A group of sporadic, familial and/or inherited, degenerative, and infectious disease processes, linked by the common theme of abnormal protein folding and deposition of AMYLOID. As the amyloid deposits enlarge they displace normal tissue structures, causing disruption of function. Various signs and symptoms depend on the location and size of the deposits.
Diseases in which there is a familial pattern of AMYLOIDOSIS.
A fibrous protein complex that consists of proteins folded into a specific cross beta-pleated sheet structure. This fibrillar structure has been found as an alternative folding pattern for a variety of functional proteins. Deposits of amyloid in the form of AMYLOID PLAQUES are associated with a variety of degenerative diseases. The amyloid structure has also been found in a number of functional proteins that are unrelated to disease.
An ACUTE PHASE REACTION protein present in low concentrations in normal sera, but found at higher concentrations in sera of older persons and in patients with AMYLOIDOSIS. It is the circulating precusor of amyloid A protein, which is found deposited in AA type AMYLOID FIBRILS.
A tetrameric protein, molecular weight between 50,000 and 70,000, consisting of 4 equal chains, and migrating on electrophoresis in 3 fractions more mobile than serum albumin. Its concentration ranges from 7 to 33 per cent in the serum, but levels decrease in liver disease.
Polypeptide chains, consisting of 211 to 217 amino acid residues and having a molecular weight of approximately 22 kDa. There are two major types of light chains, kappa and lambda. Two Ig light chains and two Ig heavy chains (IMMUNOGLOBULIN HEAVY CHAINS) make one immunoglobulin molecule.
A group of HEREDITARY AUTOINFLAMMATION DISEASES, characterized by recurrent fever, abdominal pain, headache, rash, PLEURISY; and ARTHRITIS. ORCHITIS; benign MENINGITIS; and AMYLOIDOSIS may also occur. Homozygous or compound heterozygous mutations in marenostrin gene result in autosomal recessive transmission; simple heterozygous, autosomal dominant form of the disease.
Disorders of the peripheral nervous system associated with the deposition of AMYLOID in nerve tissue. Familial, primary (nonfamilial), and secondary forms have been described. Some familial subtypes demonstrate an autosomal dominant pattern of inheritance. Clinical manifestations include sensory loss, mild weakness, autonomic dysfunction, and CARPAL TUNNEL SYNDROME. (Adams et al., Principles of Neurology, 6th ed, p1349)
An acid dye used in testing for hydrochloric acid in gastric contents. It is also used histologically to test for AMYLOIDOSIS.
Inherited disorders of the peripheral nervous system associated with the deposition of AMYLOID in nerve tissue. The different clinical types based on symptoms correspond to the presence of a variety of mutations in several different proteins including transthyretin (PREALBUMIN); APOLIPOPROTEIN A-I; and GELSOLIN.
A group of diseases in which the dominant feature is the involvement of the CARDIAC MUSCLE itself. Cardiomyopathies are classified according to their predominant pathophysiological features (DILATED CARDIOMYOPATHY; HYPERTROPHIC CARDIOMYOPATHY; RESTRICTIVE CARDIOMYOPATHY) or their etiological/pathological factors (CARDIOMYOPATHY, ALCOHOLIC; ENDOCARDIAL FIBROELASTOSIS).
An 11-kDa protein associated with the outer membrane of many cells including lymphocytes. It is the small subunit of the MHC class I molecule. Association with beta 2-microglobulin is generally required for the transport of class I heavy chains from the endoplasmic reticulum to the cell surface. Beta 2-microglobulin is present in small amounts in serum, csf, and urine of normal people, and to a much greater degree in the urine and plasma of patients with tubular proteinemia, renal failure, or kidney transplants.
Amyloid P component is a small, non-fibrillar glycoprotein found in normal serum and in all amyloid deposits. It has a pentagonal (pentaxin) structure. It is an acute phase protein, modulates immunologic responses, inhibits ELASTASE, and has been suggested as an indicator of LIVER DISEASE.
A condition characterized by severe PROTEINURIA, greater than 3.5 g/day in an average adult. The substantial loss of protein in the urine results in complications such as HYPOPROTEINEMIA; generalized EDEMA; HYPERTENSION; and HYPERLIPIDEMIAS. Diseases associated with nephrotic syndrome generally cause chronic kidney dysfunction.
A group of related diseases characterized by an unbalanced or disproportionate proliferation of immunoglobulin-producing cells, usually from a single clone. These cells frequently secrete a structurally homogeneous immunoglobulin (M-component) and/or an abnormal immunoglobulin.
Tracheal diseases refer to a range of medical conditions that affect the structure, function, and integrity of the trachea, including inflammation, infection, trauma, tumors, and congenital abnormalities, which can lead to symptoms such as cough, wheezing, difficulty breathing, and stridor.
Pathological processes of the KIDNEY or its component tissues.
The presence of an excessively large tongue, which may be congenital or may develop as a result of a tumor or edema due to obstruction of lymphatic vessels, or it may occur in association with hyperpituitarism or acromegaly. It also may be associated with malocclusion because of pressure of the tongue on the teeth. (From Jablonski, Dictionary of Dentistry, 1992)
Proteins that form the core of amyloid fibrils. For example, the core of amyloid A is formed from amyloid A protein, also known as serum amyloid A protein or SAA protein.
An alkylating nitrogen mustard that is used as an antineoplastic in the form of the levo isomer - MELPHALAN, the racemic mixture - MERPHALAN, and the dextro isomer - MEDPHALAN; toxic to bone marrow, but little vesicant action; potential carcinogen.
An abnormal protein with unusual thermosolubility characteristics that is found in the urine of patients with MULTIPLE MYELOMA.
Removal and pathologic examination of specimens in the form of small pieces of tissue from the living body.
A genus of long-legged, swift-moving felines (FELIDAE) from Africa (and formerly Asia) about the size of a small leopard.
One of the types of light chain subunits of the immunoglobulins with a molecular weight of approximately 22 kDa.
A 90-kDa protein produced by macrophages that severs ACTIN filaments and forms a cap on the newly exposed filament end. Gelsolin is activated by CALCIUM ions and participates in the assembly and disassembly of actin, thereby increasing the motility of some CELLS.
Blood coagulation disorder usually inherited as an autosomal recessive trait, though it can be acquired. It is characterized by defective activity in both the intrinsic and extrinsic pathways, impaired thromboplastin time, and impaired prothrombin consumption.
Diseases of the skin with a genetic component, usually the result of various inborn errors of metabolism.
Death resulting from the presence of a disease in an individual, as shown by a single case report or a limited number of patients. This should be differentiated from DEATH, the physiological cessation of life and from MORTALITY, an epidemiological or statistical concept.
A malignancy of mature PLASMA CELLS engaging in monoclonal immunoglobulin production. It is characterized by hyperglobulinemia, excess Bence-Jones proteins (free monoclonal IMMUNOGLOBULIN LIGHT CHAINS) in the urine, skeletal destruction, bone pain, and fractures. Other features include ANEMIA; HYPERCALCEMIA; and RENAL INSUFFICIENCY.
Works containing information articles on subjects in every field of knowledge, usually arranged in alphabetical order, or a similar work limited to a special field or subject. (From The ALA Glossary of Library and Information Science, 1983)
Plasma glycoprotein clotted by thrombin, composed of a dimer of three non-identical pairs of polypeptide chains (alpha, beta, gamma) held together by disulfide bonds. Fibrinogen clotting is a sol-gel change involving complex molecular arrangements: whereas fibrinogen is cleaved by thrombin to form polypeptides A and B, the proteolytic action of other enzymes yields different fibrinogen degradation products.
A deficiency or absence of FIBRINOGEN in the blood.

