C. elegans aging is modulated by hydrogen sulfide and the sulfhydrylase/cysteine synthase cysl-2.
Exogenous hydrogen sulfide (H2S) administration and endogenous H2S metabolism were explored in the nematode C. elegans. Chronic treatment with a slow-releasing H2S donor, GYY4137, extended median survival by 17-23% and increased tolerance towards oxidative and endoplasmic reticulum (ER) stress. Also...
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2013
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oai:doaj.org-article:a9489aeae4c74d0eaa9292ce1d8434182021-11-18T08:47:42ZC. elegans aging is modulated by hydrogen sulfide and the sulfhydrylase/cysteine synthase cysl-2.1932-620310.1371/journal.pone.0080135https://doaj.org/article/a9489aeae4c74d0eaa9292ce1d8434182013-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/24260346/pdf/?tool=EBIhttps://doaj.org/toc/1932-6203Exogenous hydrogen sulfide (H2S) administration and endogenous H2S metabolism were explored in the nematode C. elegans. Chronic treatment with a slow-releasing H2S donor, GYY4137, extended median survival by 17-23% and increased tolerance towards oxidative and endoplasmic reticulum (ER) stress. Also, cysl-2, a sulfhydrylase/cysteine synthase in C. elegans, was transcriptionally upregulated by GYY4137 treatment and the deletion of cysl-2 resulted in a significant reduction in lifespan which was partially recovered by the supplementation of GYY4137. Likewise, a mammalian cell culture system, GYY4137 was able to protect bovine aortic endothelial cells (BAECs) from oxidative stress and (H2O2)-induced cell death. Taken together, this provides further support that H2S exerts a protective function which is consistent with the longevity dividend theory. Overall, this study underlines the therapeutic potential of a slow-releasing H2S donor as regulators of the aging and cellular stress pathways.Bedoor QabazardSamanza AhmedLing LiVolker M ArltPhilip K MooreStephen R StürzenbaumPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 8, Iss 11, p e80135 (2013) |
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Medicine R Science Q Bedoor Qabazard Samanza Ahmed Ling Li Volker M Arlt Philip K Moore Stephen R Stürzenbaum C. elegans aging is modulated by hydrogen sulfide and the sulfhydrylase/cysteine synthase cysl-2. |
description |
Exogenous hydrogen sulfide (H2S) administration and endogenous H2S metabolism were explored in the nematode C. elegans. Chronic treatment with a slow-releasing H2S donor, GYY4137, extended median survival by 17-23% and increased tolerance towards oxidative and endoplasmic reticulum (ER) stress. Also, cysl-2, a sulfhydrylase/cysteine synthase in C. elegans, was transcriptionally upregulated by GYY4137 treatment and the deletion of cysl-2 resulted in a significant reduction in lifespan which was partially recovered by the supplementation of GYY4137. Likewise, a mammalian cell culture system, GYY4137 was able to protect bovine aortic endothelial cells (BAECs) from oxidative stress and (H2O2)-induced cell death. Taken together, this provides further support that H2S exerts a protective function which is consistent with the longevity dividend theory. Overall, this study underlines the therapeutic potential of a slow-releasing H2S donor as regulators of the aging and cellular stress pathways. |
format |
article |
author |
Bedoor Qabazard Samanza Ahmed Ling Li Volker M Arlt Philip K Moore Stephen R Stürzenbaum |
author_facet |
Bedoor Qabazard Samanza Ahmed Ling Li Volker M Arlt Philip K Moore Stephen R Stürzenbaum |
author_sort |
Bedoor Qabazard |
title |
C. elegans aging is modulated by hydrogen sulfide and the sulfhydrylase/cysteine synthase cysl-2. |
title_short |
C. elegans aging is modulated by hydrogen sulfide and the sulfhydrylase/cysteine synthase cysl-2. |
title_full |
C. elegans aging is modulated by hydrogen sulfide and the sulfhydrylase/cysteine synthase cysl-2. |
title_fullStr |
C. elegans aging is modulated by hydrogen sulfide and the sulfhydrylase/cysteine synthase cysl-2. |
title_full_unstemmed |
C. elegans aging is modulated by hydrogen sulfide and the sulfhydrylase/cysteine synthase cysl-2. |
title_sort |
c. elegans aging is modulated by hydrogen sulfide and the sulfhydrylase/cysteine synthase cysl-2. |
publisher |
Public Library of Science (PLoS) |
publishDate |
2013 |
url |
https://doaj.org/article/a9489aeae4c74d0eaa9292ce1d843418 |
work_keys_str_mv |
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