Metabolic regulation of CTCF expression and chromatin association dictates starvation response in mice and flies

Sen, Devashish; Maniyadath, Babukrishna; Chowdhury, Shreyam; Kaur, Amandeep; Khatri, Subhash; Chakraborty, Arnab; Mehendale, Neelay; Nadagouda, Snigdha; Sandra, Ulacco; Kamat, Siddhesh S.; Kolthur‐Seetharam, Ullas

doi:10.1016/j.isci.2023.107128

Cited by 2 publications

(2 citation statements)

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“…For studies involving ABHD12 knockout mice, age/sex matched littermates were used as controls. Primary hepatocytes were generated using established protocols previously reported by us [53][54][55] .…”

Section: Mice Experimentsmentioning

confidence: 99%

“…HEK293T (RRID: CVCL_0063, female) cells were purchased from the ATCC, and cultured and maintained as reported earlier 11 . Primary hepatocytes were generated using established protocols previously reported by us [53][54][55] . All mammalian cells were harvested by scraping, and washed threetimes with cold sterile DPBS.…”

Section: Preparation Of Cellular Proteomic Fractionsmentioning

confidence: 99%

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Identification of ABHD6 as a regulator of lysophosphatidylserines in the mammalian liver and kidneys

Chakraborty,

Punnamraju,

Sajeevan

et al. 2024

Preprint

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SUMMARYLysophosphatidylserine (lyso-PS) is a potent hormone-like signaling lysophospholipid, which regulates many facets of mammalian biology and dysregulation in its metabolism is associated with several human neurological and autoimmune diseases. Despite the physiological importance and causal relation with human pathophysiology, little is known about the metabolism of lyso-PS in tissues other than the nervous and immune systems. To address this problem, here, we attempted to identify one (or more) lipase(s) capable of degrading lyso-PS in different mammalian tissues. We found that the membrane proteomic fraction of most mammalian tissues possess lyso-PS lipase activity, yet interestingly, the only bona fide lyso-PS lipase ABHD12 displays this enzymatic activity and has control over lyso-PS metabolism only in the mammalian brain. Using anin vitroinhibitor screen against membrane proteomic fractions of different tissues, we find that another lipase from the metabolic serine hydrolase family, ABHD6, is a putative lyso-PS lipase in the mouse liver and kidney. Finally, using pharmacological tools, we validate the lyso-PS lipase activity of ABHD6in vivo, and functionally designate this enzyme as a major lyso-PS lipase in primary hepatocytes, and the mammalian liver and kidneys.HIGHLIGHTSLyso-PS lipase enzymatic activity is present in the membrane proteomic fraction of most mammalian tissuesAnin vitroinhibitor screen identifies ABHD6 as a putative lyso-PS lipase in the liver and kidneyABHD6 functions as a lyso-PS lipase in primary hepatocytesABHD6 also performs lyso-PS lipase activityin vivoand regulates lyso-PS levels in the liver and kidney

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Section: Mice Experimentsmentioning

confidence: 99%