Druvith/medqa huggingface dataset:
What are the genetic changes related to atopic dermatitis ? 

The genetics of atopic dermatitis are not completely understood. Studies suggest that several genes can be involved in development of the condition. The strongest association is with the FLG gene, which is mutated in 20 to 30 percent of people with atopic dermatitis compared with 8 to 10 percent of the general population without atopic dermatitis.  The FLG gene provides instructions for making a protein called profilaggrin, which is cut (cleaved) to produce multiple copies of the filaggrin protein. Filaggrin is involved in creating the structure of the outermost layer of skin, creating a strong barrier to keep in water and keep out foreign substances, including toxins, bacteria, and substances that can cause allergic reactions (allergens), such as pollen and dust. Further processing of the filaggrin protein produces other molecules that are part of the skin's "natural moisturizing factor," which helps maintain hydration of the outermost layer of skin.  Mutations in the FLG gene lead to production of an abnormally short profilaggrin molecule that cannot be cleaved to produce filaggrin proteins. The resulting shortage of filaggrin can impair the barrier function of the skin. In addition, a lack of natural moisturizing factor allows excess water loss through the skin, which can lead to dry skin.  Research shows that impairment of the skin's barrier function contributes to development of allergic disorders. An allergic reaction occurs when the body mistakenly recognizes a harmless substance, such as pollen, as a danger and stimulates an immune response to it. Research suggests that without a properly functioning barrier, allergens are able to get into the body through the skin. For unknown reasons, in susceptible individuals the body reacts as if the allergen is harmful and produces immune proteins called IgE antibodies specific to the allergen. Upon later encounters with the allergen, IgE antibodies recognize it, which stimulates an immune response, causing the symptoms of allergies, such as itchy, watery eyes or breathing difficulty. Although atopic dermatitis is not initially caused by an allergic reaction, flare-ups of the rashes can be triggered by allergens. The impaired barrier function caused by FLG gene mutations also contributes to the increased risk of asthma and other allergic disorders in people with atopic dermatitis.  Mutations in many other genes, most of which have not been identified, are likely associated with development of atopic dermatitis. Researchers suspect these genes are involved in the skin's barrier function or in the function of the immune system. However, not everyone with a mutation in FLG or another associated gene develops atopic dermatitis; exposure to certain environmental factors also contributes to the development of the disorder. Studies suggest that these exposures trigger epigenetic changes to the DNA. Epigenetic changes modify DNA without changing the DNA sequence. They can affect gene activity and regulate the production of proteins, which may influence the development of allergies in susceptible individuals.
Is atopic dermatitis inherited ? 

Allergic disorders tend to run in families; having a parent with atopic dermatitis, asthma, or hay fever raises the chances a person will develop atopic dermatitis. When associated with FLG gene mutations, atopic dermatitis follows an autosomal dominant inheritance pattern, which means one copy of the altered FLG gene in each cell is sufficient to increase the risk of the disorder. Individuals with two altered copies of the gene are more likely to develop the disorder and can have more severe signs and symptoms than individuals with a single altered copy. When associated with other genetic factors, the inheritance pattern is unclear.  People with changes in one of the genes associated with atopic dermatitis, including FLG, inherit an increased risk of this condition, not the condition itself. Not all people with this condition have a mutation in an associated gene, and not all people with a variation in an associated gene will develop the disorder.
What are the treatments for atopic dermatitis ? 

These resources address the diagnosis or management of atopic dermatitis:  - American Academy of Dermatology: Atopic Dermatitis: Tips for Managing   These resources from MedlinePlus offer information about the diagnosis and management of various health conditions:  - Diagnostic Tests  - Drug Therapy  - Surgery and Rehabilitation  - Genetic Counseling   - Palliative Care
What is (are) renal hypouricemia ? 

Renal hypouricemia is a kidney (renal) disorder that results in a reduced amount of uric acid in the blood. Uric acid is a byproduct of certain normal chemical reactions in the body. In the bloodstream it acts as an antioxidant, protecting cells from the damaging effects of unstable molecules called free radicals. However, having too much uric acid in the body is toxic, so excess uric acid is removed from the body in urine.  People with renal hypouricemia have little to no uric acid in their blood; they release an excessive amount of it in the urine. In many affected individuals, renal hypouricemia causes no signs or symptoms. However, some people with this condition develop kidney problems. After strenuous exercise, they can develop exercise-induced acute kidney injury, which causes pain in their sides and lower back as well as nausea and vomiting that can last several hours.  Because an excessive amount of uric acid passes through the kidneys to be excreted in urine in people with renal hypouricemia, they have an increased risk of developing kidney stones (nephrolithiasis) formed from uric acid crystals. These uric acid stones can damage the kidneys and lead to episodes of blood in the urine (hematuria). Rarely, people with renal hypouricemia develop life-threatening kidney failure.
How many people are affected by renal hypouricemia ? 