Furin initiates gelsolin familial amyloidosis in the Golgi through a defect in Ca(2+) stabilization. (1/67)

Hereditary familial amyloidosis of Finnish type (FAF) leading to amyloid in the peripheral and central nervous systems stems from deposition of a 71 residue fragment generated from the D187N/Y variants of plasma gelsolin by two sequential endoproteolytic events. We identify the protease accomplishing the first cleavage as furin, a proprotein convertase. Endoproteolysis of plasma gelsolin occurs in the trans-Golgi network due to the inability of the FAF variants to bind and be stabilized by Ca(2+). Secretion and processing of the FAF variants by furin can be uncoupled by blocking the convergence of the exocytic pathway transporting plasma gelsolin and the endocytic recycling of furin. We propose that coincidence of membrane trafficking pathways contributes to the development of proteolysis-initiated amyloid disease.  (+info)

Misdiagnosis of hereditary amyloidosis as AL (primary) amyloidosis. (2/67)

BACKGROUND: Hereditary, autosomal dominant amyloidosis, caused by mutations in the genes encoding transthyretin, fibrinogen A alpha-chain, lysozyme, or apolipoprotein A-I, is thought to be extremely rare and is not routinely included in the differential diagnosis of systemic amyloidosis unless there is a family history. METHODS: We studied 350 patients with systemic amyloidosis, in whom a diagnosis of the light-chain (AL) type of the disorder had been suggested by clinical and laboratory findings and by the absence of a family history, to assess whether they had amyloidogenic mutations. RESULTS: Amyloidogenic mutations were present in 34 of the 350 patients (9.7 percent), most often in the genes encoding fibrinogen A alpha-chain (18 patients) and transthyretin (13 patients). In all 34 of these patients, the diagnosis of hereditary amyloidosis was confirmed by additional investigations. A low-grade monoclonal gammopathy was detected in 8 of the 34 patients (24 percent). CONCLUSIONS: A genetic cause should be sought in all patients with amyloidosis that is not the reactive systemic amyloid A type and in whom confirmation of the AL type cannot be obtained.  (+info)

Mutational spectrum in the MEFV and TNFRSF1A genes in patients suffering from AA amyloidosis and recurrent inflammatory attacks. (3/67)

BACKGROUND: Among hereditary fevers characterized by recurrent attacks of fever and organ localized inflammation, familial Mediterranean fever (FMF), and tumour necrosis factor receptor superfamily 1A (TNFRSF1A) receptor associated periodic syndrome (TRAPS) are diseases with identified genes that can be associated with renal amyloidosis of the AA type. In this study we have characterized FMF and TRAPS genotypes in 38 unrelated patients suffering from amyloidosis AA and recurrent inflammatory attacks. METHODS: Mutations of the MEFV and TNFRSF1A genes, responsible respectively for FMF and TRAPS, were searched for by amplifying, using polymerase chain reaction (PCR), genomic DNA, and direct sequencing. RESULTS: Twenty-seven patients (71%) carried mutations in MEFV (22 patients with two mutations, two patients with a single mutation) or TNFRSF1A genes (three patients). Patients with MEFV mutations belonged to the classical at-risk ethnic group for FMF: Sephardic Jews, Turks, Armenians, and Arabs from the Maghreb. The main genotype encountered was M694V/M694V (19/22), one Turkish patient was M680I/M680I, and two Arab patients from the Maghreb were M694I/M694I. We found three Caucasian patients with the C55S, C70Y, R92Q mutations in the TNFRSF1A gene. CONCLUSIONS: In this series we observed that FMF is the main cause of AA amyloidosis in Sephardic Jews and Turks. MEFV and TNFRSF1A mutations were found in only 6 of 14 Arab patients from the Maghreb. We found three families (one Caucasian and two from Maghreb) with AA amyloidosis without MEFV or TNFRSF1A mutations, suggesting that other genetic cause(s) exist(s). The characterization of mutations in MEFV and TNFRSF1A is important for the therapeutic behaviour of AA amyloidosis associated with inherited recurrent fever.  (+info)

Immunoglobulin light chain variable (V) region genes influence clinical presentation and outcome in light chain-associated amyloidosis (AL). (4/67)

Light chain-associated amyloidosis (AL) is a plasma cell dyscrasia in which the secreted monoclonal immunoglobulin (Ig) light chains form amyloid fibrils. There is considerable heterogeneity in clinical presentation, and prognosis of the disease relates to the severity of organ dysfunction induced by amyloid deposits. The mechanisms by which the amyloid fibrils are deposited as well as the predilection for specific organ sites have not been clearly elucidated. This study characterizes the repertoire of immunoglobulin light chain variable genes used by the clonal B cell in AL amyloid patients, and the association of light chain variable region (VL) genes with clinical presentation and outcome is assessed in 58 (32 lambda and 26 kappa) patients. A preferential use of VL germ-line genes was noted for both AL kappa and lambda patients. There was a significant correlation between the use of the Vlambda VI germ-line donor, 6a, and renal involvement as well as the Vlambda III gene, 3r, with soft-tissue AL. The use of a biased VL gene repertoire also correlated with clinical outcome, revealing important trends for predicting prognosis. The use of Vlambda II germ-line genes was associated with cardiac amyloidosis and affected survival adversely. The presence of multiple myeloma also correlated with a poor prognosis. The presence of renal disease, on the other hand, was associated with improved survival. Therefore, identification of the clonal VL gene in AL has important implications in determining clinical outcome.  (+info)

Simulations of human lysozyme: probing the conformations triggering amyloidosis. (5/67)

A natural mutant of human lysozyme, D67H, causes hereditary systemic nonneuropathic amyloidosis, which can be fatal. In this disease, insoluble beta-stranded fibrils (amyloids) are found in tissues stemming from the aggregation of partially folded intermediates of the mutant. In this study, we specifically compare the conformation and properties of the structures adopted from the induced unfolding, at elevated temperature, using molecular dynamics. To increase the sampling of the unfolding conformational landscape, three 5 ns trajectories are performed for each of the wild-type and mutant D67H proteins resulting in a total of 30 ns simulation. Our results show that the mutant unfolds slightly faster than the wild-type with both wild-type and mutant proteins losing most of their native secondary structure within the first 2 ns. They both develop random transient beta-strands across the whole polypeptide chain. Clustering analysis of all the conformations shows that a high population of the mutant protein conformations have a distorted beta-domain. This is consistent with experimental results suggesting that this region is pivotal in the formation of conformations prone to act as "seeds" for amyloid fiber formation.  (+info)

Identification of S-sulfonation and S-thiolation of a novel transthyretin Phe33Cys variant from a patient diagnosed with familial transthyretin amyloidosis. (6/67)

