Druvith/medqa huggingface dataset:
What are the genetic changes related to Bartter syndrome ? 

Bartter syndrome can be caused by mutations in at least five genes. Mutations in the SLC12A1 gene cause type I. Type II results from mutations in the KCNJ1 gene. Mutations in the CLCNKB gene are responsible for type III. Type IV can result from mutations in the BSND gene or from a combination of mutations in the CLCNKA and CLCNKB genes.  The genes associated with Bartter syndrome play important roles in normal kidney function. The proteins produced from these genes are involved in the kidneys' reabsorption of salt. Mutations in any of the five genes impair the kidneys' ability to reabsorb salt, leading to the loss of excess salt in the urine (salt wasting). Abnormalities of salt transport also affect the reabsorption of other charged atoms (ions), including potassium and calcium. The resulting imbalance of ions in the body leads to the major features of Bartter syndrome.  In some people with Bartter syndrome, the genetic cause of the disorder is unknown. Researchers are searching for additional genes that may be associated with this condition.
Is Bartter syndrome 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 Bartter syndrome ? 

These resources address the diagnosis or management of Bartter syndrome:  - Genetic Testing Registry: Bartter syndrome antenatal type 1  - Genetic Testing Registry: Bartter syndrome antenatal type 2  - Genetic Testing Registry: Bartter syndrome type 3  - Genetic Testing Registry: Bartter syndrome type 4  - Genetic Testing Registry: Bartter syndrome, type 4b  - Genetic Testing Registry: Bartter's syndrome   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) congenital plasminogen deficiency ? 

Congenital plasminogen deficiency is a disorder that results in inflamed growths on the mucous membranes, which are the moist tissues that line body openings such as the eyelids and the inside of the mouth. Development of the growths are usually triggered by infections or injury, but they may also occur spontaneously in the absence of known triggers. The growths may recur after being removed.  Congenital plasminogen deficiency most often affects the conjunctiva, which are the mucous membranes that protect the white part of the eye (the sclera) and line the eyelids. A characteristic feature of this disorder is ligneous conjunctivitis, in which a buildup of a protein called fibrin causes inflammation of the conjunctiva (conjunctivitis) and leads to thick, woody (ligneous), inflamed growths that are yellow, white, or red. Ligneous conjunctivitis most often occurs on the inside of the eyelids. However, in about one-third of cases, ligneous conjunctivitis over the sclera grows onto the cornea, which is the clear covering that protects the colored part of the eye (the iris) and pupil. Such growths can tear the cornea or cause scarring. These corneal problems as well as obstruction by growths inside the eyelid can lead to vision loss.  People with congenital plasminogen deficiency may also develop ligneous growths on other mucous membranes, including the inside of the mouth and the gums; the lining of the nasal cavity; and in females, the vagina. Growths on the mucous membranes that line the gastrointestinal tract may result in ulcers. The growths may also develop in the windpipe, which can cause life-threatening airway obstruction, especially in children. In a small number of cases, affected individuals are born with impaired drainage of the fluid that surrounds and protects the brain and spinal cord (the cerebrospinal fluid or CSF), resulting in a buildup of this fluid in the skull (occlusive hydrocephalus). It is unclear how this feature is related to the other signs and symptoms of congenital plasminogen deficiency.
How many people are affected by congenital plasminogen deficiency ? 

The prevalence of congenital plasminogen deficiency has been estimated at 1.6 per one million people. This condition is believed to be underdiagnosed, because growths in one area are often not recognized as being a feature of a disorder that affects many body systems. Mild cases likely never come to medical attention.
What are the genetic changes related to congenital plasminogen deficiency ? 

Congenital plasminogen deficiency is caused by mutations in the PLG gene. This gene provides instructions for making a protein called plasminogen. Enzymes called plasminogen activators convert plasminogen into the protein plasmin, which breaks down another protein called fibrin. Fibrin is the main protein involved in blood clots and is important for wound healing, creating the framework for normal tissue to grow back. Excess fibrin is broken down when no longer needed, and the new, more flexible normal tissue takes its place.  PLG gene mutations can decrease the amount of plasminogen that is produced, its function, or both. When the mutations affect plasminogen levels as well as the activity of the protein, affected individuals may be said to have type I congenital plasminogen deficiency, characterized by the ligneous growths previously described. People with mutations that result in normal levels of plasminogen with reduced activity are said to have type II congenital plasminogen deficiency or dysplasminogenemia. This form of the condition often has no symptoms.  A reduction in functional plasminogen results in less plasmin to break down fibrin, leading to a buildup of fibrin. The excess fibrin and the resulting inflammation of the tissue result in the inflamed woody growths characteristic of congenital plasminogen deficiency.  It is unclear why the excess fibrin builds up in the mucous membranes but does not usually result in abnormal clots in the blood vessels (thromboses). Researchers suggest that other enzymes in the blood may also break down fibrin, helping to compensate for the reduced plasminogen levels.
Is congenital plasminogen 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 congenital plasminogen deficiency ? 

