sarnsrun/medquad huggingface dataset:
Topic: 17 alpha-hydroxylase/17,20-lyase deficiency
Question: What are the treatments for 17 alpha-hydroxylase/17,20-lyase deficiency ?
Answer: These resources address the diagnosis or management of 17 alpha-hydroxylase/17,20-lyase deficiency:  - Genetic Testing Registry: Deficiency of steroid 17-alpha-monooxygenase   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
Source: GHR
Topic: spastic paraplegia type 15
Question: What is (are) spastic paraplegia type 15 ?
Answer: Spastic paraplegia type 15 is part of a group of genetic disorders known as hereditary spastic paraplegias. These disorders are characterized by progressive muscle stiffness (spasticity) and the development of paralysis of the lower limbs (paraplegia). Spastic paraplegia type 15 is classified as a complex hereditary spastic paraplegia because it involves all four limbs as well as additional features, including abnormalities of the brain. In addition to the muscles and brain, spastic paraplegia type 15 affects the peripheral nervous system, which consists of nerves connecting the brain and spinal cord to muscles and sensory cells that detect sensations such as touch, pain, heat, and sound.  Spastic paraplegia type 15 usually becomes apparent in childhood or adolescence with the development of weak muscle tone (hypotonia), difficulty walking, or intellectual disability. In almost all affected individuals, the tissue connecting the left and right halves of the brain (corpus callosum) is abnormally thin and becomes thinner over time. Additionally, there is often a loss (atrophy) of nerve cells in several parts of the brain, including the cerebral cortex, which controls thinking and emotions, and the cerebellum, which coordinates movement.  People with this form of spastic paraplegia can have numbness, tingling, or pain in the arms and legs (sensory neuropathy); impairment of the nerves used for muscle movement (motor neuropathy); exaggerated reflexes (hyperreflexia) of the lower limbs; muscle wasting (amyotrophy); or reduced bladder control. Rarely, spastic paraplegia type 15 is associated with a group of movement abnormalities called parkinsonism, which includes tremors, rigidity, and unusually slow movement (bradykinesia). People with spastic paraplegia type 15 may have an eye condition called pigmentary maculopathy that often impairs vision. This condition results from the breakdown (degeneration) of tissue at the back of the eye called the macula, which is responsible for sharp central vision.  Most people with spastic paraplegia type 15 experience a decline in intellectual ability and an increase in muscle weakness and nerve abnormalities over time. As the condition progresses, many people require walking aids or wheelchair assistance in adulthood.
Source: GHR
Topic: spastic paraplegia type 15
Question: How many people are affected by spastic paraplegia type 15 ?
Answer: Spastic paraplegia type 15 is a rare condition, although its exact prevalence is unknown.
Source: GHR
Topic: spastic paraplegia type 15
Question: What are the genetic changes related to spastic paraplegia type 15 ?
Answer: Mutations in the ZFYVE26 gene cause spastic paraplegia type 15. This gene provides instructions for making a protein called spastizin. This protein is important in a process called autophagy, in which worn-out cell parts and unneeded proteins are recycled within cells. Specifically, spastizin is involved in the formation and maturation of sacs called autophagosomes (or autophagic vacuoles) that transport unneeded materials to be broken down. Spastizin also plays a role in the process by which dividing cells separate from one another (cytokinesis).  Many ZFYVE26 gene mutations that cause spastic paraplegia type 15 result in a shortened spastizin protein that is quickly broken down. As a result, functional autophagosomes are not produced, autophagy cannot occur, and recycling of materials within cells is decreased. An inability to break down unneeded materials, and the subsequent accumulation of these materials in cells, leads to cell dysfunction and often cell death. The loss of cells in the brain and other parts of the body is responsible for many of the features of spastic paraplegia type 15.  It is unclear whether a lack of spastizin protein interferes with normal cytokinesis and whether impaired cell division contributes to the signs and symptoms of spastic paraplegia type 15.
Source: GHR
Topic: spastic paraplegia type 15
Question: Is spastic paraplegia type 15 inherited ?
