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Optimal range: 370 - 1600 qM/g creatinine
LEARN MOREOptimal range: 47.2 - 98.5 umol/L
Histidine is a semi-essential amino acid which is formed in the breakdown of carnosine. Red meat is a common source of carnosine, and therefore histadine. Other food sources include poultry, fish, nuts, seeds, and grains. Histidine and histamine have a unique relationship. The amino acid histadine becomes histamine via a vitamin B6- dependent enzyme called histidine decarboxylase.
Optimal range: 19.7 - 58.4 µg/g creatinine
Histidine ameliorates fatigue, promotes clear thinking and concentration, reduces appetite, decreases anxiety, improves sleep and glucose homeostasis, and gives rise to histamine.
Optimal range: 6.5 - 13.3 Units
Histidine is a semi-essential amino acid which is formed in the breakdown of carnosine. Red meat is a common source of carnosine, and therefore histadine.
Other food sources include poultry, fish, nuts, seeds, and grains. Histidine and histamine have a unique relationship. The amino acid histadine becomes histamine via a vitamin B6- dependent enzyme called histidine decarboxylase.
With this, decreased amounts of histidine and insufficient vitamin B6 can subsequently lead to a decrease in histamine concentration. This may impair digestion, since histamine binds to H2 receptors located on the surface of parietal cells to stimulate gastric acid secretion, necessary for protein breakdown.
Histidine also inhibits the production of proinflammatory cytokines by monocytes and is therefore anti-inflammatory and antioxidant.
With these beneficial effects, histidine supplementation has been shown to improve insulin resistance, reduce BMI, suppress inflammation, and lower oxidative stress in obese women with metabolic syndrome.
Interestingly, histadine can also be broken down to form urocanic acid in the liver and skin. Urocanic acid absorbs UV light and is thought to act as a natural sunscreen.
Optimal range: 102 - 763 micromol/g creatinine
Histidine is a semi-essential amino acid which is formed in the breakdown of carnosine. Red meat is a common source of carnosine, and therefore histadine. Other food sources include poultry, fish, nuts, seeds, and grains. Histidine and histamine have a unique relationship. The amino acid histadine becomes histamine via a vitamin B6- dependent enzyme called histidine decarboxylase.
Optimal range: 20 - 309 mmol/mol creatinine
Histidine is a semi-essential amino acid which is formed in the breakdown of carnosine. Red meat is a common source of carnosine, and therefore histadine.
Other food sources include poultry, fish, nuts, seeds, and grains. Histidine and histamine have a unique relationship. The amino acid histadine becomes histamine via a vitamin B6- dependent enzyme called histidine decarboxylase.
With this, decreased amounts of histidine and insufficient vitamin B6 can subsequently lead to a decrease in histamine concentration. This may impair digestion, since histamine binds to H2 receptors located on the surface of parietal cells to stimulate gastric acid secretion, necessary for protein breakdown.
Histidine also inhibits the production of proinflammatory cytokines by monocytes and is therefore anti-inflammatory and antioxidant.
With these beneficial effects, histidine supplementation has been shown to improve insulin resistance, reduce BMI, suppress inflammation, and lower oxidative stress in obese women with metabolic syndrome.
Interestingly, histadine can also be broken down to form urocanic acid in the liver and skin. Urocanic acid absorbs UV light and is thought to act as a natural sunscreen.
Optimal range: 106.9 - 1235.7 nmol/mg Creatinine
LEARN MOREOptimal range: 60 - 109 umol/L
Histidine is a semi-essential amino acid which is formed in the breakdown of carnosine. Red meat is a common source of carnosine, and therefore histadine. Other food sources include poultry, fish, nuts, seeds, and grains. Histidine and histamine have a unique relationship. The amino acid histadine becomes histamine via a vitamin B6- dependent enzyme called histidine decarboxylase.
Optimal range: 106.4 - 2534.2 umol/g Cr
Histidine is a semi-essential amino acid which is formed in the breakdown of carnosine. Red meat is a common source of carnosine, and therefore histadine.
Other food sources include poultry, fish, nuts, seeds, and grains. Histidine and histamine have a unique relationship. The amino acid histadine becomes histamine via a vitamin B6- dependent enzyme called histidine decarboxylase.
With this, decreased amounts of histidine and insufficient vitamin B6 can subsequently lead to a decrease in histamine concentration. This may impair digestion, since histamine binds to H2 receptors located on the surface of parietal cells to stimulate gastric acid secretion, necessary for protein breakdown.
Histidine also inhibits the production of proinflammatory cytokines by monocytes and is therefore anti-inflammatory and antioxidant.
With these beneficial effects, histidine supplementation has been shown to improve insulin resistance, reduce BMI, suppress inflammation, and lower oxidative stress in obese women with metabolic syndrome.
Interestingly, histadine can also be broken down to form urocanic acid in the liver and skin. Urocanic acid absorbs UV light and is thought to act as a natural sunscreen.
Optimal range: 6.5 - 13.3 qmol/dL
Histidine is a semi-essential amino acid which is formed in the breakdown of carnosine. Red meat is a common source of carnosine, and therefore histadine. Other food sources include poultry, fish, nuts, seeds, and grains. Histidine and histamine have a unique relationship. The amino acid histadine becomes histamine via a vitamin B6- dependent enzyme called histidine decarboxylase.
Optimal range: 61.2 - 104.7 nmol/ML
Histidine is involved in one-carbon units for conversion of formiminoglutamic acid (FIGLU) to glutamic acid.
- High plasma histidine has been associated with increased plasma glutamic acid, alanine and glutamine, and decreased branched-chain amino acids.
