inflammation and cancer.
MeSH term(s)	Animals ; Cell Transformation, Neoplastic/genetics ; Cell Transformation, Neoplastic/pathology ; Cytosine/metabolism ; DNA Damage/genetics ; DNA Methylation ; Epigenesis, Genetic/physiology ; Humans ; Inflammation/genetics ; Inflammation/physiopathology ; Models, Molecular ; Neoplasms/genetics ; Neoplasms/pathology
Chemical Substances	Cytosine (8J337D1HZY)
Language	English
Publishing date	2007-06-15
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	1432-1
ISSN	1538-7445 ; 0008-5472
ISSN (online)	1538-7445
ISSN	0008-5472
DOI	10.1158/0008-5472.CAN-07-0846
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Article: Endogenous cytosine damage products alter the site selectivity of human DNA maintenance methyltransferase DNMT1.

Valinluck, Victoria / Sowers, Lawrence C

Cancer research

2007 Volume 67, Issue 3, Page(s) 946–950

Abstract: Alterations in cytosine methylation patterns are usually observed in human tumors. The consequences of altered cytosine methylation patterns include both inappropriate activation of transforming genes and silencing of tumor suppressor genes. Despite the ... ...

Abstract	Alterations in cytosine methylation patterns are usually observed in human tumors. The consequences of altered cytosine methylation patterns include both inappropriate activation of transforming genes and silencing of tumor suppressor genes. Despite the biological effect of methylation changes, little is known about how such changes are caused. The heritability of cytosine methylation patterns from parent to progeny cells is attributed to the fidelity of the methylation-sensitive human maintenance methyltransferase DNMT1, which methylates with high specificity the unmethylated strand of a hemimethylated CpG sequence following DNA replication. We have been studying DNA damage that might alter the specificity of DNMT1, either inhibiting the methylation of hemimethylated sites or triggering the inappropriate methylation of previously unmethylated sites. Here, we show that known forms of endogenous DNA damage can cause either hypermethylation or hypomethylation. Inflammation-induced 5-halogenated cytosine damage products, including 5-chlorocytosine, mimic 5-methylcytosine and induce inappropriate DNMT1 methylation within a CpG sequence. In contrast, oxidation damage of the methyl group of 5-methylcytosine, with the formation of 5-hydroxymethylcytosine, prevents DNMT1 methylation of the target cytosine. We propose that reduced DNMT1 selectivity resulting from DNA damage could cause heritable changes in cytosine methylation patterns, resulting in human tumor formation. These data may provide a mechanistic link for the associations documented between inflammation and cancer.
MeSH term(s)	5-Methylcytosine/metabolism ; Cytosine/metabolism ; DNA (Cytosine-5-)-Methyltransferase 1 ; DNA (Cytosine-5-)-Methyltransferases/metabolism ; DNA Damage/physiology ; DNA Methylation ; Substrate Specificity
Chemical Substances	5-Methylcytosine (6R795CQT4H) ; Cytosine (8J337D1HZY) ; DNA (Cytosine-5-)-Methyltransferase 1 (EC 2.1.1.37) ; DNA (Cytosine-5-)-Methyltransferases (EC 2.1.1.37) ; DNMT1 protein, human (EC 2.1.1.37)
Language	English
Publishing date	2007-02-01
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	1432-1
ISSN	1538-7445 ; 0008-5472
ISSN (online)	1538-7445
ISSN	0008-5472
DOI	10.1158/0008-5472.CAN-06-3123
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Article ; Online: Epigenetics and colorectal cancer.

Lao, Victoria Valinluck / Grady, William M

Nature reviews. Gastroenterology & hepatology

2011 Volume 8, Issue 12, Page(s) 686–700

Abstract: Colorectal cancer (CRC) is a leading cause of cancer deaths worldwide. It results from an accumulation of genetic and epigenetic changes in colon epithelial cells, which transforms them into adenocarcinomas. Over the past decade, major advances have been ...