These resources address the diagnosis or management of congenital plasminogen deficiency:  - Genetic Testing Registry: Plasminogen deficiency, type I  - Indiana Hemophilia and Thrombosis Center  - Plasminogen Deficiency Registry   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) intrahepatic cholestasis of pregnancy ? 

Intrahepatic cholestasis of pregnancy is a liver disorder that occurs in pregnant women. Cholestasis is a condition that impairs the release of a digestive fluid called bile from liver cells. As a result, bile builds up in the liver, impairing liver function. Because the problems with bile release occur within the liver (intrahepatic), the condition is described as intrahepatic cholestasis. Intrahepatic cholestasis of pregnancy usually becomes apparent in the third trimester of pregnancy. Bile flow returns to normal after delivery of the baby, and the signs and symptoms of the condition disappear. However, they can return during later pregnancies.  This condition causes severe itchiness (pruritus) in the expectant mother. The itchiness usually begins on the palms of the hands and the soles of the feet and then spreads to other parts of the body. Occasionally, affected women have yellowing of the skin and whites of the eyes (jaundice). Some studies have shown that women with intrahepatic cholestasis of pregnancy are more likely to develop gallstones sometime in their life than women who do not have the condition.  Intrahepatic cholestasis of pregnancy can cause problems for the unborn baby. This condition is associated with an increased risk of premature delivery and stillbirth. Additionally, some infants born to mothers with intrahepatic cholestasis of pregnancy have a slow heart rate and a lack of oxygen during delivery (fetal distress).
How many people are affected by intrahepatic cholestasis of pregnancy ? 

Intrahepatic cholestasis of pregnancy is estimated to affect 1 percent of women of Northern European ancestry. The condition is more common in certain populations, such as women of Araucanian Indian ancestry in Chile or women of Scandinavian ancestry. This condition is found less frequently in other populations.
What are the genetic changes related to intrahepatic cholestasis of pregnancy ? 

Genetic changes in the ABCB11 or the ABCB4 gene can increase a woman's likelihood of developing intrahepatic cholestasis of pregnancy.  The ABCB11 gene provides instructions for making a protein called the bile salt export pump (BSEP). This protein is found in the liver, and its main role is to move bile salts (a component of bile) out of liver cells, which is important for the normal release of bile. Changes in the ABCB11 gene associated with intrahepatic cholestasis of pregnancy reduce the amount or function of the BSEP protein, although enough function remains for sufficient bile secretion under most circumstances. Studies show that the hormones estrogen and progesterone (and products formed during their breakdown), which are elevated during pregnancy, further reduce the function of BSEP, resulting in impaired bile secretion and the features of intrahepatic cholestasis of pregnancy.  The ABCB4 gene provides instructions for making a protein that helps move certain fats called phospholipids across cell membranes and release them into bile. Phospholipids attach (bind) to bile acids (another component of bile). Large amounts of bile acids can be toxic when they are not bound to phospholipids. A mutation in one copy of the ABCB4 gene mildly reduces the production of ABCB4 protein. Under most circumstances, though, enough protein is available to move an adequate amount of phospholipids out of liver cells to bind to bile acids. Although the mechanism is unclear, the function of the remaining ABCB4 protein appears to be impaired during pregnancy, which may further reduce the movement of phospholipids into bile. The lack of phospholipids available to bind to bile acids leads to a buildup of toxic bile acids that can impair liver function, including the regulation of bile flow.  Most women with intrahepatic cholestasis of pregnancy do not have a genetic change in the ABCB11 or ABCB4 gene. Other genetic and environmental factors likely play a role in increasing susceptibility to this condition.
Is intrahepatic cholestasis of pregnancy inherited ? 

Susceptibility to intrahepatic cholestasis of pregnancy is inherited in an autosomal dominant pattern, which means one copy of the altered gene in each cell is sufficient to increase the risk of developing the disorder. Some women with an altered gene do not develop intrahepatic cholestasis of pregnancy. Many other factors likely contribute to the risk of developing this complex disorder.
What are the treatments for intrahepatic cholestasis of pregnancy ? 

These resources address the diagnosis or management of intrahepatic cholestasis of pregnancy:  - Gene Review: Gene Review: ATP8B1 Deficiency  - Genetic Testing Registry: Cholestasis of pregnancy   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) methemoglobinemia, beta-globin type ? 