Familial transthyretin amyloidosis (ATTR) is an autosomal dominant disorder associated with a variant form of the plasma carrier protein transthyretin (TTR). Amyloid fibrils consisting of variant TTR, wild-type TTR, and TTR fragments deposit in tissues and organs. The diagnosis of ATTR relies on the identification of pathologic TTR variants in plasma of symptomatic individuals who have biopsy proven amyloid disease. Previously, we have developed a mass spectrometry-based approach, in combination with direct DNA sequence analysis, to fully identify TTR variants. Our methodology uses immunoprecipitation to isolate TTR from serum, and electrospray ionization and matrix-assisted laser desorption/ionization mass spectrometry (MS) peptide mapping to identify TTR variants and posttranslational modifications. Unambiguous identification of the amino acid substitution is performed using tandem MS (MS/MS) analysis and confirmed by direct DNA sequence analysis. The MS and MS/MS analyses also yield information about posttranslational modifications. Using this approach, we have recently identified a novel pathologic TTR variant. This variant has an amino acid substitution (Phe --> Cys) at position 33. In addition, like the Cys10 present in the wild type and in this variant, the Cys33 residue was both S-sulfonated and S-thiolated (conjugated to cysteine, cysteinylglycine, and glutathione). These adducts may play a role in the TTR fibrillogenesis.  (+info)

Safety of colchicine therapy during pregnancy. (7/67)

QUESTION: A 27-year-old patient in our clinic with familial Mediterranean fever (FMF) has been treated with colchicine for the last decade. She is planning her first pregnancy. What recommendations should we give her regarding use of colchicine before and during pregnancy, bearing in mind that discontinuation of colchicine could lead to complications from amyloidosis? ANSWER: Colchicine passes through the placenta in humans, is teratogenic in animals, and raises rates of male and female infertility. Based on several patients with chromosomal anomalies, some authorities recommend that patients who require colchicine therapy during pregnancy undergo amniocentesis with karyotyping. In contrast, an increasing body of evidence suggests that colchicine use throughout pregnancy carries no substantial teratogenic or mutagenic risk when used at recommended doses. Its use prevents febrile attacks of FMF and reduces the frequency of renal complications.  (+info)

Cysteine 10 is a key residue in amyloidogenesis of human transthyretin Val30Met. (8/67)

Type I familial amyloidotic polyneuropathy (FAP), a systemic amyloidosis, is characterized by aggregation of variant transthyretin (TTR Val30Met) into stable, insoluble fibrils. This aggregation is caused by genetic and environmental factors. Genetic factors have been studied extensively. However, little is known about environmental or physiological factors involved in the disease process, and their identification may be important for development of effective treatment. X-ray crystallography of normal and amyloidogenic human TTR Val30Met in type I FAP showed that the -SH side chain of cysteine at position 10 (Cys10) forms a hydrogen bond with Gly57 in normal TTR but not in TTR Val30Met. This result suggests a crucial role for the free Cys10 residue and possible involvement of physiological factors affecting Cys residue reactivity in TTR amyloidogenesis. To analyze amyloidogenesis in vivo, our group generated murine FAP models by transgenic technology, with human TTR Val30Met. The three lines of transgenic mice expressed amyloidogenic mutant TTR (Cys10/Met30), wild-type TTR (Cys10/Val30), and artificial Cys-free mutant TTR (Ser10/Met30). Histochemical investigation showed deposition of amyloid derived from human TTR only in amyloidogenic mutant TTR (Cys10/Met30) mice. Thus, the -SH residue in Cys10 plays a crucial role in TTR Val30Met amyloidogenesis in vivo. These data suggest the possibility of innovative treatment via physiological factors modulating Cys10 residue reactivity.  (+info)

Amyloidosis is a medical condition characterized by the abnormal accumulation of insoluble proteins called amyloid in various tissues and organs throughout the body. These misfolded protein deposits can disrupt the normal function of affected organs, leading to a range of symptoms depending on the location and extent of the amyloid deposition.

There are different types of amyloidosis, classified based on the specific proteins involved:

1. Primary (AL) Amyloidosis: This is the most common form, accounting for around 80% of cases. It results from the overproduction and misfolding of immunoglobulin light chains, typically by clonal plasma cells in the bone marrow. The amyloid deposits can affect various organs, including the heart, kidneys, liver, and nervous system.
2. Secondary (AA) Amyloidosis: This form is associated with chronic inflammatory diseases, such as rheumatoid arthritis, tuberculosis, or familial Mediterranean fever. The amyloid fibrils are composed of serum amyloid A protein (SAA), an acute-phase reactant produced during the inflammatory response. The kidneys are commonly affected in this type of amyloidosis.
3. Hereditary or Familial Amyloidosis: These forms are caused by genetic mutations that result in the production of abnormal proteins prone to misfolding and amyloid formation. Examples include transthyretin (TTR) amyloidosis, fibrinogen amyloidosis, and apolipoprotein AI amyloidosis. These forms can affect various organs, including the heart, nerves, and kidneys.
4. Dialysis-Related Amyloidosis: This form is seen in patients undergoing long-term dialysis for chronic kidney disease. The amyloid fibrils are composed of beta-2 microglobulin, a protein that accumulates due to impaired clearance during dialysis. The joints and bones are commonly affected in this type of amyloidosis.

The diagnosis of amyloidosis typically involves a combination of clinical evaluation, imaging studies, and tissue biopsy with the demonstration of amyloid deposition using special stains (e.g., Congo red). Treatment depends on the specific type and extent of organ involvement and may include supportive care, medications to target the underlying cause (e.g., chemotherapy, immunomodulatory agents), and organ transplantation in some cases.

Familial amyloidosis is a genetic disorder characterized by the buildup of abnormal protein deposits called amyloid fibrils in various tissues and organs throughout the body. These abnormal protein deposits can cause damage to the affected organs, leading to a variety of symptoms.

There are several types of familial amyloidosis, but the most common type is transthyretin-related hereditary amyloidosis (TTR-HA). This form of the disorder is caused by mutations in the TTR gene, which provides instructions for making a protein called transthyretin. Transthyretin is a transport protein that helps move thyroid hormones and vitamin A around the body. In TTR-HA, mutations in the TTR gene cause the transthyretin protein to misfold and form amyloid fibrils.

Symptoms of familial amyloidosis can vary widely depending on which organs are affected. Commonly affected organs include the heart, kidneys, nerves, and gastrointestinal tract. Symptoms may include:

* Heart problems such as arrhythmias (irregular heartbeat), heart failure, or cardiac conduction abnormalities
* Kidney problems such as proteinuria (protein in the urine) or kidney failure
* Nerve damage leading to numbness, tingling, or pain in the hands and feet, or autonomic nervous system dysfunction affecting digestion, bladder function, or blood pressure regulation
* Gastrointestinal problems such as diarrhea, constipation, nausea, vomiting, or abdominal pain

Familial amyloidosis is typically inherited in an autosomal dominant manner, meaning that a child has a 50% chance of inheriting the mutated gene from a parent with the disorder. However, some cases may be due to new (de novo) mutations and occur in people without a family history of the disorder.

Diagnosis of familial amyloidosis typically involves a combination of clinical evaluation, genetic testing, and tissue biopsy to confirm the presence of amyloid fibrils. Treatment may involve medications to manage symptoms, as well as liver transplantation or other experimental therapies aimed at reducing the production of abnormal proteins that form amyloid fibrils.

Amyloid is a term used in medicine to describe abnormally folded protein deposits that can accumulate in various tissues and organs of the body. These misfolded proteins can form aggregates known as amyloid fibrils, which have a characteristic beta-pleated sheet structure. Amyloid deposits can be composed of different types of proteins, depending on the specific disease associated with the deposit.

