sarnsrun/medquadmini huggingface dataset:
Question:
What are the genetic changes related to ocular albinism ?

Answer:
Ocular albinism type 1 results from mutations in the GPR143 gene. This gene provides instructions for making a protein that plays a role in pigmentation of the eyes and skin. It helps control the growth of melanosomes, which are cellular structures that produce and store a pigment called melanin. Melanin is the substance that gives skin, hair, and eyes their color. In the retina, this pigment also plays a role in normal vision.  Most mutations in the GPR143 gene alter the size or shape of the GPR143 protein. Many of these genetic changes prevent the protein from reaching melanosomes to control their growth. In other cases, the protein reaches melanosomes normally but mutations disrupt the protein's function. As a result of these changes, melanosomes in skin cells and the retina can grow abnormally large. Researchers are uncertain how these giant melanosomes are related to vision loss and other eye abnormalities in people with ocular albinism.  Rare cases of ocular albinism are not caused by mutations in the GPR143 gene. In these cases, the genetic cause of the condition is often unknown.
Question:
Is ocular albinism inherited ?

Answer:
Ocular albinism type 1 is inherited in an X-linked pattern. A condition is considered X-linked if the mutated gene that causes the disorder is located on the X chromosome, one of the two sex chromosomes. In males (who have only one X chromosome), one altered copy of the GPR143 gene in each cell is sufficient to cause the characteristic features of ocular albinism. Because females have two copies of the X chromosome, women with only one copy of a GPR143 mutation in each cell usually do not experience vision loss or other significant eye abnormalities. They may have mild changes in retinal pigmentation that can be detected during an eye examination.
Question:
What are the treatments for ocular albinism ?

Answer:
These resources address the diagnosis or management of ocular albinism:  - Gene Review: Gene Review: Ocular Albinism, X-Linked  - Genetic Testing Registry: Albinism ocular late onset sensorineural deafness  - Genetic Testing Registry: Albinism, ocular, with sensorineural deafness  - Genetic Testing Registry: Ocular albinism, type I  - MedlinePlus Encyclopedia: Albinism   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
Question:
What is (are) DOLK-congenital disorder of glycosylation ?

Answer:
DOLK-congenital disorder of glycosylation (DOLK-CDG, formerly known as congenital disorder of glycosylation type Im) is an inherited condition that often affects the heart but can also involve other body systems. The pattern and severity of this disorder's signs and symptoms vary among affected individuals.  Individuals with DOLK-CDG typically develop signs and symptoms of the condition during infancy or early childhood. Nearly all individuals with DOLK-CDG develop a weakened and enlarged heart (dilated cardiomyopathy). Other frequent signs and symptoms include recurrent seizures; developmental delay; poor muscle tone (hypotonia); and dry, scaly skin (ichthyosis). Less commonly, affected individuals can have distinctive facial features, kidney disease, hormonal abnormalities, or eye problems.  Individuals with DOLK-CDG typically do not survive into adulthood, often because of complications related to dilated cardiomyopathy, and some do not survive past infancy.
Question:
How many people are affected by DOLK-congenital disorder of glycosylation ?

Answer:
DOLK-CDG is likely a rare condition; at least 18 cases have been reported in the scientific literature.
Question:
What are the genetic changes related to DOLK-congenital disorder of glycosylation ?

Answer:
DOLK-CDG is caused by mutations in the DOLK gene. This gene provides instructions for making the enzyme dolichol kinase, which facilitates the final step of the production of a compound called dolichol phosphate. This compound is critical for a process called glycosylation, which attaches groups of sugar molecules (oligosaccharides) to proteins. Glycosylation changes proteins in ways that are important for their functions. During glycosylation, sugars are added to dolichol phosphate in order to build the oligosaccharide chain. Once the chain is formed, dolichol phosphate transports the oligosaccharide to the protein that needs to be glycosylated and attaches it to a specific site on the protein.  Mutations in the DOLK gene lead to the production of abnormal dolichol kinase with reduced or absent activity. Without properly functioning dolichol kinase, dolichol phosphate is not produced and glycosylation cannot proceed normally. In particular, a protein known to stabilize heart muscle fibers, called alpha-dystroglycan, has been shown to have reduced glycosylation in people with DOLK-CDG. Impaired glycosylation of alpha-dystroglycan disrupts its normal function, which damages heart muscle fibers as they repeatedly contract and relax. Over time, the fibers weaken and break down, leading to dilated cardiomyopathy. The other signs and symptoms of DOLK-CDG are likely due to the abnormal glycosylation of additional proteins in other organs and tissues.
Question:
Is DOLK-congenital disorder of glycosylation 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.
Question:
What are the treatments for DOLK-congenital disorder of glycosylation ?