Methemoglobinemia, beta-globin type is a condition that affects the function of red blood cells. Specifically, it alters a molecule called hemoglobin within these cells. Hemoglobin within red blood cells attaches (binds) to oxygen molecules in the lungs, which it carries through the bloodstream, then releases in tissues throughout the body. Instead of normal hemoglobin, people with methemoglobinemia, beta-globin type have an abnormal form called methemoglobin, which is unable to efficiently deliver oxygen to the body's tissues. In methemoglobinemia, beta-globin type, the abnormal hemoglobin gives the blood a brown color. It also causes a bluish appearance of the skin, lips, and nails (cyanosis), which usually first appears around the age of 6 months. The signs and symptoms of methemoglobinemia, beta-globin type are generally limited to cyanosis, which does not cause any health problems. However, in rare cases, severe methemoglobinemia, beta-globin type can cause headaches, weakness, and fatigue.
How many people are affected by methemoglobinemia, beta-globin type ? 

The incidence of methemoglobinemia, beta-globin type is unknown.
What are the genetic changes related to methemoglobinemia, beta-globin type ? 

Methemoglobinemia, beta-globin type is caused by mutations in the HBB gene. This gene provides instructions for making a protein called beta-globin. Beta-globin is one of four components (subunits) that make up hemoglobin. In adults, hemoglobin normally contains two subunits of beta-globin and two subunits of another protein called alpha-globin. Each of these protein subunits is bound to an iron-containing molecule called heme; each heme contains an iron molecule in its center that can bind to one oxygen molecule. For hemoglobin to bind to oxygen, the iron within the heme molecule needs to be in a form called ferrous iron (Fe2+). The iron within the heme can change to another form of iron called ferric iron (Fe3+), which cannot bind oxygen. Hemoglobin that contains ferric iron is known as methemoglobin.  HBB gene mutations that cause methemoglobinemia, beta-globin type change the structure of beta-globin and promote the heme iron to change from ferrous to ferric. The ferric iron cannot bind oxygen and causes cyanosis and the brown appearance of blood.
Is methemoglobinemia, beta-globin type inherited ? 

This condition is inherited in an autosomal dominant pattern, which means one copy of the altered gene in each cell is sufficient to cause the disorder.
What are the treatments for methemoglobinemia, beta-globin type ? 

These resources address the diagnosis or management of methemoglobinemia, beta-globin type:  - Genetic Testing Registry: Methemoglobinemia, beta-globin type  - KidsHealth from Nemours: Blood Test: Hemoglobin  - MedlinePlus Encyclopedia: Hemoglobin  - MedlinePlus Encyclopedia: Methemoglobinemia  - MedlinePlus Encyclopedia: Skin Discoloration--Bluish   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) glucose-galactose malabsorption ? 

Glucose-galactose malabsorption is a condition in which the cells lining the intestine cannot take in the sugars glucose and galactose, which prevents proper digestion of these molecules and larger molecules made from them.  Glucose and galactose are called simple sugars, or monosaccharides. Sucrose (table sugar) and lactose (the sugar found in milk) are called disaccharides because they are made from two simple sugars, and are broken down into these simple sugars during digestion. Sucrose is broken down into glucose and another simple sugar called fructose, and lactose is broken down into glucose and galactose. As a result, lactose, sucrose and other compounds made from sugar molecules (carbohydrates) cannot be digested by individuals with glucose-galactose malabsorption.  Glucose-galactose malabsorption generally becomes apparent in the first few weeks of a baby's life. Affected infants experience severe diarrhea resulting in life-threatening dehydration, increased acidity of the blood and tissues (acidosis), and weight loss when fed breast milk or regular infant formulas. However, they are able to digest fructose-based formulas that do not contain glucose or galactose. Some affected children are better able to tolerate glucose and galactose as they get older.  Small amounts of glucose in the urine (mild glucosuria) may occur intermittently in this disorder. Affected individuals may also develop kidney stones or more widespread deposits of calcium within the kidneys.
How many people are affected by glucose-galactose malabsorption ? 

Glucose-galactose malabsorption is a rare disorder; only a few hundred cases have been identified worldwide. However, as many as 10 percent of the population may have a somewhat reduced capacity for glucose absorption without associated health problems. This condition may be a milder variation of glucose-galactose malabsorption.
What are the genetic changes related to glucose-galactose malabsorption ? 