In some cases, amyloid deposits can cause damage to organs and tissues, leading to various clinical symptoms. Some examples of diseases associated with amyloidosis include Alzheimer's disease (where amyloid-beta protein accumulates in the brain), systemic amyloidosis (where amyloid fibrils deposit in various organs such as the heart, kidneys, and liver), and type 2 diabetes (where amyloid deposits form in the pancreas).

It's important to note that not all amyloid deposits are harmful or associated with disease. However, when they do cause problems, treatment typically involves managing the underlying condition that is leading to the abnormal protein accumulation.

Serum Amyloid A (SAA) protein is an acute phase protein produced primarily in the liver, although it can also be produced by other cells in response to inflammation. It is a member of the apolipoprotein family and is found in high-density lipoproteins (HDL) in the blood. SAA protein levels increase rapidly during the acute phase response to infection, trauma, or tissue damage, making it a useful biomarker for inflammation.

In addition to its role as an acute phase protein, SAA has been implicated in several disease processes, including atherosclerosis and amyloidosis. In amyloidosis, SAA can form insoluble fibrils that deposit in various tissues, leading to organ dysfunction. There are four subtypes of SAA in humans (SAA1, SAA2, SAA3, and SAA4), with SAA1 and SAA2 being the most responsive to inflammatory stimuli.

Prealbumin, also known as transthyretin, is a protein produced primarily in the liver and circulates in the blood. It plays a role in transporting thyroid hormones and vitamin A throughout the body. Prealbumin levels are often used as an indicator of nutritional status and liver function. Low prealbumin levels may suggest malnutrition or inflammation, while increased levels can be seen in certain conditions like hyperthyroidism. It is important to note that prealbumin levels should be interpreted in conjunction with other clinical findings and laboratory tests for a more accurate assessment of a patient's health status.

Immunoglobulin light chains are the smaller protein subunits of an immunoglobulin, also known as an antibody. They are composed of two polypeptide chains, called kappa (κ) and lambda (λ), which are produced by B cells during the immune response. Each immunoglobulin molecule contains either two kappa or two lambda light chains, in association with two heavy chains.

Light chains play a crucial role in the antigen-binding site of an antibody, where they contribute to the specificity and affinity of the interaction between the antibody and its target antigen. In addition to their role in immune function, abnormal production or accumulation of light chains can lead to various diseases, such as multiple myeloma and amyloidosis.

Familial Mediterranean Fever (FMF) is a hereditary inflammatory disorder that primarily affects people of Mediterranean ancestry, including populations from Turkey, Armenia, Arab countries, and Jewish communities from the Middle East. It is caused by mutations in the MEFV gene, which provides instructions for making a protein called pyrin or marenostrin.

The main features of FMF include recurrent episodes of fever, serositis (inflammation of the membranes lining the abdominal cavity, chest cavity, or heart), and polyserositis (inflammation affecting multiple serous membranes simultaneously). The attacks usually last between 12 and 72 hours and can be associated with severe abdominal pain, joint pain, and skin rashes.

The diagnosis of FMF is based on clinical criteria, family history, and genetic testing. Treatment typically involves the use of colchicine, an anti-inflammatory medication that helps prevent attacks and reduces the risk of long-term complications such as amyloidosis, a condition characterized by the buildup of abnormal protein deposits in various organs.

Early diagnosis and treatment of FMF are essential to prevent complications and improve quality of life for affected individuals.

Amyloid neuropathies are a group of peripheral nerve disorders caused by the abnormal accumulation of amyloid proteins in the nerves. Amyloid is a protein that can be produced in various diseases and can deposit in different organs, including nerves. When this occurs in the nerves, it can lead to damage and dysfunction, resulting in symptoms such as numbness, tingling, pain, and weakness in the affected limbs.

There are several types of amyloid neuropathies, with the two most common being:

1. Transthyretin (TTR)-related hereditary amyloidosis: This is an inherited disorder caused by mutations in the TTR gene, which leads to the production of abnormal TTR protein that can form amyloid deposits in various organs, including nerves.
2. Immunoglobulin light chain (AL) amyloidosis: This is a disorder in which abnormal plasma cells produce excessive amounts of immunoglobulin light chains, which can form amyloid deposits in various organs, including nerves.

The diagnosis of amyloid neuropathies typically involves a combination of clinical evaluation, nerve conduction studies, and tissue biopsy to confirm the presence of amyloid deposits. Treatment options depend on the underlying cause of the disorder and may include medications, chemotherapy, stem cell transplantation, or supportive care to manage symptoms.

Congo Red is a synthetic diazo dye that is commonly used in histology and pathology for stainings and tests. It is particularly useful in identifying amyloid deposits in tissues, which are associated with various diseases such as Alzheimer's disease, type 2 diabetes, and systemic amyloidosis.

When Congo Red binds to amyloid fibrils, it exhibits a characteristic apple-green birefringence under polarized light microscopy. Additionally, Congo Red stained amyloid deposits show a shift in their emission spectrum when excited with circularly polarized light, a phenomenon known as dichroism. These properties make Congo Red a valuable tool for the diagnosis and study of amyloidosis and other protein misfolding disorders.

It is important to note that Congo Red staining should be performed with care, as it can be toxic and carcinogenic if not handled properly.

Familial amyloid neuropathies are a group of inherited disorders characterized by the accumulation of abnormal deposits of amyloid proteins in various tissues and organs of the body. These abnormal deposits can cause damage to nerves, leading to a peripheral neuropathy that affects sensation, movement, and organ function.

There are several types of familial amyloid neuropathies, each caused by different genetic mutations. The most common type is known as transthyretin-related hereditary amyloidosis (TTR-HA), which is caused by mutations in the TTR gene. Other types include apolipoprotein A1-related hereditary amyloidosis (APOA1-HA) and gelsolin-related amyloidosis (AGel-HA).

Symptoms of familial amyloid neuropathies can vary depending on the type and severity of the disorder. Common symptoms include:

* Numbness, tingling, or pain in the hands and feet
* Weakness or loss of muscle strength in the legs and arms
* Autonomic nervous system dysfunction, leading to problems with digestion, heart rate, blood pressure, and temperature regulation
* Carpal tunnel syndrome
* Eye abnormalities, such as vitreous opacities or retinal deposits
* Kidney disease

Familial amyloid neuropathies are typically inherited in an autosomal dominant manner, meaning that a child has a 50% chance of inheriting the mutated gene from an affected parent. Diagnosis is usually made through genetic testing and confirmation of the presence of amyloid deposits in tissue samples.

Treatment for familial amyloid neuropathies typically involves managing symptoms and slowing the progression of the disease. This may include medications to control pain, physical therapy to maintain muscle strength and mobility, and devices such as braces or wheelchairs to assist with mobility. In some cases, liver transplantation may be recommended to remove the source of the mutated transthyretin protein.

Cardiomyopathies are a group of diseases that affect the heart muscle, leading to mechanical and/or electrical dysfunction. The American Heart Association (AHA) defines cardiomyopathies as "a heterogeneous group of diseases of the myocardium associated with mechanical and/or electrical dysfunction that usually (but not always) exhibit inappropriate ventricular hypertrophy or dilatation and frequently lead to heart failure."

