The Active Methionine
What is S-Adenosyl Methionine (SAM-e)?
S-Adenosyl Methionine
(S-adenosyl-L-methionine or SAM-e) is an amino acid derivative that has
been clinically proven to benefit brain, liver, and joint function .
Found in all living cells, SAM-e is also called "activated methionine"
(an essential amino acid) since it is formed by the combination of ATP
(adenosine triphosphate) and methionine. Simply supplementing with
methionine, however, does not result in SAM-e elevation: conversely,
methionine can cause elevation of the toxic amino acid homocysteine. SAM-e
has undergone dozens of clinical trials involving thousands of
patients. Researchers studying the beneficial efforts of SAM-e have
identified many structure and function-based benefits of SAM-e.
Liver Detoxification
SAM-e metabolism
supports the synthesis of glutathione (GSH) and glutathione-dependent
enzymes (glutathione peroxidase and glutathione-S-transferase), which
are important for liver function.
Glutathione
is necessary for scavenging free radicals produced by glycolysis, the
breakdown of carbohydrates for energy. The amino acid taurine is
another end product of SAM-e metabolism. The glutathione family of
compounds and taurine are important for liver detoxification reactions.
Brain Function
SAM-e supports brain
function by its methylation effects. Methylation is the process by
which a four atom appendage know as methyl group (unit of one carbon
and three hydrogen atoms) is transferred from one molecule to another.
Of all methyl-donating substances known in mammalian metabolism, SAM-e
is the most important.
The
donation of methyl groups affects proper function of many metabolic
processes including brain function, energy production and DNA
metabolism. Neurotransmitters, substances involved in the brain's
cell-to-cell communication, are the products of substances known in
mammalian methylation reactions. These compounds include L-dopa,
dopamine, epinephrine and phosphatidylcholine (a component of lecithin).
Energy Production
Methylation from SAM-e
is critical for proper energy production as it coverts guanidinoacetate
to creatine. Creatine metabolizes to creatine phosphate, which is
important for recycling of ADP to ATP. Creatine maximizes physical
performance, reduces exercise fatigue and improves recovery after
exercise.
Longevity
Methylation
of DNA appears to be important in the prevention of DNA imperfections.
The demethylation of DNA is considered to contribute to the aging
process. Proper methylation through substances such as SAM-e positively
influence longevity.
Not All SAM-e is Created Equal Jarrow Formulas®
SAM-e is of the active (S,S) form. SAM-e is a chiral molecule and
therefore consists of two forms: (S,S) SAM-e and (R,S) SAM-e. The
biologically active form is the (S,S) structure, while the (R,S)
structure is a biologically inactive. Jarrow Formulas®
SAM-e is made naturally by microbiological fermentation and then
specially processed, without solvents, to preserve 68-80% (S,S) SAM-e,
the highest active level available.
Because SAM-e is a highly
reactive molecule, it is very fragile. It degrades rapidly under
conditions of high heat and/or humidity. Improper handling of SAM-e can
cause its degradation in a matter of hours, resulting in a loss of
biological activity. This is why the manufacturing process for Jarrow
Formulas® SAM-e is done under low temperature and low humidity, and the tablet is enteric coated and blister-packed.
Pharmacokinetic
studies show that oral supplementation of SAM-e is most effective when
enteric-coated by special gastric fluid-resistant polymers. Enteric
coating SAM-e results in maximum SAM-e levels in the bloodstream.
Source: Jarrow Formulas
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Scientific References
- Murray, RK, et al., (1996) Harper's Biochemistry (24th edition). (Standford, CT: Appleton & Lange.
- Strementinoil,
(1987) Pharmacologic Aspects of S-adenosyl-methionine: Pharmacokinetics
and Pharmacodynamics, American Journal Of Medicine 83, Suppl. 5A, 35-42.
- McCully, Kilmer S., The Homocysteine Revolution. (New Canaan, CT: Keats Publishing, Inc., 1997)
- Frankel,
Paul and Madsen, Fred, Stop Homocysteine Through the Methylation
Process. (Thousands Oaks, CA: The Research Corner, 1988).
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