title: Expression of Kin17 and 8-OxoG DNA glycosylase in cells of rodent and quail central nervous system.
abstract: Kin17 and 8-Oxoguanine DNA glycosylase (Ogg1) are proteins, respectively, involved in illegitimate recombination and DNA repair in eukaryotic cells. To characterize the expression of these proteins in cell types of rodent and avian brains, we combined immunocytochemistry for either Kin17 or Ogg1 proteins with glial fibrillary acidic protein (GFAP, an astrocyte marker) immunodetection on the same tissue section. Both Kin17 and Ogg1 proteins were localized in cell nuclei and were extensively distributed in neuronal populations of quail and rodent brains. However, GFAP-immunoreactive cells were never labeled by Kin17 protein. This was observed in nerve fiber tracts, in the cerebral cortex, the hippocampal formation, the hypothalamic region, and the periventricular regions of the brain of both species studied. These results were confirmed by combining in situ hybridization of kin17 mRNA and GFAP immunodetection. On the contrary, GFAP-immunoreactive cells were often labeled by the Ogg1 protein in brain structures such as fiber tracts, the cortical surface, the cerebellum, and the ependymal surface of both quail and mouse brains. Our results suggest that the expression of the Kin17 protein (observed in neurons) and that of the Ogg1 protein (observed in neurons and glial cells) is conserved in brain phylogeny.
authors.affiliation: Neurobiologie des états de sommeils et d'éveil, INSERM U480, Université Claude Bernard, Lyon Cedex, France. araneda@univ-lyon.fr
authors.forename: S
authors.initials: S
authors.lastname: Araneda
authors.forename: N
authors.initials: N
authors.lastname: Mermet
authors.forename: T
authors.initials: T
authors.lastname: Verjat
authors.forename: J F
authors.initials: JF
authors.lastname: Angulo
authors.forename: J P
authors.initials: JP
authors.lastname: Radicella
mesh_terms: D000818:Animals; D001253:Astrocytes / Q000166:cytology / Q000378:metabolism; D001369:Axons / Q000201:enzymology / Q000648:ultrastructure; D002490:Central Nervous System / Q000166:cytology / Q000201:enzymology*; D004260:DNA Repair / Q000502:physiology; D004268:DNA-Binding Proteins / Q000378:metabolism*; D043382:DNA-Formamidopyrimidine Glycosylase; D004805:Ependyma / Q000166:cytology / Q000201:enzymology; D005904:Glial Fibrillary Acidic Protein / Q000378:metabolism; D007150:Immunohistochemistry; D051379:Mice; D009699:N-Glycosyl Hydrolases / Q000378:metabolism*; D009457:Neuroglia / Q000166:cytology / Q000201:enzymology*; D009474:Neurons / Q000166:cytology / Q000201:enzymology*; D009687:Nuclear Proteins; D011784:Quail / Q000033:anatomy & histology / Q000378:metabolism*; D051381:Rats; D017207:Rats, Sprague-Dawley; D012377:Rodentia / Q000033:anatomy & histology / Q000378:metabolism*
chemical_list: D004268:DNA-Binding Proteins; D005904:Glial Fibrillary Acidic Protein; C489488:Kin protein, rat; D009687:Nuclear Proteins; C071214:Kin protein, mouse; D009699:N-Glycosyl Hydrolases; D043382:DNA-Formamidopyrimidine Glycosylase