There are several types of cardiomyopathies, including:

1. Dilated cardiomyopathy (DCM): This is the most common type of cardiomyopathy, characterized by an enlarged left ventricle and impaired systolic function, leading to heart failure.
2. Hypertrophic cardiomyopathy (HCM): In this type, there is abnormal thickening of the heart muscle, particularly in the septum between the two ventricles, which can obstruct blood flow and increase the risk of arrhythmias.
3. Restrictive cardiomyopathy (RCM): This is a rare form of cardiomyopathy characterized by stiffness of the heart muscle, impaired relaxation, and diastolic dysfunction, leading to reduced filling of the ventricles and heart failure.
4. Arrhythmogenic right ventricular cardiomyopathy (ARVC): In this type, there is replacement of the normal heart muscle with fatty or fibrous tissue, primarily affecting the right ventricle, which can lead to arrhythmias and sudden cardiac death.
5. Unclassified cardiomyopathies: These are conditions that do not fit into any of the above categories but still significantly affect the heart muscle and function.

Cardiomyopathies can be caused by genetic factors, acquired conditions (e.g., infections, toxins, or autoimmune disorders), or a combination of both. The diagnosis typically involves a comprehensive evaluation, including medical history, physical examination, electrocardiogram (ECG), echocardiography, cardiac magnetic resonance imaging (MRI), and sometimes genetic testing. Treatment depends on the type and severity of the condition but may include medications, lifestyle modifications, implantable devices, or even heart transplantation in severe cases.

Beta-2 microglobulin (β2M) is a small protein that is a component of the major histocompatibility complex class I molecule, which plays a crucial role in the immune system. It is found on the surface of almost all nucleated cells in the body and is involved in presenting intracellular peptides to T-cells for immune surveillance.

β2M is produced at a relatively constant rate by cells throughout the body and is freely filtered by the glomeruli in the kidneys. Under normal circumstances, most of the filtrated β2M is reabsorbed and catabolized in the proximal tubules of the nephrons. However, when the glomerular filtration rate (GFR) is decreased, as in chronic kidney disease (CKD), the reabsorption capacity of the proximal tubules becomes overwhelmed, leading to increased levels of β2M in the blood and its subsequent appearance in the urine.

Elevated serum and urinary β2M levels have been associated with various clinical conditions, such as CKD, multiple myeloma, autoimmune disorders, and certain infectious diseases. Measuring β2M concentrations can provide valuable information for diagnostic, prognostic, and monitoring purposes in these contexts.

Serum Amyloid P-component (SAP) is a protein that is normally present in the blood and other bodily fluids. It is a part of the larger family of pentraxin proteins, which are involved in the innate immune response, meaning they provide immediate defense against foreign invaders without needing to adapt over time. SAP plays a role in inflammation, immune complex clearance, and complement activation.

In the context of amyloidosis, SAP binds to misfolded proteins called amyloid fibrils, which can deposit in various tissues and organs, leading to their dysfunction and failure. The accumulation of these amyloid fibrils with SAP is a hallmark of systemic amyloidosis.

It's important to note that while SAP plays a role in the pathogenesis of amyloidosis, it is not directly responsible for causing the disease. Instead, its presence can serve as a useful marker for diagnosing and monitoring the progression of amyloidosis.

Nephrotic syndrome is a group of symptoms that indicate kidney damage, specifically damage to the glomeruli—the tiny blood vessel clusters in the kidneys that filter waste and excess fluids from the blood. The main features of nephrotic syndrome are:

1. Proteinuria (excess protein in urine): Large amounts of a protein called albumin leak into the urine due to damaged glomeruli, which can't properly filter proteins. This leads to low levels of albumin in the blood, causing fluid buildup and swelling.
2. Hypoalbuminemia (low blood albumin levels): As albumin leaks into the urine, the concentration of albumin in the blood decreases, leading to hypoalbuminemia. This can cause edema (swelling), particularly in the legs, ankles, and feet.
3. Edema (fluid retention and swelling): With low levels of albumin in the blood, fluids move into the surrounding tissues, causing swelling or puffiness. The swelling is most noticeable around the eyes, face, hands, feet, and abdomen.
4. Hyperlipidemia (high lipid/cholesterol levels): The kidneys play a role in regulating lipid metabolism. Damage to the glomeruli can lead to increased lipid production and high cholesterol levels in the blood.

Nephrotic syndrome can result from various underlying kidney diseases, such as minimal change disease, membranous nephropathy, or focal segmental glomerulosclerosis. Treatment depends on the underlying cause and may include medications to control inflammation, manage high blood pressure, and reduce proteinuria. In some cases, dietary modifications and lifestyle changes are also recommended.

Paraproteinemias refer to the presence of abnormal levels of paraproteins in the blood. Paraproteins are immunoglobulins (antibodies) produced by plasma cells, which are a type of white blood cell found in the bone marrow. In healthy individuals, paraproteins play a role in the immune system's response to infection and disease. However, in certain conditions, such as multiple myeloma, monoclonal gammopathy of undetermined significance (MGUS), and Waldenstrom macroglobulinemia, plasma cells produce excessive amounts of a single type of paraprotein, leading to its accumulation in the blood.

Paraproteinemias can cause various symptoms depending on the level of paraproteins present and their impact on organs and tissues. These symptoms may include fatigue, weakness, numbness or tingling in the extremities, bone pain, recurrent infections, and kidney problems. In some cases, paraproteinemias may not cause any symptoms and may only be detected during routine blood tests.

It is important to note that while paraproteinemias are often associated with plasma cell disorders, they can also occur in other conditions such as chronic inflammation or autoimmune diseases. Therefore, further testing and evaluation are necessary to determine the underlying cause of paraproteinemia and develop an appropriate treatment plan.

Tracheal diseases refer to a group of medical conditions that affect the trachea, also known as the windpipe. The trachea is a tube-like structure made up of rings of cartilage and smooth muscle, which extends from the larynx (voice box) to the bronchi (airways leading to the lungs). Its primary function is to allow the passage of air to and from the lungs.

Tracheal diseases can be categorized into several types, including:

1. Tracheitis: Inflammation of the trachea, often caused by viral or bacterial infections.
2. Tracheal stenosis: Narrowing of the trachea due to scarring, inflammation, or compression from nearby structures such as tumors or goiters.
3. Tracheomalacia: Weakening and collapse of the tracheal walls, often seen in newborns and young children but can also occur in adults due to factors like chronic cough, aging, or connective tissue disorders.
4. Tracheoesophageal fistula: An abnormal connection between the trachea and the esophagus, which can lead to respiratory complications and difficulty swallowing.
5. Tracheal tumors: Benign or malignant growths that develop within the trachea, obstructing airflow and potentially leading to more severe respiratory issues.
6. Tracheobronchial injury: Damage to the trachea and bronchi, often caused by trauma such as blunt force or penetrating injuries.
7. Congenital tracheal abnormalities: Structural defects present at birth, including complete tracheal rings, which can cause narrowing or collapse of the airway.

Symptoms of tracheal diseases may include cough, wheezing, shortness of breath, chest pain, and difficulty swallowing. Treatment options depend on the specific condition and its severity but may involve medications, surgery, or other interventions to alleviate symptoms and improve respiratory function.

Kidney disease, also known as nephropathy or renal disease, refers to any functional or structural damage to the kidneys that impairs their ability to filter blood, regulate electrolytes, produce hormones, and maintain fluid balance. This damage can result from a wide range of causes, including diabetes, hypertension, glomerulonephritis, polycystic kidney disease, lupus, infections, drugs, toxins, and congenital or inherited disorders.

