![]() |
|
|
Division of Nutritional Sciences, Cornell University, Ithaca, NY 14853
The metabolism of cysteine and cysteinesulfinate and the activities of key enzymes in cysteine catabolic pathways were investigated in hepatocytes isolated from rats fed a basal (100 g casein/kg) diet or the diet supplemented with L-methionine (3 or 10 g/kg diet) or the sulfur equivalent as L-cystine (2.4 or 8 g/kg diet). Cysteine dioxygenase activity was higher in hepatocytes from rats fed diets with the higher level of sulfur amino acid supplementation, and the higher enzyme activity was paralleled by a greater total catabolite production (taurine + sulfate) from cysteine. Taurine production as a percentage of total cysteine catabolism was significantly greater in hepatocytes from rats fed the diet with excess methionine or cystine (basal, 22%; excess methionine, 61%, excess cystine, 49%). Glutathione production was markedly lower in hepatocytes from rats fed excess sulfur amino acids such that total cysteine utilization was similar for all dietary treatments. Cysteinesulfinate decarboxylase activity and catabolism of cysteinesulfinate by hepatocytes were unaffected by the dietary supplementations. Results are in contrast to previous studies in which increased dietary protein resulted in decreased cysteinesulfinate decarboxylase activity and decreased partitioning of cysteinesulfinate to taurine vs. sulfate. Thus, sulfur amino acids may be less effective than protein in decreasing cysteinesulfinate decarboxylase activity and may result in a pattern of sulfur catabolite production from cysteine that favors taurine production.
KEY WORDS: taurine hepatocytes rats glutathione sulfur amino acids
1 Presented in part at Experimental Biology 93, March 28April 1, 1993, New Orleans, LA [Bagley, P. J. & Stipanuk, M. H. (1993) Increased sulfur amino acid intake results in increased cysteinesulfinate-dependent metabolism of cysteine to taurine. FASEB J. 7:A385 (abs.)].
2 Supported by NRICCP/USDA Competitive Research Grant no. 92-37200-7583 and by USDA/CSRS grant no. 89-34115-4498.
3 The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 USC section 1734 solely to indicate this fact.
4 Current address: USDA Human Nutrition Research Center on Aging at Tufts University, 711 Washington Street, Boston, MA 02111.
5 To whom correspondence should be addressed.
Manuscript received 22 June 1994. Revision accepted 6 September 1994.
This article has been cited by other articles:
![]() |
J. E. Dominy Jr., J. Hwang, S. Guo, L. L. Hirschberger, S. Zhang, and M. H. Stipanuk Synthesis of Amino Acid Cofactor in Cysteine Dioxygenase Is Regulated by Substrate and Represents a Novel Post-translational Regulation of Activity J. Biol. Chem., May 2, 2008; 283(18): 12188 - 12201. [Abstract] [Full Text] [PDF] |
||||
![]() |
S. C. Chai, J. R. Bruyere, and M. J. Maroney Probes of the Catalytic Site of Cysteine Dioxygenase J. Biol. Chem., June 9, 2006; 281(23): 15774 - 15779. [Abstract] [Full Text] [PDF] |
||||
![]() |
M. H. Stipanuk, J. E. Dominy Jr., J.-I. Lee, and R. M. Coloso Mammalian Cysteine Metabolism: New Insights into Regulation of Cysteine Metabolism J. Nutr., June 1, 2006; 136(6): 1652S - 1659S. [Abstract] [Full Text] [PDF] |
||||
![]() |
I. C. Mcmillen and J. S. Robinson Developmental Origins of the Metabolic Syndrome: Prediction, Plasticity, and Programming Physiol Rev, April 1, 2005; 85(2): 571 - 633. [Abstract] [Full Text] [PDF] |
||||
![]() |
M. H. Stipanuk, L. L. Hirschberger, M. P. Londono, C. L. Cresenzi, and A. F. Yu The ubiquitin-proteasome system is responsible for cysteine-responsive regulation of cysteine dioxygenase concentration in liver Am J Physiol Endocrinol Metab, March 1, 2004; 286(3): E439 - E448. [Abstract] [Full Text] |
||||
![]() |
L. Brawley, C. Torrens, F. W. Anthony, S. Itoh, T. Wheeler, A. A. Jackson, G. F. Clough, L. Poston, and M. A. Hanson Glycine rectifies vascular dysfunction induced by dietary protein imbalance during pregnancy J. Physiol., January 15, 2004; 554(2): 497 - 504. [Abstract] [Full Text] [PDF] |
||||