NAD Test - How to determine your NAD level
The NAD blood test is a simple dry blood test that allows you to determine the level of NAD in your cells. Nicotinamide adenine dinucleotide (NAD) levels decrease with age and play a role in the age-related decline in metabolic function. To date, the exact mechanism responsible for the age-related decline in NAD has not been elucidated. Thus, increasing NAD levels improves healthspan.
NAD Test - What is NAD?
NAD stands for nicotinamide adenine dinucleotide. This molecule consists of two mononucleotides linked together by a chemical bond. The molecule is a coenzyme found in almost every cell of an organism. Coenzymes are small organic molecules, like vitamins, that work with enzymes to trigger chemical reactions. You can think of it like flying an airplane: theoretically, the plane can be controlled by a single pilot, but it's important and useful to have an additional co-pilot to assist. Through this interaction in our bodies, molecules like NAD help determine the action of enzymes. For example, studies show that NAD is required for more than 500 of these enzymatic reactions. It is thus clear that the coveted co-pilots play an important role in many biological processes.
The discovery of NAD and its redox properties by Otto Warburg contributed significantly to the clarification of terminology. He is the one who defined NAD as a "charge-independent chemical framework". Thus, NAD+ is the oxidized form of NAD (which can accept electrons) and NADH is the reduced form of NAD (which can donate electrons). In overview, chemistry refers to NAD+/NADH as a so-called redox couple. The harmony of this relationship is essential for energy production in the human body. In the mitochondria, the powerhouses of the cell, NADH releases electrons into the respiratory chain, enabling the production of adenosine triphosphate (ATP), our universal energy carrier. All that remains is NAD+ and its willingness to recapture the electron.
NAD Self Test - Production of NAD
There is a "rate-limiting" step in the generation of NAD. This means that synthesis is heavily dependent on one enzyme, and that is NAMPT. If you have enough of this enzyme, you can make many molecules. If the enzyme is missing, production will stop or at least be limited. The amount of NAMPT is very dynamic. Therefore, the organism can adapt very quickly to changing NAD requirements within a cell. These changing conditions include cellular stress caused by DNA damage and starvation.
NAD test - What does NAD do in the body?
In mammals, sirtuins and PARP are the two major NAD+-responsive signaling protein families. Both enzymes are molecule-dependent. Sirtuins, also called longevity genes, were described in the mid-1980s as telomere-protecting proteins. It is now known that their roles go far beyond that. The seven-member protein family plays a role in mitochondrial metabolism, inflammation, cell division, autophagy processes, circadian rhythms and programmed cell death (apoptosis).
The PARP family is larger than the sirtuin family, but not all family members have been equally well studied or analyzed. In any case, PARP1 and PARP2 are among the well-studied proteins, and so studies have been able to understand their role to some extent. They are important in DNA repair and likewise involved in regulating the translation of DNA language into protein language. As we age, DNA damage accumulates and cell stress increases. As a result, overactivation of PARP1 may reduce NAD+ levels more. However, research findings are paradoxical in this regard. Some studies have shown that PARP blockade is a positive factor, while another found that PARP activation positively correlates with lifespan. There are still unanswered questions that research cannot answer at this time. You can test for NAD levels in your blood on your own and get clarity with an NAD test.
NAD test - metabolism
Although the amount of NAD can be measured constantly over a period of time, in reality the molecule is constantly being remodeled, degraded or recycled within the cell. NAD exists in the body in two "states" - as a free molecule or bound to proteins. The relationships between them are referred to as ratios, which are expressed differently in different cells and tissues. With the exception of neurons, mammalian cells can neither import nor produce NAD. Therefore, the molecule must first be reassembled from different components within the cell. This happens via the essential amino acid tryptophan or other forms of vitamin B3. To maintain intracellular NAD levels, it is mainly "recycled" via the so-called salvage pathway. "Salvage" is of English origin and means to save. Therefore, most of the nicotinamide adenine dinucleotide is recycled rather than newly manufactured. Our bodies are way ahead of society in this regard. Then there is a third, not quite so significant way to produce the molecule.