Depending on the severity and progression of the kidney damage, kidney diseases can be classified into two main categories: acute kidney injury (AKI) and chronic kidney disease (CKD). AKI is a sudden and often reversible loss of kidney function that occurs over hours to days, while CKD is a progressive and irreversible decline in kidney function that develops over months or years.

Symptoms of kidney diseases may include edema, proteinuria, hematuria, hypertension, electrolyte imbalances, metabolic acidosis, anemia, and decreased urine output. Treatment options depend on the underlying cause and severity of the disease and may include medications, dietary modifications, dialysis, or kidney transplantation.

Macroglossia is a medical term that refers to an abnormally large tongue in relation to the size of the oral cavity. It can result from various conditions, including certain genetic disorders (such as Down syndrome and Beckwith-Wiedemann syndrome), hormonal disorders (such as acromegaly), inflammatory diseases (such as amyloidosis), tumors or growths on the tongue, or neurological conditions. Macroglossia can cause difficulties with speaking, swallowing, and breathing, particularly during sleep. Treatment depends on the underlying cause but may include corticosteroids, radiation therapy, surgery, or a combination of these approaches.

Amyloidogenic proteins are misfolded proteins that can form amyloid fibrils, which are insoluble protein aggregates with a characteristic cross-beta sheet quaternary structure. These amyloid fibrils can accumulate in various tissues and organs, leading to the formation of amyloid deposits. The accumulation of amyloidogenic proteins and the resulting amyloid deposits have been associated with several neurodegenerative diseases, including Alzheimer's disease, Parkinson's disease, and Huntington's disease, as well as systemic amyloidoses.

In Alzheimer's disease, for example, the amyloidogenic protein is beta-amyloid, which is produced from the proteolytic processing of the amyloid precursor protein (APP). In Parkinson's disease, the amyloidogenic protein is alpha-synuclein, which forms the main component of Lewy bodies.

It's important to note that not all misfolded proteins are necessarily amyloidogenic, and not all amyloid fibrils are associated with disease. Some amyloid fibrils can have functional roles in normal physiological processes.

Melphalan is an antineoplastic agent, specifically an alkylating agent. It is used in the treatment of multiple myeloma and other types of cancer. The medical definition of Melphalan is:

A nitrogen mustard derivative that is used as an alkylating agent in the treatment of cancer, particularly multiple myeloma and ovarian cancer. Melphalan works by forming covalent bonds with DNA, resulting in cross-linking of the double helix and inhibition of DNA replication and transcription. This ultimately leads to cell cycle arrest and apoptosis (programmed cell death) in rapidly dividing cells, such as cancer cells.

Melphalan is administered orally or intravenously, and its use is often accompanied by other anticancer therapies, such as radiation therapy or chemotherapy. Common side effects of Melphalan include nausea, vomiting, diarrhea, and bone marrow suppression, which can lead to anemia, neutropenia, and thrombocytopenia. Other potential side effects include hair loss, mucositis, and secondary malignancies.

It is important to note that Melphalan should be used under the close supervision of a healthcare professional, as it can cause serious adverse reactions if not administered correctly.

Bence Jones protein is a type of immunoglobulin light chain that can be detected in the urine or blood of some patients with certain diseases, most notably multiple myeloma. It's named after Henry Bence Jones, a 19th-century English physician who first described it.

These proteins are produced by malignant plasma cells, which are a type of white blood cell found in the bone marrow. In multiple myeloma, these cancerous cells multiply and produce abnormal amounts of immunoglobulins, leading to the overproduction of Bence Jones proteins.

When these proteins are excreted in the urine, they can cause damage to the kidneys, leading to kidney dysfunction or failure. Therefore, the detection of Bence Jones protein in the urine can be a sign of multiple myeloma or other related diseases. However, it's important to note that not all patients with multiple myeloma will have Bence Jones proteins in their urine.

A biopsy is a medical procedure in which a small sample of tissue is taken from the body to be examined under a microscope for the presence of disease. This can help doctors diagnose and monitor various medical conditions, such as cancer, infections, or autoimmune disorders. The type of biopsy performed will depend on the location and nature of the suspected condition. Some common types of biopsies include:

1. Incisional biopsy: In this procedure, a surgeon removes a piece of tissue from an abnormal area using a scalpel or other surgical instrument. This type of biopsy is often used when the lesion is too large to be removed entirely during the initial biopsy.

2. Excisional biopsy: An excisional biopsy involves removing the entire abnormal area, along with a margin of healthy tissue surrounding it. This technique is typically employed for smaller lesions or when cancer is suspected.

3. Needle biopsy: A needle biopsy uses a thin, hollow needle to extract cells or fluid from the body. There are two main types of needle biopsies: fine-needle aspiration (FNA) and core needle biopsy. FNA extracts loose cells, while a core needle biopsy removes a small piece of tissue.

4. Punch biopsy: In a punch biopsy, a round, sharp tool is used to remove a small cylindrical sample of skin tissue. This type of biopsy is often used for evaluating rashes or other skin abnormalities.

5. Shave biopsy: During a shave biopsy, a thin slice of tissue is removed from the surface of the skin using a sharp razor-like instrument. This technique is typically used for superficial lesions or growths on the skin.

After the biopsy sample has been collected, it is sent to a laboratory where a pathologist will examine the tissue under a microscope and provide a diagnosis based on their findings. The results of the biopsy can help guide further treatment decisions and determine the best course of action for managing the patient's condition.

"Acinonyx" is a genus name that refers to a single species of big cat, the cheetah. The correct medical definition of "Acinonyx" is:

* Acinonyx jubatus: a large, slender wild cat that is known for its incredible speed and unique adaptations for running. It is the fastest land animal, capable of reaching speeds up to 60-70 miles per hour. The cheetah's body is built for speed, with long legs, a flexible spine, and a non-retractable claw that provides traction while running.

The cheetah's habitat ranges from the savannas of Africa to the deserts of Iran. It primarily hunts medium-sized ungulates, such as gazelles and wildebeest. The cheetah's population has been declining due to habitat loss, human-wildlife conflict, and illegal wildlife trade. Conservation efforts are underway to protect this iconic species and its habitat.

Immunoglobulin lambda-chains (Igλ) are one type of light chain found in the immunoglobulins, also known as antibodies. Antibodies are proteins that play a crucial role in the immune system's response to foreign substances, such as bacteria and viruses.

Immunoglobulins are composed of two heavy chains and two light chains, which are interconnected by disulfide bonds. There are two types of light chains: kappa (κ) and lambda (λ). Igλ chains are one type of light chain that can be found in association with heavy chains to form functional antibodies.

Igλ chains contain a variable region, which is responsible for recognizing and binding to specific antigens, and a constant region, which determines the class of the immunoglobulin (e.g., IgA, IgD, IgE, IgG, or IgM).

In humans, approximately 60% of all antibodies contain Igλ chains, while the remaining 40% contain Igκ chains. The ratio of Igλ to Igκ chains can vary depending on the type of immunoglobulin and its function in the immune response.

Gelsolin is a protein that plays a role in the regulation of actin, which is a major component of the cytoskeleton in cells. The gelsolin protein can bind to and sever actin filaments, as well as cap their plus ends, preventing further growth. This regulation of actin dynamics is important for various cellular processes, including cell motility, wound healing, and the immune response.