The prevalence of renal hypouricemia is unknown; at least 150 affected individuals have been described in the scientific literature. This condition is thought to be most prevalent in Asian countries such as Japan and South Korea, although affected individuals have been found in Europe. Renal hypouricemia is likely underdiagnosed because it does not cause any symptoms in many affected individuals.
What are the genetic changes related to renal hypouricemia ? 

Mutations in the SLC22A12 or SLC2A9 gene cause renal hypouricemia. These genes provide instructions for making proteins called urate transporter 1 (URAT1) and glucose transporter 9 (GLUT9), respectively. These proteins are found in the kidneys, specifically in structures called proximal tubules. These structures help to reabsorb needed nutrients, water, and other materials into the blood and excrete unneeded substances into the urine. Within the proximal tubules, both the URAT1 and GLUT9 proteins reabsorb uric acid into the bloodstream or release it into the urine, depending on the body's needs. Most uric acid that is filtered through the kidneys is reabsorbed into the bloodstream; about 10 percent is released into urine.  Mutations that cause renal hypouricemia lead to the production of URAT1 or GLUT9 protein with a reduced ability to reabsorb uric acid into the bloodstream. Instead, large amounts of uric acid are released in the urine. The specific cause of the signs and symptoms of renal hypouricemia is unclear. Researchers suspect that when additional uric acid is produced during exercise and passed through the kidneys, it could lead to tissue damage. Alternatively, without the antioxidant properties of uric acid, free radicals could cause tissue damage in the kidneys. Another possibility is that other substances are prevented from being reabsorbed along with uric acid; accumulation of these substances in the kidneys could cause tissue damage. It is likely that individuals with renal hypouricemia who have mild or no symptoms have enough protein function to reabsorb a sufficient amount of uric acid into the bloodstream to prevent severe kidney problems.
Is renal hypouricemia inherited ? 

This condition is typically inherited in an autosomal recessive pattern, which means both copies of the SLC22A12 or SLC2A9 gene in each cell have mutations. The parents of an individual with an autosomal recessive condition each carry one copy of the mutated gene, but they usually do not show signs and symptoms of the condition.  Sometimes, individuals with one SLC2A9 gene mutation in each cell have reduced levels of uric acid. The levels usually are not as low as they are in people who have mutations in both copies of the gene, and they often do not cause any signs or symptoms. Rarely, people who carry one copy of the mutated gene will develop uric acid kidney stones.
What are the treatments for renal hypouricemia ? 

These resources address the diagnosis or management of renal hypouricemia:  - Genetic Testing Registry: Familial renal hypouricemia  - Genetic Testing Registry: Renal hypouricemia 2  - KidsHealth from Nemours: Blood Test: Uric Acid  - MedlinePlus Encyclopedia: Uric Acid--Blood   These resources from MedlinePlus offer information about the diagnosis and management of various health conditions:  - Diagnostic Tests  - Drug Therapy  - Surgery and Rehabilitation  - Genetic Counseling   - Palliative Care
What is (are) 3-hydroxy-3-methylglutaryl-CoA lyase deficiency ? 

3-hydroxy-3-methylglutaryl-CoA lyase deficiency (also known as HMG-CoA lyase deficiency) is an uncommon inherited disorder in which the body cannot process a particular protein building block (amino acid) called leucine. Additionally, the disorder prevents the body from making ketones, which are used for energy during periods without food (fasting).  The signs and symptoms of HMG-CoA lyase deficiency usually appear within the first year of life. The condition causes episodes of vomiting, diarrhea, dehydration, extreme tiredness (lethargy), and weak muscle tone (hypotonia). During an episode, blood sugar levels can become dangerously low (hypoglycemia), and a buildup of harmful compounds can cause the blood to become too acidic (metabolic acidosis). If untreated, the disorder can lead to breathing problems, convulsions, coma, and death. Episodes are often triggered by an infection, fasting, strenuous exercise, or other types of stress.  HMG-CoA lyase deficiency is sometimes mistaken for Reye syndrome, a severe disorder that develops in children while they appear to be recovering from viral infections such as chicken pox or flu. Most cases of Reye syndrome are associated with the use of aspirin during these viral infections.
How many people are affected by 3-hydroxy-3-methylglutaryl-CoA lyase deficiency ? 

HMG-CoA lyase deficiency is a rare condition; it has been reported in fewer than 100 individuals worldwide. Most people diagnosed with this disorder have been from Saudi Arabia, Portugal, or Spain.
What are the genetic changes related to 3-hydroxy-3-methylglutaryl-CoA lyase deficiency ? 

