Glutaric acid is made from lysine & tryptophan via alphaketo-adipic acid.

- Elevated in the genetic diseases glutaric academia types I and II.
- Moderate increases may be due to deficiencies in riboflavin and coenzyme Q10, or celiac disease.
- Moderate increases are common in autism possibly due to defective vitamin absorption or microbial production in the GI tract.

Glutaric Acid (Glutarate) is endogenously produced in the catabolism of lysine and tryptophan.

- Increased Glutaric acid is associated with secondary carnitine deficiency.

- Glutaryl-CoA (from lysine or tryptophan) normally enters the Krebs cycle via transition to acetyl-CoA.

    » Glutaryl-CoA dehydrogenase (GCDH) + glutaryl-CoA + B2 → acetyl-CoA.

    » If GCDH is blocked, glutaryl-CoA + carnitine → elevated glutaric acid.

Glutaric Acid is formed from the essential amino acids lysine and tryptophan through the intermediaries of alpha ketoadipic acid and glutaryl-CoA. Glutaryl-CoA is further metabolized to glutaconyl- and crotonyl-CoA by an enzyme called glutaryl-CoA dehydrogenase. This enzyme requires riboflavin (vitamin B2) as a cofactor.

Glutaric acid is a breakdown product of lysine and/or tryptophan.

Glutaric Acid is formed from the essential amino acids lysine and tryptophan through the intermediaries of alpha ketoadipic acid and glutaryl-CoA. Glutaryl-CoA is further metabolized to glutaconyl- and crotonyl-CoA by an enzyme called glutaryl-CoA dehydrogenase. This enzyme requires riboflavin (vitamin B2) as a cofactor.

Glutaric Acid is formed from the essential amino acids lysine and tryptophan through the intermediaries of alpha ketoadipic acid and glutaryl-CoA. Glutaryl-CoA is further metabolized to glutaconyl- and crotonyl-CoA by an enzyme called glutaryl-CoA dehydrogenase. This enzyme requires riboflavin (vitamin B2) as a cofactor.

Glutathione is implicated in many cellular functions including antioxidant protection and detoxification. It is also essential for the maintenance of cell membrane integrity in red blood cells.

Glutathione (GSH) is a tripeptide comprised of three amino acids (cysteine, glycine, and glutamic acid). Glutathione is the body’s most potent intracellular antioxidant. It exists intracellularly in either an oxidized or reduced state.

GSH acts as an antioxidant, free radical scavenger, and detoxifying agent. Excessive formation of reactive oxygen species (ROS), including hydrogen peroxide (H2O2), is toxic to the cell. Hence, the metabolism of these free radicals are critical, and they are tightly controlled. [L]

Glutathione (GSH) is composed of cysteine, glutamine & glycine. GSH is a source of sulfate and plays a key role in antioxidant activity and detoxification of toxins.

Glutathione is the most powerful antioxidant in the human body. It is found in nearly every cell in the body and is the primary agent of detoxification in the liver. Glutathione can also act as a hormone, regulating the release of GABA and dopamine. Glutathione is produced from three amino acids glutamate, cysteine, and glycine which are obtained from food or supplementation. Deficiency in glutathione may lead to production of free radicals and oxidative damage throughout the body. Recent evidence suggests that the gut microbiome determines levels of glutathione throughout the body.

Glutathione (GSH) is a tripeptide (λ-glutamyl-cysteinylglycine) synthesized by most cells, serving as a critical marker of cellular health and resilience against toxic stress. In erythrocytes, GSH levels are a sensitive indicator of the body's intracellular GSH status and overall cellular well-being. It is the most abundant non-protein thiol in mammalian cells, playing key roles in various biological processes, such as detoxifying harmful compounds (xenobiotics), neutralizing reactive oxygen species, regulating cellular redox balance, and maintaining the oxidative state of vital protein sulfhydryl groups. Additionally, GSH supports immune function. Intracellular GSH concentrations are significantly higher than plasma levels, with plasma GSH largely derived from the liver.

The allergen-specific IgE antibody test is a key diagnostic method for identifying gluten allergies, measuring an individual's IgE response to gluten. It is used alongside clinical evaluations for a comprehensive allergy diagnosis. While sensitive, this test indicates only IgE sensitization, not necessarily an allergy, as many sensitized individuals don't exhibit symptoms. Wheat, containing gluten, is a common allergen with varied symptoms and affects a small percentage of the global population. Management of wheat allergy primarily involves dietary avoidance and, in some cases, oral immunotherapy, with epinephrine auto-injectors prescribed for severe reactions. The prevalence and severity of wheat allergy vary globally, often associated with other atopic disorders in children.

Gluten (F79) IgG is a specific immunoglobulin G antibody marker used in the immunological assessment of gluten sensitivity and related disorders. This antibody targets a fraction of gluten proteins, primarily found in wheat and related grains, and its presence in the bloodstream can be indicative of an immune response to gluten ingestion.

Fecal gluten monitoring is an important tool to:

- Quantitively evaluate amount of gluten peptide in stool for accurate assessment of potential exposure

- Monitor adherence to gluten-free diet for anyone aiming to follow a GF lifestyle

- Monitor accidental (unintentional) consumption of gluten for both the celiac and non-celiac gluten sensitive patient, even if they are not experiencing symptoms

- Assist in the assessment of refractory celiac (failure to heal despite going GF)