Abstract
Hydrogen sulfide is the third and most recently discovered gaseous signaling molecule following nitric oxide and carbon monoxide, playing important roles both in normal physiological conditions and disease progression. The trimethylsulfonium ion (TMS) can result from successive methylation reactions of hydrogen sulfide. No report exists so far about the presence or quantities of TMS in human urine. We developed a method for determining TMS in urine using liquid chromatography-electrospray ionization-triple quadrupole mass spectrometry (LC-ESI-QQQ), and applied the method to establish the urinary levels of TMS in a group of human volunteers. The measured urinary levels of TMS were in the nanomolar range, which is commensurate with the steady-state tissue concentrations of hydrogen sulfide previously reported in the literature. The developed method can be used in future studies for the quantification of urinary TMS as a potential biomarker for hydrogen sulfide body pools.
Highlights
Hydrogen sulfide is the third and most recently discovered gaseous signaling molecule following nitric oxide and carbon monoxide, playing important roles both in normal physiological conditions and disease progression
One of the pathways that may potentially contribute to the regulation of hydrogen sulfide is the successive methylation reactions via the thiol S-methyltransferase enzyme into dimethylsulfide[13]
Mozier et al detected trimethylsulfonium ion (TMS) in the urine of rats treated with 250 μmol/kg of dimethylsulfide and [methyl-3H] methionine[15], but the endogenous levels of TMS in animals and whether it is significantly produced without administration of the parent thioether is not known
Summary
Hydrogen sulfide is the third and most recently discovered gaseous signaling molecule following nitric oxide and carbon monoxide, playing important roles both in normal physiological conditions and disease progression. One of the pathways that may potentially contribute to the regulation of hydrogen sulfide is the successive methylation reactions via the thiol S-methyltransferase enzyme into dimethylsulfide[13]. Another enzyme, the thioether S-methyltransferase, was shown to convert various thioethers including dimethylsulfide into their respective sulfonium ions in rats[14,15]. Mozier et al detected TMS in the urine of rats treated with 250 μmol/kg of dimethylsulfide and [methyl-3H] methionine[15], but the endogenous levels of TMS in animals and whether it is significantly produced without administration of the parent thioether is not known. We discuss the results in terms of the possible use of urinary TMS as an indicator of hydrogen sulfide levels in humans
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