Redox Signaling Molecules
Redox signaling molecules include reactive oxygen species (ROS), reduced species (RS) and other electronically activated species such as nitric oxide and act as biological messengers. Arguably, hydrogen sulfide and carbon monoxide are also redox signaling molecules.
The concept of electronically activated species as messengers in both normal metabolism and in pathogenesis goes back to the 19th century. For example, we now know that reactive oxygen species likely play a key role in fibrocyte activation and thus scar formation.
In a series of papers beginning in 1941, Szent-Gyorgyi raised the possibility that modulation of electronic processes in semiconductive macromolecules plays a key role in biological function and in diseases such as cancer. Hush reviews the history of such molecular electronics.
Similarly, the first modern statement of the "ROS are messengers" component of redox signaling appears to be that of Proctor, who at a congress of free radical investigators in 1979 generalized the concept to suggest that " ....active oxygen metabolites act as specific intermediary transmitter substances for a variety of biological processes including inflammation, fibrosis, and possibly, neurotransmission.." and " One explanation for this data is that various active oxygen species ( or such products as hydroperoxides ) may act as specific transmitter substances....". This was formally published in a review in 1984.
The primary source of redox signaling molecules are produced from the mitochondria. It is estimated that mitochondria account for 50% of a person's dry weight, which is about 15% of normal weight. As the mitochondria produce ATP (adenosine tri-phosphate), the main energy molecule of the body, ROS and RS molecules are produced simultaneously. These were seen as "cellular waste" for many years until it was understood that these matabolites act as specific intermediary transmitter substances.
The formation of ROS such as hydrogen peroxide underlies much biotic and abiotic stress signaling. For example, as signaling molecules, hydrogen peroxide and other ROS post- translationally modify target proteins by oxidizing thiol groups, thus forming disulfide bonds that reversibly alter protein structure and function. Specificity is achieved by localized production, concatenate hormone or calcium signaling, with targeted secondary oxidation occurring via glutaredoxins or thioredoxins. Target proteins containing reduction-oxidation (redox) sensitive thiol groups include i) signal transduction pathway proteins, such as phosphatases and mitogen-activated protein kinases, ii) embryogenesis regulating proteins iii) any transcription factors, iv) RNA-binding proteins that direct DNA methylation, and v) proteins involved in histone acetylation, deacetylation or methylation.
ROS molecules are the weapon of choice used by the immune system. When an immune cell attacks a pathogen, it destroys it by emitting a blast of ROS molecules known as an "oxidative burst" or "respiratory burst." Pathogens are incapable of living in an enviroment of positively charged ROS that will instantly destroy them.
The ROS molecules play a crucial role is aiding the immune system in detecting damaged cells. Once damaged cells are detected, it is determined whether or not they are repairable or not. If they are repairable, they are repaired and if not, apoptosis genes are signaled to destroy the cell so that a health cell can split and fill the gap.
The reduced species or RS moleucles are not in and of themselves antioxidants although they are negatively charged. These molecules are primarily hydrogen based and compliment the ROS molecules.
The primary function of the RS molecules are to activate antioxidants. This activation process has only been understood for a relatively short period of time compared to the overall history and popularity of antioxidant science. Because of this relationship between RS molecules and antioxidants, the majority of the antioxidant properties in nutritional supplements that are purported to contain high strenghts of antioxidants are ineffective in neutralizing free radicals because of the lack of RS molecules.
Because of the balanced and complex nature of redox signaling molecules, it has been thought by the scientific community to be impossible to replicate this delicate stabilized balance outside of the body.
The body creates the majority of these molecules from sodium chloride and water in the body (salt water). Through electrochemical forms of electrolysis at a cellular level, sodium chloride and water are split into four different atoms, sodium, chlorine, hydrogen and oxygen, they are reassembled into multiple species of molecules.
Conventionally, when salt water is electrolyzed, various chorine derivities, ozone, hydrogen peroxides and other molecules are formed. However, because of the unstable nature of these molecules, they quickly revert back into common salt water. Therfore, it has been counter-intuitive to create multiple redox signaling molecules in a balance between ROS and RS in one single solution because of this reversion back to salt water.
For nearly 16 years, Medical Discoveries, Inc. from Salt Lake City, has been the leader in this field creating this balanced but unstable molecular combination. In 2009, Gary Samuelson, PhD, a medical atomic physicist had joined MDI and was the first to make the connection that the solution MDI had been producing is indeed the same molecular combination that the mitochondria produce. Dr. Samuelson went on to achive the "impossible" by developing a method to stabilize these molecules so that they do not neutarlize themselves and turn into salt water. This remarkable success has been hailed by many in the scientific community as being such an advancement that there are rumors that Dr. Samuelson may be nominated for a Nobel Prize for his breakthrough.