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Are we getting enough sulfur in our diet?

Nimni ME, Han B, Cordoba F - Nutr Metab (Lond) (2007)

Bottom Line: Sulfur, after calcium and phosphorus, is the most abundant mineral element found in our body.This method asses amino acid requirements for protein synthesis, only one of the pathways that methionine follows after ingestion.Out of this study came information that suggested that a significant proportion of the population that included disproportionally the aged, may not be receiving sufficient sulfur and that these dietary supplements, were very likely exhibiting their pharmacological actions by supplying inorganic sulfur.

View Article: PubMed Central - HTML - PubMed

Affiliation: Departments of Surgery and Biochemistry and Molecular Biology, Keck School of Medicine, University of Southern California, Los Angeles, CA, 90032, USA. nimni007@aol.com.

ABSTRACT
Sulfur, after calcium and phosphorus, is the most abundant mineral element found in our body. It is available to us in our diets, derived almost exclusively from proteins, and yet only 2 of the 20 amino acids normally present in proteins contains sulfur. One of these amino acids, methionine, cannot be synthesized by our bodies and therefore has to be supplied by the diet. Cysteine, another sulfur containing amino acid, and a large number of key metabolic intermediates essential for life, are synthesized by us, but the process requires a steady supply of sulfur.Proteins contain between 3 and 6% of sulfur amino acids. A very small percentage of sulfur comes in the form of inorganic sulfates and other forms of organic sulfur present in foods such as garlic, onion, broccoli, etc.The minimal requirements (RDA) for all the essential amino acids have always been estimated in terms of their ability to maintain a nitrogen balance. This method asses amino acid requirements for protein synthesis, only one of the pathways that methionine follows after ingestion. To adequately evaluate the RDA for methionine, one should perform, together with a nitrogen balance a sulfur balance, something never done, neither in humans nor animals.With this in mind we decided to evaluate the dietary intake of sulfur (as sulfur amino acids) in a random population and perform sulfur balance studies in a limited number of human volunteers. Initially this was done to try and gain some information on the possible mode of action of a variety of sulfur containing compounds (chondroitin sulfate, glucosamine sulfate, and others, ) used as dietary supplements to treat diseases of the joints. Out of this study came information that suggested that a significant proportion of the population that included disproportionally the aged, may not be receiving sufficient sulfur and that these dietary supplements, were very likely exhibiting their pharmacological actions by supplying inorganic sulfur.

No MeSH data available.


Related in: MedlinePlus

Enzymatic conversion of arachidonic acid (AA) to PGs and the sites of inhibition by GSH and GSH peroxidase (GSSPx). (Adapted from Marglit et al. [36]).
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Figure 2: Enzymatic conversion of arachidonic acid (AA) to PGs and the sites of inhibition by GSH and GSH peroxidase (GSSPx). (Adapted from Marglit et al. [36]).

Mentions: The observation that both the constitutive and the mitogen inducible isoforms of prostaglandin H2 synthetase are markedly affected by GSH and GSH peroxidase [35], has catalyzed significant interest in connection with this process. The sites of action of GSH and GSH peroxidase on the metabolic pathway in question is shown in Fig 2.


Are we getting enough sulfur in our diet?

Nimni ME, Han B, Cordoba F - Nutr Metab (Lond) (2007)

Enzymatic conversion of arachidonic acid (AA) to PGs and the sites of inhibition by GSH and GSH peroxidase (GSSPx). (Adapted from Marglit et al. [36]).
© Copyright Policy - open-access
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC2198910&req=5

Figure 2: Enzymatic conversion of arachidonic acid (AA) to PGs and the sites of inhibition by GSH and GSH peroxidase (GSSPx). (Adapted from Marglit et al. [36]).
Mentions: The observation that both the constitutive and the mitogen inducible isoforms of prostaglandin H2 synthetase are markedly affected by GSH and GSH peroxidase [35], has catalyzed significant interest in connection with this process. The sites of action of GSH and GSH peroxidase on the metabolic pathway in question is shown in Fig 2.

Bottom Line: Sulfur, after calcium and phosphorus, is the most abundant mineral element found in our body.This method asses amino acid requirements for protein synthesis, only one of the pathways that methionine follows after ingestion.Out of this study came information that suggested that a significant proportion of the population that included disproportionally the aged, may not be receiving sufficient sulfur and that these dietary supplements, were very likely exhibiting their pharmacological actions by supplying inorganic sulfur.

View Article: PubMed Central - HTML - PubMed

Affiliation: Departments of Surgery and Biochemistry and Molecular Biology, Keck School of Medicine, University of Southern California, Los Angeles, CA, 90032, USA. nimni007@aol.com.

ABSTRACT
Sulfur, after calcium and phosphorus, is the most abundant mineral element found in our body. It is available to us in our diets, derived almost exclusively from proteins, and yet only 2 of the 20 amino acids normally present in proteins contains sulfur. One of these amino acids, methionine, cannot be synthesized by our bodies and therefore has to be supplied by the diet. Cysteine, another sulfur containing amino acid, and a large number of key metabolic intermediates essential for life, are synthesized by us, but the process requires a steady supply of sulfur.Proteins contain between 3 and 6% of sulfur amino acids. A very small percentage of sulfur comes in the form of inorganic sulfates and other forms of organic sulfur present in foods such as garlic, onion, broccoli, etc.The minimal requirements (RDA) for all the essential amino acids have always been estimated in terms of their ability to maintain a nitrogen balance. This method asses amino acid requirements for protein synthesis, only one of the pathways that methionine follows after ingestion. To adequately evaluate the RDA for methionine, one should perform, together with a nitrogen balance a sulfur balance, something never done, neither in humans nor animals.With this in mind we decided to evaluate the dietary intake of sulfur (as sulfur amino acids) in a random population and perform sulfur balance studies in a limited number of human volunteers. Initially this was done to try and gain some information on the possible mode of action of a variety of sulfur containing compounds (chondroitin sulfate, glucosamine sulfate, and others, ) used as dietary supplements to treat diseases of the joints. Out of this study came information that suggested that a significant proportion of the population that included disproportionally the aged, may not be receiving sufficient sulfur and that these dietary supplements, were very likely exhibiting their pharmacological actions by supplying inorganic sulfur.

No MeSH data available.


Related in: MedlinePlus