Abstract	Colorectal cancer (CRC) is a leading cause of cancer deaths worldwide. It results from an accumulation of genetic and epigenetic changes in colon epithelial cells, which transforms them into adenocarcinomas. Over the past decade, major advances have been made in understanding cancer epigenetics, particularly regarding aberrant DNA methylation. Assessment of the colon cancer epigenome has revealed that virtually all CRCs have aberrantly methylated genes and that the average CRC methylome has hundreds to thousands of abnormally methylated genes. As with gene mutations in the cancer genome, a subset of these methylated genes, called driver genes, is presumed to have a functional role in CRC. The assessment of methylated genes in CRCs has also revealed a unique molecular subgroup of CRCs called CpG island methylator phenotype (CIMP) cancers; these tumors have a particularly high frequency of methylated genes. These advances in our understanding of aberrant methylation in CRC have led to epigenetic alterations being developed as clinical biomarkers for diagnostic, prognostic and therapeutic applications. Progress in this field suggests that these epigenetic alterations will be commonly used in the near future to direct the prevention and treatment of CRC.
MeSH term(s)	Biomarkers, Tumor/biosynthesis ; Biomarkers, Tumor/genetics ; Colorectal Neoplasms/genetics ; Colorectal Neoplasms/metabolism ; Colorectal Neoplasms/mortality ; DNA, Neoplasm/genetics ; Epigenomics/methods ; Global Health ; Humans ; Survival Rate/trends
Chemical Substances	Biomarkers, Tumor ; DNA, Neoplasm
Language	English
Publishing date	2011-10-18
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	2493722-8
ISSN	1759-5053 ; 1759-5045
ISSN (online)	1759-5053
ISSN	1759-5045
DOI	10.1038/nrgastro.2011.173
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Article ; Online: Postoperative Bowel Perforation due to Heterotopic Ossification (Myositis Ossificans Traumatica)

Edgar Figueredo / Oliver B. Lao / Victoria Valinluck Lao

Case Reports in Gastrointestinal Medicine, Vol

A Case Report and Review of the Literature

2011 Volume 2011

Keywords	Diseases of the digestive system. Gastroenterology ; RC799-869 ; Specialties of internal medicine ; RC581-951 ; Internal medicine ; RC31-1245 ; Medicine ; R ; DOAJ:Gastroenterology ; DOAJ:Medicine (General) ; DOAJ:Health Sciences
Language	English
Publishing date	2011-01-01T00:00:00Z
Publisher	Hindawi Publishing Corporation
Document type	Article ; Online
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Article ; Online: Laparoscopic transperitoneal repair of pediatric diaphragm eventration using an endostapler device.

Lao, Victoria Valinluck / Lao, Oliver B / Abdessalam, Shahab F

Journal of laparoendoscopic & advanced surgical techniques. Part A

2013 Volume 23, Issue 9, Page(s) 808–813

Abstract: Background: Minimally invasive repairs of pediatric diaphragm eventration have been well described via a thoracoscopic approach, oftentimes requiring single-lung ventilation and tube thoracostomy, with the disadvantage of not being able to clearly ... ...

Abstract	Background: Minimally invasive repairs of pediatric diaphragm eventration have been well described via a thoracoscopic approach, oftentimes requiring single-lung ventilation and tube thoracostomy, with the disadvantage of not being able to clearly visualize what lies beneath the diaphragm. We describe a novel pediatric diaphragm eventration repair using a laparoscopic transperitoneal approach and an endostapler device. We also describe our initial experience with this technique. Patients and methods: Four pediatric diaphragmatic eventration patients underwent laparoscopic transperitoneal repair using an endostapler device. Repairs were performed in both male and female patients with right-sided eventrations. We approach the repair in a transperitoneal fashion using inverting sutures at the apex of the diaphragm to create tension toward the pelvis. Subsequently, an endostapler is used to remove the redundant portion of diaphragm, leaving a repaired, taut diaphragm. Results: The median age at operation was 10.5 months. The median operative time was 70 minutes. There was no mortality, surgical complications, or recurrence at a median follow-up of 17 months. Conclusions: This laparoscopic approach allows for clear visualization of the intraabdominal organs and, at least in our early experience, a very simple, straightforward operation. Additionally, with the use of the endostapler, the redundant, often weakened diaphragm is removed, leaving the native, healthy diaphragm behind, resulting in a reliable and reproducible repair. This repair should be considered as a feasible alternative approach to the more traditional open and thoracoscopic repairs.
MeSH term(s)	Child ; Diaphragm/surgery ; Diaphragmatic Eventration/surgery ; Female ; Humans ; Infant ; Laparoscopy/methods ; Male ; Minimally Invasive Surgical Procedures ; Operative Time ; Peritoneum/surgery ; Surgical Stapling/instrumentation ; Surgical Stapling/methods
Language	English
Publishing date	2013-08-12
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	1381909-4
ISSN	1557-9034 ; 1092-6429
ISSN (online)	1557-9034
ISSN	1092-6429
DOI	10.1089/lap.2013.0113
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Article ; Online: Postoperative Bowel Perforation due to Heterotopic Ossification (Myositis Ossificans Traumatica): A Case Report and Review of the Literature.