Answer:
These resources address the diagnosis or management of DOLK-CDG:  - Gene Review: Gene Review: Congenital Disorders of N-Linked Glycosylation Pathway Overview  - Genetic Testing Registry: Congenital disorder of glycosylation type 1M  - MedlinePlus Encyclopedia: Dilated Cardiomyopathy   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
Question:
What is (are) mucolipidosis III gamma ?

Answer:
Mucolipidosis III gamma is a slowly progressive disorder that affects many parts of the body. Signs and symptoms of this condition typically appear around age 3.  Individuals with mucolipidosis III gamma grow slowly and have short stature. They also have stiff joints and dysostosis multiplex, which refers to multiple skeletal abnormalities seen on x-ray. Many affected individuals develop low bone mineral density (osteoporosis), which weakens the bones and makes them prone to fracture. Osteoporosis and progressive joint problems in people with mucolipidosis III gamma also cause pain, which becomes more severe over time.  People with mucolipidosis III gamma often have heart valve abnormalities and mild clouding of the clear covering of the eye (cornea). Their facial features become slightly thickened or "coarse" as they get older. A small percentage of people with this condition have mild intellectual disability or learning problems. Individuals with mucolipidosis III gamma generally survive into adulthood, but they may have a shortened lifespan.
Question:
How many people are affected by mucolipidosis III gamma ?

Answer:
Mucolipidosis III gamma is a rare disorder, although its exact prevalence is unknown. It is estimated to occur in about 1 in 100,000 to 400,000 individuals worldwide.
Question:
What are the genetic changes related to mucolipidosis III gamma ?

Answer:
Mutations in the GNPTG gene cause mucolipidosis III gamma. This gene provides instructions for making one part (subunit) of an enzyme called GlcNAc-1-phosphotransferase. This enzyme helps prepare certain newly made enzymes for transport to lysosomes. Lysosomes are compartments within the cell that use digestive enzymes to break down large molecules into smaller ones that can be reused by cells. GlcNAc-1-phosphotransferase is involved in the process of attaching a molecule called mannose-6-phosphate (M6P) to specific digestive enzymes. Just as luggage is tagged at the airport to direct it to the correct destination, enzymes are often "tagged" after they are made so they get to where they are needed in the cell. M6P acts as a tag that indicates a digestive enzyme should be transported to the lysosome.  Mutations in the GNPTG gene that cause mucolipidosis III gamma result in reduced activity of GlcNAc-1-phosphotransferase. These mutations disrupt the tagging of digestive enzymes with M6P, which prevents many enzymes from reaching the lysosomes. Digestive enzymes that do not receive the M6P tag end up outside the cell, where they have increased activity. The shortage of digestive enzymes within lysosomes causes large molecules to accumulate there. Conditions that cause molecules to build up inside lysosomes, including mucolipidosis III gamma, are called lysosomal storage disorders. The signs and symptoms of mucolipidosis III gamma are most likely due to the shortage of digestive enzymes inside lysosomes and the effects these enzymes have outside the cell.
Question:
Is mucolipidosis III gamma 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.
Question:
What are the treatments for mucolipidosis III gamma ?

Answer:
These resources address the diagnosis or management of mucolipidosis III gamma:  - Gene Review: Gene Review: Mucolipidosis III Gamma  - Genetic Testing Registry: Mucolipidosis III Gamma  - MedlinePlus Encyclopedia: Cloudy Cornea  - MedlinePlus Encyclopedia: Heart Valves   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
Question:
What is (are) Hutchinson-Gilford progeria syndrome ?

Answer:
Hutchinson-Gilford progeria syndrome is a genetic condition characterized by the dramatic, rapid appearance of aging beginning in childhood. Affected children typically look normal at birth and in early infancy, but then grow more slowly than other children and do not gain weight at the expected rate (failure to thrive). They develop a characteristic facial appearance including prominent eyes, a thin nose with a beaked tip, thin lips, a small chin, and protruding ears. Hutchinson-Gilford progeria syndrome also causes hair loss (alopecia), aged-looking skin, joint abnormalities, and a loss of fat under the skin (subcutaneous fat). This condition does not disrupt intellectual development or the development of motor skills such as sitting, standing, and walking.  People with Hutchinson-Gilford progeria syndrome experience severe hardening of the arteries (arteriosclerosis) beginning in childhood. This condition greatly increases the chances of having a heart attack or stroke at a young age. These serious complications can worsen over time and are life-threatening for affected individuals.
Question:
How many people are affected by Hutchinson-Gilford progeria syndrome ?

Answer:
This condition is very rare; it is reported to occur in 1 in 4 million newborns worldwide. More than 130 cases have been reported in the scientific literature since the condition was first described in 1886.
Question:
What are the genetic changes related to Hutchinson-Gilford progeria syndrome ?

