
NADH (vitamin B3), in nature, is found in all the living cells of plants, animals and humans. All 60 trillion cells found in the human body contain it. Brain cells contain about 50 mcg of NADH per gram of brain tissue. Heart cells contain 90 mcg of NADH per gram of heart tissue. Red blood cells contain 4 mcg of NADH. The more energy a cell needs, the higher the concentrations of NADH.
NADH is also known as co-enzyme #1 because it is top ranked over all other co-enzymes. This includes a ranking over the well known co-enzyme Q-10.
Co-enzymes are essential components of enzymes which are necessary for every metabolic reaction in our body. Co-enzymes also form other molecules in cells. Cells need these molecules to perform their functions. Without co-enzymes, the human machine does not work and all cell processes stop.
In our bodies, NADH is destroyed or depleted. The world’s most renowned doctors and scientists don’t know why NADH is being depleted from our body’s. Somehow stress, fatigue, old age, environmental chemicals, and disease may damaged or deplete our NADH supplies. Even with enough glucose and oxygen (fuel and air) some cellular engines don’t produce enough power.
We can obtain some NADH from our diet or from a dietary supplement. Either way NADH has to come from outside the body. The body doesn’t make NADH. The problem is, NADH is destroyed almost instantly by the digestive tract in humans and thus what we can get from our food or from the multitude of supplements you can find all over the net is not going to be enough to supplement our needs.

In comes NAD+
NAD+, is a redox pair to NADH and is not broken down in the digestive tract like NADH is. NAD+ activates SIRT1 (sirtuin 1). SIRT1 is the most extensively studied of the seven-member family of mammalian sirtuins. SIRT1 couples NAD+ hydrolysis with protein deacylation. It is a member of the class III family of histone deacylases and regulates DNA repair and gene transcription. SIRT1 has profound beneficial effects on renal diseases including renal aging, diabetic nephropathy, and the response to unilateral ureteral obstruction. Furthermore, SIRT1 has recently received much attention because it has salutary effects on metabolic syndrome and may mediate some of the life-prolonging effects of caloric restriction.
NAD+ is an essential cofactor for the poly-(ADP-ribose) polymerases (PARPs). These enzymes attach negatively charged polymers of ADP-ribose to proteins and change their function; in this way, PARP1 regulates apoptosis, DNA repair, necrosis, and gene transcription, including transcription of proinflammatory genes. This regulation is germane to this discussion because PARP1 is required for cisplatin nephrotoxicity.

So why am I mentioning NADH if this topic is about NAD+? Well, as mentioned above, because NAD+ is a redox pair of NADH, that means that after NAD+ has carried out its function in your body it will convert to NADH and after NADH has carried out its function, will convert back to NAD+. This conversion, however, is not on par. It will continually reduce with the eventual destruction and elimination of the co-enzymes so it is necessary to continue intake and up regulation of both. As mention previous, however, taking NADH orally will not help because it is destroyed by the intestinal tract.

So, stop looking for Vitamin B3 and start looking for supplies of NAD+.

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