Unknown

Dataset Information

0

Reduced Sulfation Enhanced Oxytosis and Ferroptosis in Mouse Hippocampal HT22 Cells.


ABSTRACT: Sulfation is a common modification of extracellular glycans, tyrosine residues on proteins, and steroid hormones, and is important in a wide variety of signaling pathways. We investigated the role of sulfation on endogenous oxidative stress, such as glutamate-induced oxytosis and erastin-induced ferroptosis, using mouse hippocampal HT22 cells. Sodium chlorate competitively inhibits the formation of 3'-phosphoadenosine 5'-phosphosulfate, the high energy sulfate donor in cellular sulfation reactions. The treatment of HT22 cells with sodium chlorate decreased sulfation of heparan sulfate proteoglycans and chondroitin sulfate proteoglycans. Sodium chlorate and ?-d-xyloside, which prevents proteoglycan glycosaminoglycan chain attachment, exacerbated both glutamate- and erastin-induced cell death, suggesting that extracellular matrix influenced oxytosis and ferroptosis. Moreover, sodium chlorate enhanced the generation of reactive oxygen species and influx of extracellular Ca2+ in the process of oxytosis and ferroptosis. Interestingly, sodium chlorate did not affect antioxidant glutathione levels. Western blot analysis revealed that sodium chlorate enhanced erastin-induced c-Jun N-terminal kinase phosphorylation, which is preferentially activated by cell stress-inducing signals. Collectively, our findings indicate that sulfation is an important modification for neuroprotection against oxytosis and ferroptosis in neuronal hippocampal cells.

PROVIDER: S-EPMC7022473 | BioStudies |

REPOSITORIES: biostudies

Similar Datasets

2017-01-01 | S-EPMC5382034 | BioStudies
| S-EPMC6439002 | BioStudies
| S-EPMC8217649 | BioStudies
| S-EPMC3423038 | BioStudies
| S-EPMC4019256 | BioStudies
2013-01-01 | S-EPMC3564003 | BioStudies
| S-EPMC2786843 | BioStudies
| S-EPMC4955955 | BioStudies
| S-EPMC9240796 | BioStudies
| S-EPMC2562295 | BioStudies