Answer: 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.
Source: GHR
Topic: spastic paraplegia type 15
Question: What are the treatments for spastic paraplegia type 15 ?
Answer: These resources address the diagnosis or management of spastic paraplegia type 15:  - Gene Review: Gene Review: Hereditary Spastic Paraplegia Overview  - Spastic Paraplegia Foundation, Inc: Treatments and Therapies   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
Source: GHR
Topic: Char syndrome
Question: What is (are) Char syndrome ?
Answer: Char syndrome is a condition that affects the development of the face, heart, and limbs. It is characterized by a combination of three major features: a distinctive facial appearance, a heart defect called patent ductus arteriosus, and hand abnormalities.  Most people with Char syndrome have a characteristic facial appearance that includes flattened cheek bones and a flat nasal bridge (the area of the nose between the eyes). The tip of the nose is also flat and broad. The eyes are wide-set with droopy eyelids (ptosis) and outside corners that point downward (down-slanting palpebral fissures). Additional facial differences include a shortened distance between the nose and upper lip (a short philtrum), a triangular-shaped mouth, and thick, prominent lips.  Patent ductus arteriosus is a common heart defect in newborns, and it occurs in most babies with Char syndrome. Before birth, the ductus arteriosus forms a connection between two major arteries (the aorta and the pulmonary artery). This connection normally closes shortly after birth, but it remains open in babies with patent ductus arteriosus. If untreated, this heart defect causes infants to breathe rapidly, feed poorly, and gain weight slowly. In severe cases, it can lead to heart failure. People with patent ductus arteriosus also have an increased risk of infection.  Hand abnormalities are another feature of Char syndrome. In most people with this condition, the middle section of the fifth (pinky) finger is shortened or absent. Other abnormalities of the hands and feet have been reported but are less common.
Source: GHR
Topic: Char syndrome
Question: How many people are affected by Char syndrome ?
Answer: Char syndrome is rare, although its exact incidence is unknown. Only a few families with this condition have been identified worldwide.
Source: GHR
Topic: Char syndrome
Question: What are the genetic changes related to Char syndrome ?
Answer: Mutations in the TFAP2B gene cause Char syndrome. This gene provides instructions for making a protein known as transcription factor AP-2. A transcription factor is a protein that attaches (binds) to specific regions of DNA and helps control the activity of particular genes. Transcription factor AP-2 regulates genes that are involved in development before birth. In particular, this protein appears to play a role in the normal formation of structures in the face, heart, and limbs.  TFAP2B mutations alter the structure of transcription factor AP-2. Some of these mutations prevent the protein from binding to DNA, while other mutations render it unable to regulate the activity of other genes. A loss of this protein's function disrupts the normal development of several parts of the body before birth, resulting in the major features of Char syndrome.
Source: GHR
Topic: Char syndrome
Question: Is Char syndrome inherited ?
Answer: 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.  In some cases, an affected person inherits the mutation from one affected parent. Other cases may result from new mutations in the gene and occur in people with no history of the disorder in their family.
Source: GHR
Topic: Char syndrome
Question: What are the treatments for Char syndrome ?
Answer: These resources address the diagnosis or management of Char syndrome:  - Gene Review: Gene Review: Char Syndrome  - Genetic Testing Registry: Char syndrome  - MedlinePlus Encyclopedia: Patent Ductus Arteriosus   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
Source: GHR
Topic: nonsyndromic holoprosencephaly
Question: How many people are affected by nonsyndromic holoprosencephaly ?
Answer: Nonsyndromic holoprosencephaly accounts for approximately 25 to 50 percent of all cases of holoprosencephaly, which affects an estimated 1 in 10,000 newborns.
Source: GHR
Topic: nonsyndromic holoprosencephaly
Question: What are the genetic changes related to nonsyndromic holoprosencephaly ?
