Abstract
Peptidylarginine deiminases (PADs) are Ca2t+-dependant post-translational modification enzymes that catalyze the citrullination of protein arginyl residues. PAD type 2 (PAD2) is thought to be involved in some processes of neurodegeneration and myelination in the central nervous system. In this study, we found PAD2-positive cells in rat cerebra in 19-to 21-day old embryos, i.e. at a developmental stage well before myelination begins. Most of the cells were microglial marker-positive cells found mainly in the prospective medulla, and others were microglial marker-negative cells found mainly in the prospective dentate gyrus of the hippocampus. The former seemed to be in an activated state as judged by morphological criteria. The specificity of the enzyme activity, immunoblotting and reverse transcriptase-polymerase chain reaction analyses revealed that these cells expressed PAD2 and not PAD1, PAD3 or PAD4. Our data is indicative of microglial expression of PAD2 in the prenatal developing cerebrum.
Key words: Protein deimination, Post-translational modification enzyme, Microglial cells, Central nervous system, Gene expression
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Abbreviations used
- BAEE
benzoyl-L-arginine ethyl ester
- BzArg
benzoyl-L-arginine
- GAPDH
glyceraldehyde-3-phosphatedehydrogenase
- GFAP
glial fibrillary acidic protein
- KA
kainic acid
- MAP2
microtubule associated protein 2
- mAb
monoclonal antibody
- MBP
myelin basic protein
- PAD
peptydylarginine deiminase
- PAD2
peptidylarginine deiminase type 2
- RT-PCR
reverse transcriptase-polymerase chain reaction
- SDS
sodium dodecyl sulfate
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