There are two forms of gelsolin in humans: plasma gelsolin, which is found in blood plasma, and cytoplasmic gelsolin, which is found in the cytoplasm of cells. Plasma gelsolin has been shown to have anti-inflammatory properties and may play a role in protecting against sepsis and other inflammatory conditions.

Mutations in the gene that encodes gelsolin can lead to various genetic disorders, including familial amyloidosis, Finnish type (FAF), which is characterized by progressive nerve damage and muscle weakness.

Factor X deficiency, also known as Stuart-Prower factor deficiency, is a rare bleeding disorder that affects the body's ability to form blood clots. It is caused by a mutation in the gene that provides instructions for making coagulation factor X, a protein involved in the coagulation cascade, which is a series of chemical reactions that lead to the formation of a blood clot.

People with factor X deficiency may experience excessive bleeding after injury or surgery, and they may also have an increased risk of spontaneous bleeding, such as nosebleeds, heavy menstrual periods, and joint bleeds. The severity of the condition can vary widely, from mild to severe, depending on the level of factor X activity in the blood.

Factor X deficiency can be inherited or acquired. Inherited forms of the disorder are caused by mutations in the F10 gene and are usually present at birth. Acquired forms of the disorder can develop later in life due to conditions such as liver disease, vitamin K deficiency, or the use of certain medications that interfere with coagulation.

Treatment for factor X deficiency typically involves replacement therapy with fresh frozen plasma or recombinant factor X concentrates to help restore normal clotting function. In some cases, other treatments such as antifibrinolytic agents or desmopressin may also be used to manage bleeding symptoms.

Genetic skin diseases are a group of disorders caused by mutations or alterations in the genetic material (DNA), which can be inherited from one or both parents. These mutations affect the structure, function, or development of the skin and can lead to various conditions with different symptoms, severity, and prognosis.

Some examples of genetic skin diseases include:

1. Epidermolysis Bullosa (EB): A group of disorders characterized by fragile skin and mucous membranes that blister and tear easily, leading to painful sores and wounds. There are several types of EB, each caused by mutations in different genes involved in anchoring the epidermis to the dermis.
2. Ichthyosis: A family of genetic disorders characterized by dry, thickened, scaly, or rough skin. The severity and symptoms can vary widely, depending on the specific type and underlying genetic cause.
3. Neurofibromatosis: A group of conditions caused by mutations in the NF1 gene, which regulates cell growth and division. The most common types, NF1 and NF2, are characterized by the development of benign tumors called neurofibromas on the skin and nerves, as well as other symptoms affecting various organs and systems.
4. Tuberous Sclerosis Complex (TSC): A genetic disorder caused by mutations in the TSC1 or TSC2 genes, which control cell growth and division. TSC is characterized by the development of benign tumors in multiple organs, including the skin, brain, heart, kidneys, and lungs.
5. Xeroderma Pigmentosum (XP): A rare genetic disorder caused by mutations in genes responsible for repairing DNA damage from ultraviolet (UV) radiation. People with XP are extremely sensitive to sunlight and have a high risk of developing skin cancer and other complications.
6. Incontinentia Pigmenti (IP): A genetic disorder that affects the development and growth of skin, hair, nails, teeth, and eyes. IP is caused by mutations in the IKBKG gene and primarily affects females.
7. Darier's Disease: An inherited skin disorder characterized by greasy, crusted, keratotic papules and plaques, usually located on the trunk, scalp, and seborrheic areas of the body. Darier's disease is caused by mutations in the ATP2A2 gene.

These are just a few examples of genetic skin disorders. There are many more, each with its unique set of symptoms, causes, and treatments. If you or someone you know has a genetic skin disorder, it is essential to consult with a dermatologist or other healthcare professional for proper diagnosis and treatment.

A fatal outcome is a term used in medical context to describe a situation where a disease, injury, or illness results in the death of an individual. It is the most severe and unfortunate possible outcome of any medical condition, and is often used as a measure of the severity and prognosis of various diseases and injuries. In clinical trials and research, fatal outcome may be used as an endpoint to evaluate the effectiveness and safety of different treatments or interventions.

Multiple myeloma is a type of cancer that forms in a type of white blood cell called a plasma cell. Plasma cells help your body fight infection by producing antibodies. In multiple myeloma, cancerous plasma cells accumulate in the bone marrow and crowd out healthy blood cells. Rather than producing useful antibodies, the cancer cells produce abnormal proteins that can cause complications such as kidney damage, bone pain and fractures.

Multiple myeloma is a type of cancer called a plasma cell neoplasm. Plasma cell neoplasms are diseases in which there is an overproduction of a single clone of plasma cells. In multiple myeloma, this results in the crowding out of normal plasma cells, red and white blood cells and platelets, leading to many of the complications associated with the disease.

The abnormal proteins produced by the cancer cells can also cause damage to organs and tissues in the body. These abnormal proteins can be detected in the blood or urine and are often used to monitor the progression of multiple myeloma.

Multiple myeloma is a relatively uncommon cancer, but it is the second most common blood cancer after non-Hodgkin lymphoma. It typically occurs in people over the age of 65, and men are more likely to develop multiple myeloma than women. While there is no cure for multiple myeloma, treatments such as chemotherapy, radiation therapy, and stem cell transplantation can help manage the disease and its symptoms, and improve quality of life.

An encyclopedia is a comprehensive reference work containing articles on various topics, usually arranged in alphabetical order. In the context of medicine, a medical encyclopedia is a collection of articles that provide information about a wide range of medical topics, including diseases and conditions, treatments, tests, procedures, and anatomy and physiology. Medical encyclopedias may be published in print or electronic formats and are often used as a starting point for researching medical topics. They can provide reliable and accurate information on medical subjects, making them useful resources for healthcare professionals, students, and patients alike. Some well-known examples of medical encyclopedias include the Merck Manual and the Stedman's Medical Dictionary.

Fibrinogen is a soluble protein present in plasma, synthesized by the liver. It plays an essential role in blood coagulation. When an injury occurs, fibrinogen gets converted into insoluble fibrin by the action of thrombin, forming a fibrin clot that helps to stop bleeding from the injured site. Therefore, fibrinogen is crucial for hemostasis, which is the process of stopping bleeding and starting the healing process after an injury.

Afibrinogenemia is a rare genetic disorder characterized by the complete absence or severely decreased levels of fibrinogen, a protein involved in blood clotting. This condition leads to an increased risk of excessive bleeding due to the inability to form proper blood clots. It is caused by mutations in the genes that provide instructions for making the three chains (Aα, Bβ, and γ) that make up the fibrinogen protein. Inheritance is autosomal recessive, meaning an individual must inherit two copies of the defective gene, one from each parent, to have the condition.