Mutations in the HMGCL gene cause HMG-CoA lyase deficiency. The HMGCL gene provides instructions for making an enzyme known as 3-hydroxymethyl-3-methylglutaryl-coenzyme A lyase (HMG-CoA lyase). This enzyme plays a critical role in breaking down dietary proteins and fats for energy. Specifically, it is responsible for processing leucine, an amino acid that is part of many proteins. HMG-CoA lyase also produces ketones during the breakdown of fats. Ketones are compounds that certain organs and tissues, particularly the brain, use for energy when the simple sugar glucose is not available. For example, ketones are important sources of energy during periods of fasting.  If a mutation in the HMGCL gene reduces or eliminates the activity of HMG-CoA lyase, the body is unable to process leucine or make ketones properly. When leucine is not processed normally, a buildup of chemical byproducts called organic acids can result in metabolic acidosis. A shortage of ketones often leads to hypoglycemia. Metabolic acidosis and hypoglycemia can damage cells, particularly in the brain, resulting in serious illness in children with HMG-CoA lyase deficiency.
Is 3-hydroxy-3-methylglutaryl-CoA lyase deficiency inherited ? 

This condition is inherited in an autosomal recessive pattern, which means both copies of the gene in each cell have mutations. The parents of an individual with an autosomal recessive condition each carry one copy of the mutated gene, but they typically do not show signs and symptoms of the condition.
What are the treatments for 3-hydroxy-3-methylglutaryl-CoA lyase deficiency ? 

These resources address the diagnosis or management of HMG-CoA lyase deficiency:  - Baby's First Test  - Genetic Testing Registry: Deficiency of hydroxymethylglutaryl-CoA lyase   These resources from MedlinePlus offer information about the diagnosis and management of various health conditions:  - Diagnostic Tests  - Drug Therapy  - Surgery and Rehabilitation  - Genetic Counseling   - Palliative Care
What is (are) Poland syndrome ? 

Poland syndrome is a disorder in which affected individuals are born with missing or underdeveloped muscles on one side of the body, resulting in abnormalities that can affect the chest, shoulder, arm, and hand. The extent and severity of the abnormalities vary among affected individuals.  People with Poland syndrome are typically missing part of one of the major chest muscles, called the pectoralis major. In most affected individuals, the missing part is the large section of the muscle that normally runs from the upper arm to the breastbone (sternum). The abnormal pectoralis major muscle may cause the chest to appear concave. In some cases, additional muscles on the affected side of the torso, including muscles in the chest wall, side, and shoulder, may be missing or underdeveloped. There may also be rib cage abnormalities, such as shortened ribs, and the ribs may be noticeable due to less fat under the skin (subcutaneous fat). Breast and nipple abnormalities may also occur, and underarm (axillary) hair is sometimes sparse or abnormally placed. In most cases, the abnormalities in the chest area do not cause health problems or affect movement.  Many people with Poland syndrome have hand abnormalities on the affected side, commonly including an underdeveloped hand with abnormally short fingers (brachydactyly); small, underdeveloped (vestigial) fingers; and some fingers that are fused together (syndactyly). This combination of hand abnormalities is called symbrachydactyly. Some affected individuals have only one or two of these features, or have a mild hand abnormality that is hardly noticeable; more severe abnormalities can cause problems with use of the hand. The bones of the forearm (radius and ulna) are shortened in some people with Poland syndrome, but this shortening may also be difficult to detect unless measured.  Mild cases of Poland syndrome without hand involvement may not be evident until puberty, when the differences (asymmetry) between the two sides of the chest become more apparent. By contrast, severely affected individuals have abnormalities of the chest, hand, or both that are apparent at birth. In rare cases, severely affected individuals have abnormalities of internal organs such as a lung or a kidney, or the heart is abnormally located in the right side of the chest (dextrocardia).  Rarely, chest and hand abnormalities resembling those of Poland syndrome occur on both sides of the body, but researchers disagree as to whether this condition is a variant of Poland syndrome or a different disorder.
How many people are affected by Poland syndrome ? 

Poland syndrome has been estimated to occur in 1 in 20,000 newborns. For unknown reasons, this disorder occurs more than twice as often in males than in females. Poland syndrome may be underdiagnosed because mild cases without hand involvement may never come to medical attention.
What are the genetic changes related to Poland syndrome ? 

