ProImmune Scientist Unravels 125-year-old enigma--Pleiotropic Paradox for Glutathione Synthesis

Share Article

The U.S. Patent Trademark Office has issued a patent for a discovery involving a pleiotropic delivery system that can revolutionize Immune System support for physiological replenishment of Glutathione by The ProImmune Company.

The ProImmune Company

Past News Releases


The tripeptide Glutathione is considered the master antioxidant and primary protector of the Immune System. It protects the body from toxins and oxidative stress. Glutathione is synthesized intracellularly, in every cell of the body. However, there are certain biochemical complexities associated with its synthesis.

The Glutathione molecule itself cannot enter or re-enter the cell. It is called out “as needed.” The proper precursors are required for Glutathione synthesis. The amino acid L-Cysteine is the pivotal rate-limiting amino acid for Glutathione synthesis, but it is highly oxidizable. It requires a special, safe delivery system, involving examples of the pleiotropic paradox.

The U.S. Patent Trademark Office issued patent RE42645E/RE39734, entitled “Nutritional or Therapeutic Compositions and Methods to Increase Bodily Glutathione Levels” to Dr. Albert B. Crum on August 23, 2011. The Patent is the basis of the Dietary Supplement Immune Formulation 200® from The ProImmune Company, L.L.C. Dr. Crum is a Harvard-educated scientist and a renowned physician. His patent recites a composition and method for the physiological synthesis of Glutathione, which unraveled examples of the pleiotropic paradox, Nature's versatility in Glutathione synthesis. In the pleiotropic paradox a single molecule can serve multiple purposes and diverse roles that provide an evolutionary advantage.The patent provides the certain precursors so the pleiotropic paradox can attain optimal function and Glutathione can be replenished as Nature has evolved over eons.

This pleiotropic paradox provides four delivery systems for the oxidizable L-Cysteine from other previously committed molecular functions.

Dr. Crum explained, the pleiotropic paradox might appear counterintuitive. Glutathione is made up of three amino acids. One of these, L-Cysteine, is considered the Glutathione molecule's most vital and functional moiety. Notwithstanding its importance as part of Glutathione, L-Cysteine in a solo state is highly oxidizable, reactive, and somewhat toxic. It is unlikely to gain admission into the intracellular Glutathione synthesis chain without a safe "neutralizing" delivery system. One pleiotropic delivery system is L-Cystine, which is the form that L-Cysteine takes when it self-oxidizes. L-Cystine is actually two molecules of L-Cysteine, which are locked in a disulfide bond like two oxen yoked. Without L-Cystine carrier help, trying to control L-Cysteine would be like trying to control rambunctious horses without harnesses. The disulfide bond neutralizes L-Cysteine's electronic distractibility, holds the two L-Cysteines fast, thus providing safe carriage to the cell membrane.

L-Cystine had long been considered "used-up," inert or spent, because its two L-Cysteines are locked like yoked oxen. But Dr. Crum saw L-Cystine as a temporary "sleeper" for a safe delivery system. He perceived how Nature intends to recycle the so-called "used up" L-Cysteines. He saw used up L-Cysteines as only temporarily bound up in the L-Cystine: a safe delivery system and a form of bodily protection from the oxidizing mischief of solo L-Cysteine. The L-Cystine would later release these two L-Cysteines safely for recycling when contact is made with substrate-specific enzymes in the cell membrane. This is only one example of the pleiotropic paradox.

The pleiotropic paradox recognizes another carrier role for L-Cystine’s disulfide bond. This is also counter-intuitive: L-Cystine itself is a marker of oxidative stress, and at the same time it is also a protection from oxidants of L-Cysteine and a carrier for two L-Cysteines to be safely recycled into the master antioxidant Glutathione. In addition, the highly reactive and highly oxidizable solo L-Cysteine can "catch a ride" on that disulfide bond by way of an electronic coupling relationship. This coupling relationship can be likened to a quantum-like electron exchange. That relationship holds the high oxidizability of solo L-Cysteine in abeyance and provides safe delivery of an extra L-Cysteine to the cell membrane facilitating Glutathione synthesis with this extra supply of L-Cysteine.

Another example of the pleiotropic paradox delivery system is manifested by the amino acid L-Methionine, which has its own functions as an amino acid. However, it has another role: like a butterfly emerging from its existence as a caterpillar, it also serves to metamorphose as a carrier for the vital L-Cysteine. L-Methionine safely carries the L-Cysteine as a part of its internal molecular structure, and after transsulfuration, it intracellularly releases its "butterfly," which is the L-Cysteine molecule. The vital immune enhancing process of Glutathione synthesis, which protects and supports the immune system, requires a constant supply of L-Cysteine.

The fourth pleiotropic paradox in Glutathione synthesis is Glutathione itself! In addition to its multiple immune/detox functions, it also functions to deliver another L-Cysteine from within its own molecular structure. While "cruising" the bloodstream, Glutathione can stop by a cell, whereupon the cell's enzymes dismantle the Glutathione molecule, which “sacrifices” itself to release an L-Cysteine for the cell to make additional Glutathione.

Many university research studies have documented the "proof of principle" inherent in the patent, and the resultant findings have been published in peer-reviewed scientific journals.

Share article on social media or email:

View article via:

Pdf Print

Contact Author

Gail Speckamp
Visit website