Lao, Victoria Valinluck / Lao, Oliver B / Figueredo, Edgar

Case reports in gastrointestinal medicine

2011 Volume 2011, Page(s) 908514

Abstract: Heterotopic ossification (HO) is the ectopic development of normal bone within soft tissue that can occur after traumatic injury. It is uncommon and may be missed or misdiagnosed, which can lead to complications. We report the case of an 84-year-old male ...

Abstract	Heterotopic ossification (HO) is the ectopic development of normal bone within soft tissue that can occur after traumatic injury. It is uncommon and may be missed or misdiagnosed, which can lead to complications. We report the case of an 84-year-old male with a previous history of a laparotomy who underwent resection of an intra-abdominal tumor through a midline incision. On postoperative day six, the patient was taken to the operating room, as succus was draining from the incision. Upon re-exploration, sharp bone-like material was found in the wound directly adjacent to an enterotomy. Pathology confirmed mature lamellar bone and the diagnosis of HO. This is the first report of postoperative intestinal perforation secondary to HO in a midline wound. We report this case to encourage accurate reporting of HO and its morbidity and complications for the benefit of appropriate surgical planning and epidemiologic tracking of outcomes.
Language	English
Publishing date	2011-07-10
Publishing country	United States
Document type	Case Reports
ZDB-ID	2627636-7
ISSN	2090-6536 ; 2090-6528
ISSN (online)	2090-6536
ISSN	2090-6528
DOI	10.1155/2011/908514
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Article ; Online: Impact of base analogues within a CpG dinucleotide on the binding of DNA by the methyl-binding domain of MeCP2 and methylation by DNMT1.

Lao, Victoria Valinluck / Darwanto, Agus / Sowers, Lawrence C

Biochemistry

2010 Volume 49, Issue 47, Page(s) 10228–10236

Abstract: The epigenetic control of transcription requires the selective recognition of methylated CpG dinucleotides by methylation-sensitive sequence-specific DNA binding proteins. In order to probe the mechanism of selective interaction of the methyl-binding ... ...

Abstract	The epigenetic control of transcription requires the selective recognition of methylated CpG dinucleotides by methylation-sensitive sequence-specific DNA binding proteins. In order to probe the mechanism of selective interaction of the methyl-binding protein with methylated DNA, we have prepared a series of oligonucleotides containing modified purines and pyrimidines at the recognition site, and we have examined the binding of these oligonucleotides to the methyl-binding domain (MBD) of the methyl-CpG-binding protein 2 (MeCP2). Our results suggest that pyrimidine 5-substituents similar in size to a methyl group facilitate protein binding; however, binding affinity does not correlate with the hydrophobicity of the substituent, and neither the 4-amino group of 5-methylcytosine (mC) nor Watson-Crick base pair geometry is essential for MBD binding. However, 5-substituted uracil analogues in one strand do not direct human DNA methyltransferase 1 (DNMT1) methylation of the opposing strand, as does mC. Important recognition elements do include the guanine O6 and N7 atoms present in the major groove. Unexpectedly, removal of the guanine 2-amino group from the minor groove substantially enhances MBD binding, likely resulting from DNA bending at the substitution site. The enhanced binding of the MBD to oligonucleotides containing several cytosine analogues observed here is better explained by a DNA-protein interface mediated by structured water as opposed to hydrophobic interactions.
MeSH term(s)	5-Methylcytosine/metabolism ; CpG Islands ; DNA (Cytosine-5-)-Methyltransferase 1 ; DNA (Cytosine-5-)-Methyltransferases/metabolism ; Epigenomics ; Humans ; Hydrophobic and Hydrophilic Interactions ; Methyl-CpG-Binding Protein 2/metabolism ; Structure-Activity Relationship
Chemical Substances	Methyl-CpG-Binding Protein 2 ; 5-Methylcytosine (6R795CQT4H) ; DNA (Cytosine-5-)-Methyltransferase 1 (EC 2.1.1.37) ; DNA (Cytosine-5-)-Methyltransferases (EC 2.1.1.37) ; DNMT1 protein, human (EC 2.1.1.37)
Language	English
Publishing date	2010-11-09
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	1108-3
ISSN	1520-4995 ; 0006-2960
ISSN (online)	1520-4995
ISSN	0006-2960
DOI	10.1021/bi1011942
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Article: Impact of cytosine 5-halogens on the interaction of DNA with restriction endonucleases and methyltransferase.

Valinluck, Victoria / Wu, Winnie / Liu, Pingfang / Neidigh, Jonathan W / Sowers, Lawrence C

Chemical research in toxicology

2006 Volume 19, Issue 4, Page(s) 556–562

Abstract: Growing evidence from both prokaryotes and eukaryotes indicates that pyrimidine 5-methyl groups can have profound biological consequences that are mediated by the affinity of DNA-protein interactions. The presence of the 5-methyl group could potentially ... ...

