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The essentiality of sulfur is closely related to nitrogen metabolism: a clue to hyperhomocysteinaemia

Published online by Cambridge University Press:  14 December 2007

Yves Ingenbleek*
Affiliation:
Laboratory of Nutrition, Faculty of Pharmacy, University Louis Pasteur, 74 Route du Rhin, 67401 Illkirch, France
Vernon R Young
Affiliation:
Laboratory of Human Nutrition, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, MA O2139-4307, USA
*
Corresponding author: Dr Yves Ingenbleek, fax +33 390 24 43 17, email [email protected]
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Abstract

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N and S metabolisms are closely interwoven throughout both the plant and animal kingdoms. The essentiality of S relates to its participation in the structure of S-containing amino acids (SAA), to its inclusion in many sulfonated molecules, and to a myriad of metabolic and catalytic reactions of vital importance. Methionine (Met) is the indispensable SAA supplied by food proteins and its plasma homeostasis is achieved via a number of highly efficient regulatory mechanisms. In all conditions characterised by a negative body protein balance such as in dietary restriction or cytokine-induced hypercatabolic losses, N and S endogenous pools manifest parallel tissue depletion rates. Adaptive conservation of N and S body stores is reached by a functional restraint of the trans-sulfuration cascade, through the depression of cystathionine β-synthase activity. As a result, upstream accumulation of homocysteine favours its re-methylation conversion to Met which helps maintain metabolic pathways of survival value. In addition to the measurement of vitamin indices, that of plasma transthyretin, a sensitive marker of protein nutritional status, is proposed to identify the fluctuations of the total body N component accountable for the alterations of homocysteine concentrations in body fluids.

Type
Research Article
Copyright
Copyright © The Authors 2004

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