Answer:
Mutations in the LMNA gene cause Hutchinson-Gilford progeria syndrome.  The LMNA gene provides instructions for making a protein called lamin A. This protein plays an important role in determining the shape of the nucleus within cells. It is an essential scaffolding (supporting) component of the nuclear envelope, which is the membrane that surrounds the nucleus. Mutations that cause Hutchinson-Gilford progeria syndrome result in the production of an abnormal version of the lamin A protein. The altered protein makes the nuclear envelope unstable and progressively damages the nucleus, making cells more likely to die prematurely. Researchers are working to determine how these changes lead to the characteristic features of Hutchinson-Gilford progeria syndrome.
Question:
Is Hutchinson-Gilford progeria syndrome inherited ?

Answer:
Hutchinson-Gilford progeria syndrome is considered an autosomal dominant condition, which means one copy of the altered gene in each cell is sufficient to cause the disorder. The condition results from new mutations in the LMNA gene, and almost always occurs in people with no history of the disorder in their family.
Question:
What are the treatments for Hutchinson-Gilford progeria syndrome ?

Answer:
These resources address the diagnosis or management of Hutchinson-Gilford progeria syndrome:  - Gene Review: Gene Review: Hutchinson-Gilford Progeria Syndrome  - Genetic Testing Registry: Hutchinson-Gilford syndrome  - MedlinePlus Encyclopedia: Progeria   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
Question:
What is (are) Northern epilepsy ?

Answer:
Northern epilepsy is a genetic condition that causes recurrent seizures (epilepsy) beginning in childhood, usually between ages 5 and 10. Seizures are often the generalized tonic-clonic type, which involve muscle rigidity, convulsions, and loss of consciousness. These seizures typically last less than 5 minutes but can last up to 15 minutes. Some people with Northern epilepsy also experience partial seizures, which do not cause a loss of consciousness. The seizures occur approximately one to two times per month until adolescence; then the frequency decreases to about four to six times per year by early adulthood. By middle age, seizures become even less frequent.  Two to 5 years after the start of seizures, people with Northern epilepsy begin to experience a decline in intellectual function, which can result in mild intellectual disability. Problems with coordination usually begin in young adulthood and lead to clumsiness and difficulty with fine motor activities such as writing, using eating utensils, and fastening buttons. During this time, affected individuals often begin to develop balance problems and they walk slowly with short, wide steps. These intellectual and movement problems worsen over time. A loss of sharp vision (reduced visual acuity) may also occur in early to mid-adulthood.  Individuals with Northern epilepsy often live into late adulthood, but depending on the severity of the intellectual disability and movement impairments, they may require assistance with tasks of everyday living.  Northern epilepsy is one of a group of disorders known as neuronal ceroid lipofuscinoses (NCLs), which are also known as Batten disease. These disorders affect the nervous system and typically cause progressive problems with vision, movement, and thinking ability. The different types of NCLs are distinguished by the age at which signs and symptoms first appear. Northern epilepsy is the mildest form of NCL.
Question:
How many people are affected by Northern epilepsy ?

Answer:
Northern epilepsy appears to affect only individuals of Finnish ancestry, particularly those from the Kainuu region of northern Finland. Approximately 1 in 10,000 individuals in this region have the condition.
Question:
What are the genetic changes related to Northern epilepsy ?

Answer:
Mutations in the CLN8 gene cause Northern epilepsy. The CLN8 gene provides instructions for making a protein whose function is not well understood. The CLN8 protein is thought to play a role in transporting materials in and out of a cell structure called the endoplasmic reticulum. The endoplasmic reticulum is involved in protein production, processing, and transport. Based on the structure of the CLN8 protein, it may also help regulate the levels of fats (lipids) in cells.  A single CLN8 gene mutation has been identified to cause Northern epilepsy. Nearly all affected individuals have this mutation in both copies of the CLN8 gene in each cell. The effects of this mutation on protein function are unclear. Unlike other forms of NCL that result in the accumulation of large amounts of fatty substances called lipopigments in cells, contributing to cell death, Northern epilepsy is associated with very little lipopigment buildup. People with Northern epilepsy do have mild brain abnormalities resulting from cell death, but the cause of this brain cell death is unknown. It is also unclear how changes in the CLN8 protein and a loss of brain cells cause the neurological problems associated with Northern epilepsy.
Question:
Is Northern epilepsy 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.
Question:
What are the treatments for Northern epilepsy ?

Answer:
These resources address the diagnosis or management of Northern epilepsy:  - Gene Review: Gene Review: Neuronal Ceroid-Lipofuscinoses  - Genetic Testing Registry: Ceroid lipofuscinosis, neuronal, 8, northern epilepsy variant   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
Question:
What is (are) mandibuloacral dysplasia ?

