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Catabolism of Cyst(e)ine by Rat Renal Cortical Tubules¹

Division of Nutritional Sciences, Cornell University, Ithaca, NY 14853

Both cysteinesulfinate-independent and cysteinesulfinate-dependent pathways are involved in the catabolism of cyst(e)ine by freshly isolated rat renal cortical tubules. Sulfate and thiosulfate were shown to be the major sulfur-containing products that accumulated in incubations of renal tubules with 1 mmol/L or 25 mmol/L [³⁵S]cyst(e)ine. Thiosulfate is an intermediate in the oxidation of the sulfide produced by the cysteinesulfinate-independent catabolism of cyst(e)ine by desulfhydration pathway(s), whereas sulfate is formed both by further oxidation of thiosulfate and by oxidation of the sulfite formed by the cysteinesuifinate-transamination pathway. Incubation of renal tubules with propargylglycine inhibited -cystathionase activity by 85%, and this resulted in a 46% decrease in sulfate production and a 68% decrease in thiosulfate production when the treated renal tubules were incubated with 1 mmol/L [³⁵S]cyst(e)ine. Addition of 25 mmol/L unlabeled cysteinesulfinate to create a diluting/trapping pool for [³⁵S]cysteinesulfinate formed from [³⁵S]cysteine resulted in a 53% decrease in [³⁵S]sulfate production in incubations with 1 mmol/L cysteine. Thus, some cyst(e)ine catabolism probably occurred by a cysteinesulfinate-dependent pathway. No production of taurine or hypotaurine was detected in incubations with cyst(e)ine. Thus, cysteinesulfinate formed from cysteine was further catabolized primarily to sulfate instead of to taurine and hypotaurine. Most cyst(e)ine catabolism by the epithelial cells of the renal tubule probably can be accounted for by two pathways: 1) the ß-cleavage of cystine catalyzed by -cystathionase and 2) the formation and transamination of cysteinesulfinate catalyzed by cysteine dioxygenase and aspartate aminotransferase.

KEY WORDS: • cysteine • cysteinesulfinate • cystathionase • thiosulfate • rat

¹ Supported by National Institutes of Health grant DK-26959 and by New York State Hatch Project 399-492.

² To whom reprint requests should be sent.

Manuscript received 6 November 1989. Revision accepted 18 January 1990.

This article has been cited by other articles:

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