0000000000068017

AUTHOR

Kirsten Schlink

showing 3 related works from this author

Activity of O 6 -methylguanine DNA methyltransferase in mononuclear blood cells of formaldehyde-exposed medical students

1999

A recent study reported that exposure of student embalmers in Cincinnati to high concentrations of formaldehyde (2 mg/m3) reduced the activity of the DNA repair protein O6-methylguanine DNA methyltransferase (MGMT). Reduction in a DNA repair enzyme may strongly increase the cancer risk not only with respect to the repair-enzyme causing agent but with respect to all carcinogens causing lesions subject to repair by the enzyme in question. Thus, we examined whether formaldehyde exposure of 57 medical students during their anatomy course at two different Universities in Germany influenced MGMT activity in mononuclear blood cells. Mean formaldehyde exposure of 41 students was 0.2 +/- 0.05 mg/m3 …

AdultMalemedicine.medical_specialtyPathologyStudents MedicalTime FactorsMethyltransferaseAlcohol DrinkingDNA repairHealth Toxicology and MutagenesisFormaldehydeToxicologyPeripheral blood mononuclear cellDNA methyltransferaseFixativesO(6)-Methylguanine-DNA Methyltransferasechemistry.chemical_compoundFormaldehydeInternal medicineHypersensitivitymedicineHumansneoplasmsCarcinogenchemistry.chemical_classificationbusiness.industrySmokingEnvironmental ExposureGeneral MedicineEndocrinologyEnzymechemistryData Interpretation StatisticalToxicityLeukocytes MononuclearFemalebusinessArchives of Toxicology
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Long-time expression of DNA repair enzymes MGMT and APE in human peripheral blood mononuclear cells.

2001

The DNA repair enzymes O6-methylguanine-DNA methyltransferase (MGMT) and apurinic/apyrimidinic endonuclease (APE, also known as Ref-1) play an important role in cellular defense against the mutagenic and carcinogenic effects of DNA-damaging agents. Cells with low enzyme activity are more sensitive to induced DNA damage and may confer a higher carcinogenic risk to the individuals in question. To study the level of variability of MGMT and APE expression in human, we analyzed in a long-time study MGMT and APE expression in peripheral blood mononuclear cells (PBMC) from healthy individuals. The data revealed high inter- and intraindividual variability of MGMT but not of APE. For MGMT, the inter…

AdultMaleMethyltransferaseTime FactorsDNA LigasesDNA repairDNA damageHealth Toxicology and MutagenesisBlotting WesternCarbon-Oxygen LyasesBiologyToxicologyPeripheral blood mononuclear cellMonocytesEndonucleaseO(6)-Methylguanine-DNA MethyltransferaseGene expressionDNA-(Apurinic or Apyrimidinic Site) LyaseHumansneoplasmsCarcinogenSmokingGeneral MedicineDNA-(apurinic or apyrimidinic site) lyaseMolecular biologydigestive system diseasesDeoxyribonuclease IV (Phage T4-Induced)biology.proteinFemaleArchives of toxicology
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DNA repair activity of 8-oxoguanine DNA glycosylase 1 (OGG1) in human lymphocytes is not dependent on genetic polymorphism Ser326/Cys326.

2001

8-oxoguanine DNA glycosylase 1 (OGG1) is a DNA repair enzyme that excises 7,8-dihydro-8-oxoguanine (8oxoG) from DNA. Since 8oxoG is a highly mispairing lesion, decreased OGG1 expression level could lead to a higher background mutation frequency and could possibly increase the cancer risk of an individual under oxidative stress. In order to analyse the natural variation of OGG1, we measured the DNA repair activity in human lymphocytes of healthy individuals by means of an 8oxoG-containing oligonucleotide assay. The data obtained revealed a two fold interindividual variation of OGG1 activity in lymphocytes. There was no difference in OGG1 activity due to gender and smoking behaviour. Transcri…

MaleDNA RepairDNA damageDNA repairBiologyIn Vitro TechniquesToxicologyDNA-formamidopyrimidine glycosylasechemistry.chemical_compoundGene FrequencyMUTYHGeneticsHumansAmino Acid SequenceLymphocytesMolecular BiologyGeneN-Glycosyl HydrolasesAllelesDNA PrimersPolymorphism GeneticBase SequenceOligonucleotideReverse Transcriptase Polymerase Chain ReactionMolecular biologyIsoenzymeschemistryDNA-Formamidopyrimidine GlycosylaseDNA glycosylaseDNADNA DamageMutation research
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