- Elevated urine histidine means it is not available for hemoglobin production. Hemoglobin is 10% histidine.
- High levels have been associated with progression of type 2 diabetes after gestational diabetes (= a type of diabetes that can develop during pregnancy in women who don't already have diabetes.)
- Decreased plasma histidine was associated with increased risk of ulcerative colitis relapse; a higher serum CRP in Crohn’s disease; chronic kidney disease; increased inflammation; and atopic dermatitis.
Optimal range: 57 - 114 µmol/L , 5.70 - 11.40 µmol/dL
Histidine is the amino acid most necessary during stress. Amino acids are the building blocks of protein in our bodies.
Optimal range: 124 - 894 micromol/g creatinine
Histidine is the amino acid most necessary during stress. Amino acids are the building blocks of protein in our bodies.
Histidine ameliorates fatigue, promotes clear thinking and concentration, reduces appetite, decreases anxiety, improves sleep and glucose homeostasis, and gives rise to histamine.
Optimal range: 0 - 96 units/ml
This test distinguishes drug-induced lupus from other lupus variants and autoimmune conditions. Though not a definitive diagnostic tool, histone antibodies align with drug-induced lupus. It's often ordered alongside a positive ANA test and sometimes an anti-dsDNA test. Following drug-induced lupus diagnosis, discontinuing the drug is advised, with histone antibody tests for monitoring. These tests are ordered when an individual taking medication for weeks to years exhibits symptoms linked to drug-induced lupus, especially without prior autoimmune history. Symptoms include joint pain, fatigue, fever, myalgia, malar rash, sunlight sensitivity, and weight loss. CNS and kidney symptoms are rarer in drug-induced lupus compared to systemic lupus erythematosus (SLE). Post-drug discontinuation, the histone antibody test can track changes. A negative result suggests alternatives, yet drug-induced lupus is possible without histone antibodies.
Optimal range: 0 - 0.5 ng/mL
Histoplasma complement fixation is a blood test that checks for infection from a fungus called Histoplasma capsulatum (H capsulatum), which causes the disease histoplasmosis.
Reference range: Non Reactive, Reactive
AIDS is caused by 2 known types of HIV. HIV type 1 (HIV-1) is found in patients with AIDS or AIDS-related complex and in asymptomatic infected individuals at high risk for AIDS. The virus is transmitted by sexual contact, by exposure to infected blood or blood products, or from an infected mother to her fetus or infant. HIV type 2 (HIV-2) infection is endemic only in West Africa, and it has been identified in individuals who had sexual relations with individuals from that geographic region. HIV-2 is similar to HIV-1 in viral morphology, overall genomic structure, and its ability to cause AIDS.
Reference range: NEGATIVE, POSITIVE
AIDS is caused by 2 known types of HIV. HIV type 1 (HIV-1) is found in patients with AIDS or AIDS-related complex and in asymptomatic infected individuals at high risk for AIDS. The virus is transmitted by sexual contact, by exposure to infected blood or blood products, or from an infected mother to her fetus or infant. HIV type 2 (HIV-2) infection is endemic only in West Africa, and it has been identified in individuals who had sexual relations with individuals from that geographic region. HIV-2 is similar to HIV-1 in viral morphology, overall genomic structure, and its ability to cause AIDS.
Reference range: Non-Reactive, Reactive
Human Immunodeficiency Virus (HIV) is categorized into two distinct types: HIV-1 and HIV-2. Both are retroviruses that attack the body's immune system, but they have differences in their geographical prevalence, transmission rates, and progression to Acquired Immunodeficiency Syndrome (AIDS).
HIV-1: This is the most common type of HIV and is found worldwide. It's responsible for the vast majority of HIV infections globally. HIV-1 is characterized by its rapid transmission and progression. It is more aggressive and infects cells faster than HIV-2, leading to a quicker decline in immune function if left untreated. HIV-1 is divided into four groups: M (Main), O (Outlier), N (Non-M, Non-O), and P, with Group M responsible for the majority of infections worldwide. Further, Group M is divided into multiple subtypes and circulating recombinant forms (CRFs).
HIV-2: This type is less common and is predominantly found in West Africa, with some cases in India and Europe. Compared to HIV-1, HIV-2 is transmitted less efficiently, particularly from mother to child and through heterosexual contact. The progression of HIV-2 to AIDS is generally slower, and it may have a longer asymptomatic stage. HIV-2 is also less responsive to certain antiretroviral therapies, requiring specific treatment regimens.
Reference range: Non Reactive, Reactive
AIDS is caused by 2 known types of HIV. HIV type 1 (HIV-1) is found in patients with AIDS or AIDS-related complex and in asymptomatic infected individuals at high risk for AIDS. The virus is transmitted by sexual contact, by exposure to infected blood or blood products, or from an infected mother to her fetus or infant. HIV type 2 (HIV-2) infection is endemic only in West Africa, and it has been identified in individuals who had sexual relations with individuals from that geographic region. HIV-2 is similar to HIV-1 in viral morphology, overall genomic structure, and its ability to cause AIDS.
Reference range: NEGATIVE, POSITIVE
AIDS is caused by 2 known types of HIV. HIV type 1 (HIV-1) is found in patients with AIDS or AIDS-related complex and in asymptomatic infected individuals at high risk for AIDS. The virus is transmitted by sexual contact, by exposure to infected blood or blood products, or from an infected mother to her fetus or infant. HIV type 2 (HIV-2) infection is endemic only in West Africa, and it has been identified in individuals who had sexual relations with individuals from that geographic region. HIV-2 is similar to HIV-1 in viral morphology, overall genomic structure, and its ability to cause AIDS.