Mutations in the SLC5A1 gene cause glucose-galactose malabsorption.  The SLC5A1 gene provides instructions for producing a sodium/glucose cotransporter protein called SGLT1. This protein is found mainly in the intestinal tract and, to a lesser extent, in the kidneys, where it is involved in transporting glucose and the structurally similar galactose across cell membranes.  The sodium/glucose cotransporter protein is important in the functioning of intestinal epithelial cells, which are cells that line the walls of the intestine. These cells have fingerlike projections called microvilli that absorb nutrients from food as it passes through the intestine. Based on their appearance, groups of these microvilli are known collectively as the brush border. The sodium/glucose cotransporter protein is involved in the process of using energy to move glucose and galactose across the brush border membrane for absorption, a mechanism called active transport. Sodium and water are transported across the brush border along with the sugars in this process.  Mutations that prevent the sodium/glucose cotransporter protein from performing this function result in a buildup of glucose and galactose in the intestinal tract. This failure of active transport prevents the glucose and galactose from being absorbed and providing nourishment to the body. In addition, the water that normally would have been transported across the brush border with the sugar instead remains in the intestinal tract to be expelled with the stool, resulting in dehydration of the body's tissues and severe diarrhea.
Is glucose-galactose malabsorption inherited ? 

This condition is inherited in an autosomal recessive pattern, which means both copies of the gene in each cell have mutations. Most often, the parents of an individual with an autosomal recessive condition each carry one copy of the mutated gene, but do not show signs and symptoms of the condition. In some cases, individuals with one altered gene have reduced levels of glucose absorption capacity as measured in laboratory tests, but this has not generally been shown to have significant health effects.
What are the treatments for glucose-galactose malabsorption ? 

These resources address the diagnosis or management of glucose-galactose malabsorption:  - Genetic Testing Registry: Congenital glucose-galactose malabsorption   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) fibronectin glomerulopathy ? 

Fibronectin glomerulopathy is a kidney disease that usually develops between early and mid-adulthood but can occur at any age. It eventually leads to irreversible kidney failure (end-stage renal disease).  Individuals with fibronectin glomerulopathy usually have blood and excess protein in their urine (hematuria and proteinuria, respectively). They also have high blood pressure (hypertension). Some affected individuals develop renal tubular acidosis, which occurs when the kidneys are unable to remove enough acid from the body and the blood becomes too acidic.  The kidneys of people with fibronectin glomerulopathy have large deposits of the protein fibronectin-1 in structures called glomeruli. These structures are clusters of tiny blood vessels in the kidneys that filter waste products from blood. The waste products are then released in urine. The fibronectin-1 deposits impair the glomeruli's filtration ability.  Fifteen to 20 years following the appearance of signs and symptoms, individuals with fibronectin glomerulopathy often develop end-stage renal disease. Affected individuals may receive treatment in the form of a kidney transplant; in some cases, fibronectin glomerulopathy comes back (recurs) following transplantation.
How many people are affected by fibronectin glomerulopathy ? 

Fibronectin glomerulopathy is likely a rare condition, although its prevalence is unknown. At least 45 cases have been described in the scientific literature.
What are the genetic changes related to fibronectin glomerulopathy ? 

Fibronectin glomerulopathy can be caused by mutations in the FN1 gene. The FN1 gene provides instructions for making the fibronectin-1 protein. Fibronectin-1 is involved in the continual formation of the extracellular matrix, which is an intricate lattice of proteins and other molecules that forms in the spaces between cells. During extracellular matrix formation, fibronectin-1 helps individual cells expand (spread) and move (migrate) to cover more space, and it also influences cell shape and maturation (differentiation).  FN1 gene mutations lead to production of an abnormal fibronectin-1 protein that gets deposited in the glomeruli of the kidneys, probably as the body attempts to filter it out as waste. Even though there is an abundance of fibronectin-1 in the glomeruli, the extracellular matrix that supports the blood vessels is weak because the altered fibronectin-1 cannot assist in the matrix's continual formation. Without a strong cellular support network, the glomeruli are less able to filter waste. As a result, products that normally are retained by the body, such as protein and blood, get released in the urine, and acids are not properly filtered from the blood. Over time, the kidneys' ability to filter waste decreases until the kidneys can no longer function, resulting in end-stage renal disease.  It is estimated that mutations in the FN1 gene are responsible for 40 percent of cases of fibronectin glomerulopathy. The cause of the remaining cases of this condition is unknown.
Is fibronectin glomerulopathy inherited ? 

When fibronectin glomerulopathy is caused by mutations in the FN1 gene, it is inherited in an autosomal dominant pattern, which means one copy of the altered gene in each cell is sufficient to cause the disorder. In some of these cases, an affected person inherits the mutation from one affected parent. Other cases result from new mutations in the gene and occur in people with no history of the disorder in their family. Some people who have the altered FN1 gene never develop the condition, a situation known as reduced penetrance.
What are the treatments for fibronectin glomerulopathy ? 

These resources address the diagnosis or management of fibronectin glomerulopathy:  - Genetic Testing Registry: Glomerulopathy with fibronectin deposits 2  - MedlinePlus Encyclopedia: Protein Urine Test   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