Expression of kynurenine aminotransferase-2 in different mouse brain-derived cells A comprehensive study in cell cultures /
The kynurenine pathway is the principal route of tryptophan metabolism in the brain, generating several neuroactive metabolites, including kynurenic acid (KYNA). KYNA functions as both a neuromodulator and a neuroprotective compound, and its dysregulation has been associated with numerous neurologic...
Elmentve itt :
| Szerzők: | |
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| Dokumentumtípus: | Cikk |
| Megjelent: |
2026
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| Sorozat: | TISSUE & CELL
98 |
| Tárgyszavak: | |
| doi: | 10.1016/j.tice.2025.103230 |
| mtmt: | 36438126 |
| Online Access: | http://publicatio.bibl.u-szeged.hu/38299 |
| Tartalmi kivonat: | The kynurenine pathway is the principal route of tryptophan metabolism in the brain, generating several neuroactive metabolites, including kynurenic acid (KYNA). KYNA functions as both a neuromodulator and a neuroprotective compound, and its dysregulation has been associated with numerous neurological and psychiatric disorders. Kynurenine aminotransferase-2 (KAT-2) is the key enzyme responsible for KYNA synthesis, yet its precise cellular localization in the mouse brain remains insufficiently characterized. In this study, we systematically compared KAT-2 expression in primary astrocytic, microglial, and neuronal cultures derived from mouse brain, complemented by in situ immunolabeling of brain sections. Immunocytochemistry combined with quantitative colocalization analysis revealed that KAT-2 is expressed in all three major brain cell types, with significant overlap with cell type-specific markers. Furthermore, KAT-2 immunoreactivity was largely restricted to the soma, showing a perinuclear distribution in glial cells and partial extension into dendritic compartments in neurons. These findings provide the first parallel characterization of KAT-2 distribution across astrocytes, microglia, and neurons in the mouse brain. Overall, our results indicate that KAT-2 is widely expressed in neural cells, a finding that supports the hypothesis that KAT-2 contributes broadly to kynurenine metabolism. Taken together, our findings provide a foundation for future studies aimed at defining the cell type-specific functional roles of KAT-2. |
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| Terjedelem/Fizikai jellemzők: | 10 |
| ISSN: | 0040-8166 |