Answer: Mutations in 11 genes have been found to cause nonsyndromic holoprosencephaly. These genes provide instructions for making proteins that are important for normal embryonic development, particularly for determining the shape of the brain and face. About 25 percent of people with nonsyndromic holoprosencephaly have a mutation in one of these four genes: SHH, ZIC2, SIX3, or TGIF1. Mutations in the other genes related to nonsyndromic holoprosencephaly are found in only a small percentage of cases. Many individuals with this condition do not have an identified gene mutation. The cause of the disorder is unknown in these individuals.  The brain normally divides into right and left hemispheres during the third to fourth week of pregnancy. To establish the line that separates the two hemispheres (the midline), the activity of many genes must be tightly regulated and coordinated. These genes provide instructions for making signaling proteins, which instruct the cells within the brain to form the right and left hemispheres.  Signaling proteins are also important for the formation of the eyes. During early development, the cells that develop into the eyes form a single structure called the eye field. This structure is located in the center of the developing face. The signaling protein produced from the SHH gene causes the eye field to separate into two distinct eyes. The SIX3 gene is involved in the formation of the lens of the eye and the specialized tissue at the back of the eye that detects light and color (the retina).  Mutations in the genes that cause nonsyndromic holoprosencephaly lead to the production of abnormal or nonfunctional signaling proteins. Without the correct signals, the eyes will not form normally and the brain does not separate into two hemispheres. The development of other parts of the face is affected if the eyes do not move to their proper position. The signs and symptoms of nonsyndromic holoprosencephaly are caused by abnormal development of the brain and face.  Researchers believe that other genetic or environmental factors, many of which have not been identified, play a role in determining the severity of nonsyndromic holoprosencephaly.
Source: GHR
Topic: nonsyndromic holoprosencephaly
Question: Is nonsyndromic holoprosencephaly inherited ?
Answer: Nonsyndromic holoprosencephaly is inherited in an autosomal dominant pattern, which means an alteration in one copy of a gene in each cell is usually sufficient to cause the disorder. However, not all people with a gene mutation will develop signs and symptoms of the condition.  In some cases, an affected person inherits the mutation from one parent who may or may not have mild features of the condition. Other cases result from a new gene mutation and occur in people with no history of the disorder in their family.
Source: GHR
Topic: nonsyndromic holoprosencephaly
Question: What are the treatments for nonsyndromic holoprosencephaly ?
Answer: These resources address the diagnosis or management of nonsyndromic holoprosencephaly:  - Gene Review: Gene Review: Holoprosencephaly Overview  - Genetic Testing Registry: Holoprosencephaly 1  - Genetic Testing Registry: Holoprosencephaly 10  - Genetic Testing Registry: Holoprosencephaly 2  - Genetic Testing Registry: Holoprosencephaly 3  - Genetic Testing Registry: Holoprosencephaly 4  - Genetic Testing Registry: Holoprosencephaly 5  - Genetic Testing Registry: Holoprosencephaly 6  - Genetic Testing Registry: Holoprosencephaly 7  - Genetic Testing Registry: Holoprosencephaly 8  - Genetic Testing Registry: Holoprosencephaly 9  - Genetic Testing Registry: Holoprosencephaly sequence  - Genetic Testing Registry: NODAL-Related Holoprosencephaly   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
Source: GHR
Topic: lactate dehydrogenase deficiency
Question: What is (are) lactate dehydrogenase deficiency ?
Answer: Lactate dehydrogenase deficiency is a condition that affects how the body breaks down sugar to use as energy in cells, primarily muscle cells.  There are two types of this condition: lactate dehydrogenase-A deficiency (sometimes called glycogen storage disease XI) and lactate dehydrogenase-B deficiency.  People with lactate dehydrogenase-A deficiency experience fatigue, muscle pain, and cramps during exercise (exercise intolerance). In some people with lactate dehydrogenase-A deficiency, high-intensity exercise or other strenuous activity leads to the 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. Some people with lactate dehydrogenase-A deficiency develop skin rashes. The severity of the signs and symptoms among individuals with lactate dehydrogenase-A deficiency varies greatly.  People with lactate dehydrogenase-B deficiency typically do not have any signs or symptoms of the condition. They do not have difficulty with physical activity or any specific physical features related to the condition. Affected individuals are usually discovered only when routine blood tests reveal reduced lactate dehydrogenase activity.