Abstract	Growing evidence from both prokaryotes and eukaryotes indicates that pyrimidine 5-methyl groups can have profound biological consequences that are mediated by the affinity of DNA-protein interactions. The presence of the 5-methyl group could potentially create a steric block preventing the binding of some proteins whereas the affinity of many other proteins is substantially increased by pyrimidine methylation. In this paper, we have constructed a series of oligonucleotides containing cytosine and a series of 5-substituted cytosine analogues including all halogens. This set of oligonucleotides has been used to probe the relationship between the size of the substituent and its capacity to modulate cleavage by the methylation-sensitive restriction endonucleases MspI and HpaII. Additionally, we have examined the impact of the halogen substitution on the corresponding bacterial methyltransferase (M.HpaII). We observed that MspI cleavage is only subtly affected by substituted cytosine analogues at the inner position of the CCGG recognition site. In contrast, HpaII cleaves cytosine-containing oligonucleotides completely whereas 5-fluorocytosine-containing oligonucleotides are cleaved at a reduced rate. The presence of the larger halogens Cl, Br, or I as well as a methyl group completely prevents cleavage by HpaII. These data suggest that the steric wall is encountered by HpaII slightly beyond the fluorine substituent, at about 2.65 A from the pyrimidine C5-position. It is known that 5-fluorocytosine in an oligonucleotide can form a covalent irreversible suicide complex with either prokaryotic or eukaryotic methyltransferases. Kinetic data reported here suggest that the 5-fluorocytosine-containing oligonucleotide can also inhibit M.HpaII by formation of a reversible, noncovalent complex. Our results indicate that although a 5-Cl substituent has electronic properties similar to 5-F, 5-chlorocytosine duplexes neither form a complex with M.HpaII nor inhibit enzymatic methylation. Emerging data suggest that halogenation of cytosine can occur in DNA in vivo from inflammation-mediated reactive molecules. The results reported here suggest that the inadvertent halogenation of cytosine residues in DNA could alter the affinity of sequence-specific DNA-binding proteins.
MeSH term(s)	Cytosine/chemistry ; DNA/chemistry ; DNA Restriction Enzymes/chemistry ; Halogens/chemistry ; Methyltransferases/chemistry
Chemical Substances	Halogens ; Cytosine (8J337D1HZY) ; DNA (9007-49-2) ; Methyltransferases (EC 2.1.1.-) ; DNA Restriction Enzymes (EC 3.1.21.-)
Language	English
Publishing date	2006-04
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	639353-6
ISSN	1520-5010 ; 0893-228X
ISSN (online)	1520-5010
ISSN	0893-228X
DOI	10.1021/tx050341w
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Article ; Online: Synthesis of stable-isotope enriched 5-methylpyrimidines and their use as probes of base reactivity in DNA.

Burdzy, Artur / Noyes, Katherine T / Valinluck, Victoria / Sowers, Lawrence C

Nucleic acids research

2002 Volume 30, Issue 18, Page(s) 4068–4074

Abstract: A specific and efficient method is presented for the conversion of 2'-deoxyuridine to thymidine via formation and reduction of the intermediate 5-hydroxymethyl derivative. The method has been used to generate both thymidine and 5-methyl-2'-deoxycytidine ... ...

