ArticleNeurotoxicity research2015
Inhibition of transglutaminase exacerbates polyglutamine-induced neurotoxicity by increasing the aggregation of mutant ataxin-3 in an SCA3 Drosophila model.
Article in Neurotoxicity research, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed, 9 citations in OpenAlex.
- Drosophila Transglutaminase preserves the integrity of muscle attachments with and without mechanical strain.Journal of cell science · 2026Article
- Transglutaminase inhibition stimulates hematopoiesis and reduces aggressive behavior of crayfish,The Journal of biological chemistry · 2019Article
- Cystamine and cysteamine as inhibitors of transglutaminase activityBioscience reports · 2018Review
- NF-κB Immunity in the Brain Determines Fly Lifespan in Healthy Aging and Age-Related Neurodegeneration.Cell reports · 2017Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Transglutaminases (TGs) comprise a family of Ca(2+)-dependent enzymes that catalyze protein cross-linking, which include nine family members in humans but only a single homolog in Drosophila with three conserved domains. Drosophila Tg plays important roles in cuticle morphogenesis, hemolymph clotting, and innate immunity. Mammalian tissue TG (TG2) is involved in polyglutamine diseases (polyQ diseases), and TG6 has been identified as a causative gene of a novel spinocerebellar ataxia, SCA35. Using a well-established SCA3 fly model, we found that RNA interference-mediated suppression of Tg aggravated polyQ-induced neurodegenerative phenotypes. The administration of cystamine, a known effective Tg inhibitor, enhanced ommatidial degeneration in SCA3 flies. We also demonstrated that the aggregates of pathogenic ataxin-3 increased greatly, when the Tg activity was repressed. These findings indicate that Tg is crucial for polyQ-induced neurotoxicity because Tg ablation resulted in more severe neurodegeneration due to the elevated accumulation of insoluble ataxin-3 complexes in the SCA3 Drosophila model.
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Registered trials
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