Source: GHR
Topic: lactate dehydrogenase deficiency
Question: How many people are affected by lactate dehydrogenase deficiency ?
Answer: Lactate dehydrogenase deficiency is a rare disorder. In Japan, this condition affects 1 in 1 million individuals; the prevalence of lactate dehydrogenase deficiency in other countries is unknown.
Source: GHR
Topic: lactate dehydrogenase deficiency
Question: What are the genetic changes related to lactate dehydrogenase deficiency ?
Answer: Mutations in the LDHA gene cause lactate dehydrogenase-A deficiency, and mutations in the LDHB gene cause lactate dehydrogenase-B deficiency. These genes provide instructions for making the lactate dehydrogenase-A and lactate dehydrogenase-B pieces (subunits) of the lactate dehydrogenase enzyme. This enzyme is found throughout the body and is important for creating energy for cells. There are five different forms of this enzyme, each made up of four protein subunits. Various combinations of the lactate dehydrogenase-A and lactate dehydrogenase-B subunits make up the different forms of the enzyme.  The version of lactate dehydrogenase made of four lactate dehydrogenase-A subunits is found primarily in skeletal muscles, which are muscles used for movement. Skeletal muscles need large amounts of energy during high-intensity physical activity when the body's oxygen intake is not sufficient for the amount of energy required (anaerobic exercise). During anaerobic exercise, the lactate dehydrogenase enzyme is involved in the breakdown of sugar stored in the muscles (in the form of glycogen) to create additional energy. During the final stage of glycogen breakdown, lactate dehydrogenase converts a molecule called pyruvate to a similar molecule called lactate.  Mutations in the LDHA gene result in the production of an abnormal lactate dehydrogenase-A subunit that cannot attach (bind) to other subunits to form the lactate dehydrogenase enzyme. A lack of functional subunit reduces the amount of enzyme that is formed, mostly affecting skeletal muscles. As a result, glycogen is not broken down efficiently, leading to decreased energy in muscle cells. When muscle cells do not get sufficient energy during exercise or strenuous activity, the muscles become weak and muscle tissue can break down, as experienced by people with lactate dehydrogenase-A deficiency.  The version of lactate dehydrogenase made of four lactate dehydrogenase-B subunits is found primarily in heart (cardiac) muscle. In cardiac muscle, lactate dehydrogenase converts lactate to pyruvate, which can participate in other chemical reactions to create energy. LDHB gene mutations lead to the production of an abnormal lactate dehydrogenase-B subunit that cannot form the lactate dehydrogenase enzyme. Even though lactate dehydrogenase activity is decreased in the cardiac muscle of people with lactate dehydrogenase-B deficiency, they do not appear to have any signs or symptoms related to their condition. It is unclear why this type of enzyme deficiency does not cause any health problems.
Source: GHR
Topic: lactate dehydrogenase deficiency
Question: Is lactate dehydrogenase deficiency inherited ?
Answer: 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.
Source: GHR
Topic: lactate dehydrogenase deficiency
Question: What are the treatments for lactate dehydrogenase deficiency ?
Answer: These resources address the diagnosis or management of lactate dehydrogenase deficiency:  - Genetic Testing Registry: Glycogen storage disease XI  - Genetic Testing Registry: Lactate dehydrogenase B deficiency  - MedlinePlus Encyclopedia: LDH Isoenzymes  - MedlinePlus Encyclopedia: Lactate Dehydrogenase 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
Source: GHR
Topic: Diamond-Blackfan anemia
Question: What is (are) Diamond-Blackfan anemia ?