Answer:
Mandibuloacral dysplasia is a condition that causes a variety of abnormalities involving bone development, skin coloring (pigmentation), and fat distribution. People with this condition may grow slowly after birth. Most affected individuals are born with an underdeveloped lower jaw bone (mandible) and small collar bones (clavicles), leading to the characteristic features of a small chin and sloped shoulders. Other bone problems include loss of bone from the tips of the fingers (acroosteolysis), which causes bulbous finger tips; delayed closure of certain skull bones; and joint deformities (contractures).  People with mandibuloacral dysplasia can have mottled or patchy skin pigmentation or other skin abnormalities. Some people with this condition have features of premature aging (a condition called progeria), such as thin skin, loss of teeth, loss of hair, and a beaked nose. Some individuals with mandibuloacral dysplasia have metabolic problems, such as diabetes.  A common feature of mandibuloacral dysplasia is a lack of fatty tissue under the skin (lipodystrophy) in certain regions of the body. The two types of this disorder, mandibuloacral dysplasia with type A lipodystrophy (MADA) and mandibuloacral dysplasia with type B lipodystrophy (MADB) are distinguished by the pattern of fat distribution throughout the body. Type A is described as partial lipodystrophy; affected individuals have a loss of fatty tissue from the torso and limbs, but it may build up around the neck and shoulders. Type B is a generalized lipodystrophy, with loss of fatty tissue in the face, torso, and limbs.  MADA usually begins in adulthood, although children can be affected. MADB begins earlier, often just after birth. Many babies with MADB are born prematurely.
Question:
How many people are affected by mandibuloacral dysplasia ?

Answer:
Mandibuloacral dysplasia is a rare condition; its prevalence is unknown.
Question:
What are the genetic changes related to mandibuloacral dysplasia ?

Answer:
The two forms of mandibuloacral dysplasia are caused by mutations in different genes. Mutations in the LMNA gene cause MADA, and mutations in the ZMPSTE24 gene cause MADB. Within cells, these genes are involved in maintaining the structure of the nucleus and may play a role in many cellular processes.  The LMNA gene provides instructions for making two related proteins, lamin A and lamin C. These proteins act as scaffolding (supporting) components of the nuclear envelope, which is the membrane that surrounds the nucleus in cells. The nuclear envelope regulates the movement of molecules into and out of the nucleus and may help regulate the activity of certain genes. Mutations in this gene likely change the structure of lamin A and lamin C.  The lamin A protein (but not lamin C) must be processed within the cell before becoming part of the nuclear envelope. The protein produced from the ZMPSTE24 gene is involved in this processing; it cuts the immature lamin A protein (prelamin A) at a particular location, forming mature lamin A. Mutations in the ZMPSTE24 gene lead to a buildup of prelamin A and a shortage of the mature protein.  Mutations in the LMNA or ZMPSTE24 gene likely disrupt the structure of the nuclear envelope. Researchers are working to understand how these genetic changes result in the signs and symptoms of mandibuloacral dysplasia.
Question:
Is mandibuloacral dysplasia 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.
Question:
What are the treatments for mandibuloacral dysplasia ?

Answer:
These resources address the diagnosis or management of mandibuloacral dysplasia:  - Genetic Testing Registry: Mandibuloacral dysostosis  - Genetic Testing Registry: Mandibuloacral dysplasia with type B lipodystrophy   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
Question:
What is (are) sporadic hemiplegic migraine ?

Answer:
Sporadic hemiplegic migraine is a rare form of migraine headache. Migraines typically cause intense, throbbing pain in one area of the head. Some people with migraines also experience nausea, vomiting, and sensitivity to light and sound. These recurrent headaches typically begin in childhood or adolescence and can be triggered by certain foods, emotional stress, and minor head trauma. Each headache may last from a few hours to a few days.  In sporadic hemiplegic migraine and some other types of migraine, a pattern of neurological symptoms called an aura occurs before onset of the headache. An aura commonly includes temporary visual changes such as blind spots (scotomas), flashing lights, zig-zagging lines, and double vision. In people with sporadic hemiplegic migraine, auras are also characterized by temporary numbness or weakness, often affecting one side of the body (hemiparesis). Additional features of an aura can include difficulty with speech, confusion, and drowsiness. An aura typically develops gradually over a few minutes and lasts about an hour.  Some people with sporadic hemiplegic migraine experience unusually severe migraine episodes. These episodes can include fever, prolonged weakness, seizures, and coma. Although most people with sporadic hemiplegic migraine recover completely between episodes, neurological symptoms such as memory loss and problems with attention can last for weeks or months. Some affected individuals develop mild but permanent difficulty coordinating movements (ataxia), which may worsen with time, and rapid, involuntary eye movements called nystagmus. Mild to severe intellectual disability has been reported in some people with sporadic hemiplegic migraine.