Abstract	A specific and efficient method is presented for the conversion of 2'-deoxyuridine to thymidine via formation and reduction of the intermediate 5-hydroxymethyl derivative. The method has been used to generate both thymidine and 5-methyl-2'-deoxycytidine containing the stable isotopes 2H, 13C and 15N. Oligodeoxyribonucleotides have been constructed with these mass-tagged bases to investigate sequence-selectivity in hydroxyl radical reactions of pyrimidine methyl groups monitored by mass spectrometry. Studying the reactivity of 5-methylcytosine (5mC) is difficult as the reaction products can deaminate to the corresponding thymine derivatives, making the origin of the reaction products ambiguous. The method reported here can distinguish products derived from 5mC and thymine as well as investigate differences in reactivity for either base in different sequence contexts. The efficiency of formation of 5-hydroxymethyluracil from thymine is observed to be similar in magnitude in two different sequence contexts and when present in a mispair with guanine. The oxidation of 5mC proceeds slightly more efficiently than that of thymine and generates both 5-hydroxymethylcytosine and 5-formylcytosine but not the deaminated products. Thymine glycol is generated by both thymine and 5mC, although with reduced efficiency for 5mC. The method presented here should be widely applicable, enabling the examination of the reactivity of selected bases in DNA.
MeSH term(s)	Base Sequence ; Carbon Isotopes ; DNA/chemistry ; DNA Probes/chemistry ; Deuterium ; Gas Chromatography-Mass Spectrometry ; Hydroxyl Radical/chemistry ; Nitrogen Isotopes ; Oligonucleotides/chemistry ; Pyrimidines/chemical synthesis ; Reactive Oxygen Species/chemistry ; Thymidine/chemistry ; Thymine/chemistry
Chemical Substances	Carbon Isotopes ; DNA Probes ; Nitrogen Isotopes ; Oligonucleotides ; Pyrimidines ; Reactive Oxygen Species ; Hydroxyl Radical (3352-57-6) ; DNA (9007-49-2) ; Deuterium (AR09D82C7G) ; Thymine (QR26YLT7LT) ; Thymidine (VC2W18DGKR)
Language	English
Publishing date	2002-09-13
Publishing country	England
Document type	Journal Article ; Research Support, U.S. Gov't, P.H.S.
ZDB-ID	186809-3
ISSN	1362-4962 ; 1362-4954 ; 0301-5610 ; 0305-1048
ISSN (online)	1362-4962 ; 1362-4954
ISSN	0301-5610 ; 0305-1048
DOI	10.1093/nar/gkf520
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Article ; Online: 5-halogenated pyrimidine lesions within a CpG sequence context mimic 5-methylcytosine by enhancing the binding of the methyl-CpG-binding domain of methyl-CpG-binding protein 2 (MeCP2).

Valinluck, Victoria / Liu, Pingfang / Kang, Joseph I / Burdzy, Artur / Sowers, Lawrence C

Nucleic acids research

2005 Volume 33, Issue 9, Page(s) 3057–3064

Abstract: Perturbations in cytosine methylation signals are observed in the majority of human tumors; however, it is as yet unknown how methylation patterns become altered. Epigenetic changes can result in the activation of transforming genes as well as in the ... ...

Abstract	Perturbations in cytosine methylation signals are observed in the majority of human tumors; however, it is as yet unknown how methylation patterns become altered. Epigenetic changes can result in the activation of transforming genes as well as in the silencing of tumor suppressor genes. We report that methyl-CpG-binding proteins (MBPs), specific for methyl-CpG dinucleotides, bind with high affinity to halogenated pyrimidine lesions, previously shown to result from peroxidase-mediated inflammatory processes. Emerging data suggest that the initial binding of MBPs to methyl-CpG sequences may be a seeding event that recruits chromatin-modifying enzymes and DNA methyltransferase, initiating a cascade of events that result in gene silencing. MBD4, a protein with both methyl-binding and glycosylase activity demonstrated repair activity against a series of 5-substituted pyrimidines, with the greatest efficiency against 5-chlorouracil, but undetectable activity against 5-chlorocytosine. The data presented here suggest that halogenated pyrimidine damage products can potentially accumulate and mimic endogenous methylation signals.
MeSH term(s)	5-Methylcytosine/chemistry ; Animals ; Binding Sites ; Chromosomal Proteins, Non-Histone/chemistry ; Chromosomal Proteins, Non-Histone/metabolism ; CpG Islands ; DNA Damage ; DNA Glycosylases/metabolism ; DNA Methylation ; DNA-Binding Proteins/chemistry ; DNA-Binding Proteins/metabolism ; Electrophoretic Mobility Shift Assay ; Endodeoxyribonucleases/metabolism ; Halogens/chemistry ; Humans ; Methyl-CpG-Binding Protein 2 ; Mice ; Protein Binding ; Protein Structure, Tertiary ; Pyrimidines/chemistry ; Repressor Proteins/chemistry ; Repressor Proteins/metabolism
Chemical Substances	Chromosomal Proteins, Non-Histone ; DNA-Binding Proteins ; Halogens ; MECP2 protein, human ; Mecp2 protein, mouse ; Methyl-CpG-Binding Protein 2 ; Pyrimidines ; Repressor Proteins ; 5-Methylcytosine (6R795CQT4H) ; Endodeoxyribonucleases (EC 3.1.-) ; MBD4 protein, human (EC 3.1.-) ; DNA Glycosylases (EC 3.2.2.-)
Language	English
Publishing date	2005
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, P.H.S.
ZDB-ID	2205588-5
ISSN	1362-4962 ; 1746-8272 ; 0305-1048 ; 0261-3166
ISSN (online)	1362-4962 ; 1746-8272
ISSN	0305-1048 ; 0261-3166
DOI	10.1093/nar/gki612
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