The cause of Poland syndrome is unknown. Researchers have suggested that it may result from a disruption of blood flow during development before birth. This disruption is thought to occur at about the sixth week of embryonic development and affect blood vessels that will become the subclavian and vertebral arteries on each side of the body. The arteries normally supply blood to embryonic tissues that give rise to the chest wall and hand on their respective sides. Variations in the site and extent of the disruption may explain the range of signs and symptoms that occur in Poland syndrome. Abnormality of an embryonic structure called the apical ectodermal ridge, which helps direct early limb development, may also be involved in this disorder.  Rare cases of Poland syndrome are thought to be caused by a genetic change that can be passed down in families, but no related genes have been identified.
Is Poland syndrome inherited ? 

Most cases of Poland syndrome are sporadic, which means they are not inherited and occur in people with no history of the disorder in their families. Rarely, this condition is passed through generations in families. In these families the condition appears to be inherited in an autosomal dominant pattern, which means one copy of an altered gene in each cell is sufficient to cause the disorder, although no associated genes have been found.
What are the treatments for Poland syndrome ? 

These resources address the diagnosis or management of Poland syndrome:  - Children's Medical Center of Dallas  - Great Ormond Street Hospital (UK): Treatment Options for Symbrachydactyly  - St. Louis Children's Hospital: Chest Wall Deformities   These resources from MedlinePlus offer information about the diagnosis and management of various health conditions:  - Diagnostic Tests  - Drug Therapy  - Surgery and Rehabilitation  - Genetic Counseling   - Palliative Care
What is (are) myopathy with deficiency of iron-sulfur cluster assembly enzyme ? 

Myopathy with deficiency of iron-sulfur cluster assembly enzyme is an inherited disorder that primarily affects muscles used for movement (skeletal muscles). This condition does not usually affect other types of muscle, such as the heart (cardiac) muscle.  From early childhood, affected individuals experience extreme fatigue in response to physical activity (exercise intolerance). Mild exertion results in a rapid heartbeat (tachycardia), shortness of breath, and muscle weakness and pain. However, people with this condition typically have normal muscle strength when they are at rest.  Prolonged or recurrent physical activity causes more severe signs and symptoms, including a breakdown of muscle tissue (rhabdomyolysis). The destruction of muscle tissue releases a protein called myoglobin, which is processed by the kidneys and released in the urine (myoglobinuria). Myoglobin causes the urine to be red or brown. This protein can also damage the kidneys, in some cases leading to life-threatening kidney failure.  In most affected individuals, the muscle problems associated with this condition do not worsen with time. However, at least two people with a severe variant of this disorder have experienced progressive muscle weakness and wasting starting in childhood.
How many people are affected by myopathy with deficiency of iron-sulfur cluster assembly enzyme ? 

This condition has been reported in several families of northern Swedish ancestry.
What are the genetic changes related to myopathy with deficiency of iron-sulfur cluster assembly enzyme ? 

Myopathy with deficiency of iron-sulfur cluster assembly enzyme is caused by mutations in the ISCU gene. This gene provides instructions for making a protein called the iron-sulfur cluster assembly enzyme. As its name suggests, this enzyme is involved in the formation of clusters of iron and sulfur atoms (Fe-S clusters). These clusters are critical for the function of many different proteins, including those needed for DNA repair and the regulation of iron levels. Proteins containing Fe-S clusters are also necessary for energy production within mitochondria, which are the cell structures that convert the energy from food into a form that cells can use.  Mutations in the ISCU gene severely limit the amount of iron-sulfur cluster assembly enzyme that is made in cells. A shortage of this enzyme prevents the normal production of proteins that contain Fe-S clusters, which disrupts a variety of cellular activities. A reduction in the amount of iron-sulfur cluster assembly enzyme is particularly damaging to skeletal muscle cells. Within the mitochondria of these cells, a lack of this enzyme causes problems with energy production and an overload of iron. These defects lead to exercise intolerance and the other features of myopathy with deficiency of iron-sulfur cluster assembly enzyme.
Is myopathy with deficiency of iron-sulfur cluster assembly enzyme inherited ? 

This condition is inherited in an autosomal recessive pattern, which means both copies of the gene in each cell have mutations. The parents of an individual with an autosomal recessive condition each carry one copy of the mutated gene, but they typically do not show signs and symptoms of the condition.
What are the treatments for myopathy with deficiency of iron-sulfur cluster assembly enzyme ? 

These resources address the diagnosis or management of myopathy with deficiency of iron-sulfur cluster assembly enzyme:  - Gene Review: Gene Review: Myopathy with Deficiency of ISCU  - Genetic Testing Registry: Myopathy with lactic acidosis, hereditary  - MedlinePlus Encyclopedia: Rhabdomyolysis   These resources from MedlinePlus offer information about the diagnosis and management of various health conditions:  - Diagnostic Tests  - Drug Therapy  - Surgery and Rehabilitation  - Genetic Counseling   - Palliative Care