Dietary restriction transforms the mammalian protein persulfidome in a tissue-specific and cystathionine γ-lyase-dependent manner

Nazmin Bithi, Christopher Link, Yoko O. Henderson, Suzie Kim, Jie Yang, Ling Li, Rui Wang, Belinda Willard and Christopher Hine ()
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Nazmin Bithi: Cleveland Clinic Lerner Research Institute
Christopher Link: Cleveland Clinic Lerner Research Institute
Yoko O. Henderson: Cleveland Clinic Lerner Research Institute
Suzie Kim: Cleveland Clinic Lerner Research Institute
Jie Yang: Cleveland Clinic Lerner Research Institute
Ling Li: Cleveland Clinic Lerner Research Institute
Rui Wang: York University
Belinda Willard: Cleveland Clinic Lerner Research Institute
Christopher Hine: Cleveland Clinic Lerner Research Institute

Nature Communications, 2021, vol. 12, issue 1, 1-20

Abstract: Abstract Hydrogen sulfide (H2S) is a cytoprotective redox-active metabolite that signals through protein persulfidation (R-SSnH). Despite the known importance of persulfidation, tissue-specific persulfidome profiles and their associated functions are not well characterized, specifically under conditions and interventions known to modulate H2S production. We hypothesize that dietary restriction (DR), which increases lifespan and can boost H2S production, expands tissue-specific persulfidomes. Here, we find protein persulfidation enriched in liver, kidney, muscle, and brain but decreased in heart of young and aged male mice under two forms of DR, with DR promoting persulfidation in numerous metabolic and aging-related pathways. Mice lacking cystathionine γ-lyase (CGL) have overall decreased tissue protein persulfidation numbers and fail to functionally augment persulfidomes in response to DR, predominantly in kidney, muscle, and brain. Here, we define tissue- and CGL-dependent persulfidomes and how diet transforms their makeup, underscoring the breadth for DR and H2S to impact biological processes and organismal health.

Date: 2021
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Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:12:y:2021:i:1:d:10.1038_s41467-021-22001-w

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DOI: 10.1038/s41467-021-22001-w

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