Answer: Diamond-Blackfan anemia is a disorder of the bone marrow. The major function of bone marrow is to produce new blood cells. In Diamond-Blackfan anemia, the bone marrow malfunctions and fails to make enough red blood cells, which carry oxygen to the body's tissues. The resulting shortage of red blood cells (anemia) usually becomes apparent during the first year of life. Symptoms of anemia include fatigue, weakness, and an abnormally pale appearance (pallor).  People with Diamond-Blackfan anemia have an increased risk of several serious complications related to their malfunctioning bone marrow. Specifically, they have a higher-than-average chance of developing myelodysplastic syndrome (MDS), which is a disorder in which immature blood cells fail to develop normally. Affected individuals also have an increased risk of developing certain cancers, including a cancer of blood-forming tissue known as acute myeloid leukemia (AML) and a type of bone cancer called osteosarcoma.  Approximately half of individuals with Diamond-Blackfan anemia have physical abnormalities. They may have an unusually small head size (microcephaly) and a low frontal hairline, along with distinctive facial features such as wide-set eyes (hypertelorism); droopy eyelids (ptosis); a broad, flat bridge of the nose; small, low-set ears; and a small lower jaw (micrognathia). Affected individuals may also have an opening in the roof of the mouth (cleft palate) with or without a split in the upper lip (cleft lip). They may have a short, webbed neck; shoulder blades which are smaller and higher than usual; and abnormalities of their hands, most commonly malformed or absent thumbs. About one-third of affected individuals have slow growth leading to short stature.  Other features of Diamond-Blackfan anemia may include eye problems such as clouding of the lens of the eyes (cataracts), increased pressure in the eyes (glaucoma), or eyes that do not look in the same direction (strabismus). Affected individuals may also have kidney abnormalities; structural defects of the heart; and, in males, the opening of the urethra on the underside of the penis (hypospadias).  The severity of Diamond-Blackfan anemia may vary, even within the same family. Increasingly, individuals with "non-classical" Diamond-Blackfan anemia have been identified. This form of the disorder typically has less severe symptoms that may include mild anemia beginning in adulthood.
Source: GHR
Topic: Diamond-Blackfan anemia
Question: How many people are affected by Diamond-Blackfan anemia ?
Answer: Diamond-Blackfan anemia affects approximately 5 to 7 per million liveborn infants worldwide.
Source: GHR
Topic: Diamond-Blackfan anemia
Question: What are the genetic changes related to Diamond-Blackfan anemia ?
Answer: Diamond-Blackfan anemia can be caused by mutations in the RPL5, RPL11, RPL35A, RPS7, RPS10, RPS17, RPS19, RPS24, and RPS26 genes. These genes provide instructions for making several of the approximately 80 different ribosomal proteins, which are components of cellular structures called ribosomes. Ribosomes process the cell's genetic instructions to create proteins.  Each ribosome is made up of two parts (subunits) called the large and small subunits. The RPL5, RPL11, and RPL35A genes provide instructions for making ribosomal proteins that are among those found in the large subunit. The ribosomal proteins produced from the RPS7, RPS10, RPS17, RPS19, RPS24, and RPS26 genes are among those found in the small subunit.  The specific functions of each ribosomal protein within these subunits are unclear. Some ribosomal proteins are involved in the assembly or stability of ribosomes. Others help carry out the ribosome's main function of building new proteins. Studies suggest that some ribosomal proteins may have other functions, such as participating in chemical signaling pathways within the cell, regulating cell division, and controlling the self-destruction of cells (apoptosis).  Mutations in any of the genes listed above are believed to affect the stability or function of the ribosomal proteins. Studies indicate that a shortage of functioning ribosomal proteins may increase the self-destruction of blood-forming cells in the bone marrow, resulting in anemia. Abnormal regulation of cell division or inappropriate triggering of apoptosis may contribute to the other health problems that affect some people with Diamond-Blackfan anemia.  Approximately 25 percent of individuals with Diamond-Blackfan anemia have identified mutations in the RPS19 gene. About another 25 to 35 percent of individuals with this disorder have identified mutations in the RPL5, RPL11, RPL35A, RPS7, RPS10, RPS17, RPS24, or RPS26 genes. In the remaining 40 to 50 percent of cases, the cause of the condition is unknown. Researchers suspect that other genes may also be associated with Diamond-Blackfan anemia.
Source: GHR