... is a form of amyloidosis primarily presenting in the kidney. It is associated most commonly with ... March 2005). "Underdiagnosed amyloidosis: amyloidosis of lysozyme variant". Am. J. Med. 118 (3): 321-2. doi:10.1016/j.amjmed. ... January 2006). "Lysozyme amyloidosis: report of 4 cases and a review of the literature". Medicine (Baltimore). 85 (1): 66-73. ... August 1992). "Apolipoprotein AI mutation Arg-60 causes autosomal dominant amyloidosis". Proc. Natl. Acad. Sci. U.S.A. 89 (16 ...
... (FAF), also called hereditary gelsolin amyloidosis and AGel amyloidosis (AGel), is an ... "The role of gelsolin domain 3 in familial amyloidosis (Finnish type)". Proceedings of the National Academy of Sciences. 116 (28 ... "Elucidating the mechanism of familial amyloidosis- Finnish type: NMR studies of human gelsolin domain 2". Proceedings of the ... Familial amyloid neuropathy type IV Familial amyloidotic polyneuropathy (FAP) type IV Lattice corneal dystrophy, gelsolin type ...
The familial amyloid neuropathies (or familial amyloidotic neuropathies, neuropathic heredofamilial amyloidosis, familial ... Liver transplantation has proven to be effective for ATTR familial amyloidosis due to Val30Met mutation. In 2011 the European ... Fibrinogen, apolipoprotein A1, and lysozyme are associated with a closely related condition, familial visceral amyloidosis. ... Senile systemic amyloidosis [abbreviated "SSA"] is also associated with transthyretin aggregation.) "FAP-III" is also known as ...
Thus, Senile systemic amyloidosis and familial amyloid polyneuropathy are often treatable diseases that are misdiagnosed. ... Senile systemic amyloidosis presenting with heart failure: a comparison with light chain-associated amyloidosis. Arch Intern ... The onset of FAC caused by aggregation of the V122I mutation and wild-type TTR, and senile systemic amyloidosis caused by the ... Familial amyloid cardiomyopathy (FAC), or transthyretin amyloid cardiomyopathy (ATTR-CM) results from the aggregation and ...
"Familial Danish Dementia: A Novel Form of Cerebral Amyloidosis Associated with Deposition of Both Amyloid-Dan and Amyloid-Beta ... Familial Danish Dementia has been reported in a single family spanning three generations, with there being nine reported cases ... first described Familial Danish Dementia as heredopathia opthalmo-oto-encephalica. It was discovered in 9 members of a Danish ... "ADan amyloidosis - About the Disease". rarediseases.info.nih.gov. Retrieved 22 July 2023. Paul, Robert H. (2007-11-17). ...
... familial, and localized amyloidosis. The modern era of amyloidosis classification began in the late 1960s with the development ... Congo Red Amyloidosis, blood vessels, H&E Amyloidosis, lymph node, H&E Amyloidosis, lymph node, polarizer Cardiac amyloidosis. ... including the Amyloidosis Research Consortium, Amyloidosis Foundation, Amyloidosis Support Groups, and Australian Amyloidosis ... Descriptive terms such as primary amyloidosis, secondary amyloidosis, and others (e.g., senile amyloidosis), which are not ...
Prevention of Amyloidosis in Familial Mediterranean Fever with Colchicine. A Case-Control Study in Armenia. Medical Principles ... Khachadurian AK, Armenian HK: Familial Paroxysmal Polyserositis. Mode of Inheritance and Incidence of Amyloidosis. Proceedings ... Khachadurian AK, Armenian HK: The Management of Familial Paroxysmal Polyserositis (Familial Mediterranean Fever). Experience ... Familial aggregation of fainting in a case-control study of neurally mediated hypotension patients who present with unexplained ...
Partington MW, Marriott PJ, Prentice RS, Cavaglia A, Simpson NE (1981). "Familial cutaneous amyloidosis with systemic ...
Muckle TJ (April 1962). "Urticaria, deafness, and amyloidosis: a new heredo-familial syndrome". The Quarterly Journal of ... In addition, the prolonged inflammation can lead to deposition of proteins in the kidney, a condition known as amyloidosis.[ ... MWS is closely related to two other syndromes, familial cold urticaria and neonatal onset multisystem inflammatory disease-in ... Familial cold urticaria, a similar disease List of cutaneous conditions NOMID, a similar disease Urticarial syndromes CINCA ...
... has multiple sub-types including light chain, familial, and senile. One of the most studied types is light ... This type of amyloidosis can be identified by genetic testing for protein mutation. For the diagnosis of familial cardiac ... For familial amyloidosis, ACE-inhibitors and beta-blockers can be prescribed if there is no autonomic neuropathy. Suppression ... The vast majority of familial cardiac amyloidosis still present after the age of 60. A common mutation is the TTR gene mutation ...
Familial amyloidosis-Finnish type is associated with gelsolin amyloid (AGel). The vascular amyloid pathology characteristic of ... In familial forms of CAA, the cause of Aβ build up is likely due to increased production rather than poor clearance. Mutations ... The amyloid material is only found in the brain and as such the disease is not related to other forms of amyloidosis. CAA is ... Several familial variants exist. The condition is usually associated with amyloid beta. However, there are types involving ...
January 2008). "Oncostatin M receptor-beta mutations underlie familial primary localized cutaneous amyloidosis". Am. J. Hum. ... Primary cutaneous amyloidosis is a form of amyloidosis associated with oncostatin M receptor. This type of amyloidosis has been ... deposits Lichen amyloidosis on a 56-year-old male's leg Lichen amyloidosis on a 56-year-old male's leg Nodular amyloidosis is a ... and provide support to the theory that these two variants of amyloidosis exist on the same disease spectrum. Lichen amyloidosis ...
"Oncostatin M receptor-beta mutations underlie familial primary localized cutaneous amyloidosis". American Journal of Human ... The oncostatin M receptor is associated with primary cutaneous amyloidosis. OSM signaling via the OSMR is believed to play an ...
One of several such mutations leads to Finnish Familial Amyloidosis, a disorder in which pGSN becomes more conformationally ... "The role of gelsolin domain 3 in familial amyloidosis (Finnish type)". Proceedings of the National Academy of Sciences. 116 (28 ...
Liver transplant can treat amyloidosis if it is related to familial transthyretin. Outcomes for amyloid cardiomyopathy are ... 66-79, doi:10.1016/b978-0-12-809657-4.11051-8, ISBN 978-0-12-805154-2, retrieved 2020-11-27 "Cardiac amyloidosis: MedlinePlus ... Chemotherapy can treat amyloidosis if it is related to immunoglobulins. ... Amyloidosis and Other Protein Deposition Diseases", Emery and Rimoin's Principles and Practice of Medical Genetics, Oxford: ...
Familial transthyretin amyloidosis Fetal death and perinatal death caused by genetic heterogeneity. Microphthalmia. "diagram ... familial Mediterranean fever fmf in east block and Libya Morocco, beta thalassemia in all countries, g6dh deficiency all ... Familial Mediterranean fever, Fragile X syndrome, Gaucher disease, Glucose 6 phosphatase dihedrogenase deficiency, Hereditary ...
This accumulation leads over time to one form of familial renal amyloidosis. Plasma fibrinogen levels are similar to that seen ... Hereditary fibrinogen Aα-Chain amyloidosis is an autosomal dominant extremely rare inherited disorder caused by a mutation in ... Fibrinogen Aα-Chain amyloidosis has not associated with abnormal bleeding or thrombosis. Acquired dysfibrinogenemia is a rare ...
Amyloidosis such as familial amyloid neuropathy, AL amyloidosis, and AA amyloidosis [publication pending]. During the course of ... Castro, J.; Costa, J.; de Castro, I.; & Conceição, I. (2018). "Electrochemical skin conductance in hereditary amyloidosis ... and assessment of sweat disturbances is routine in the evaluation of amyloidosis. ESC may provide a measure of subclinical ... in the assessment of patients with familial amyloid polyneuropathy". Clinical Neurophysiology. 129 (8): 1565-1569. doi:10.1016/ ...
... which causes familial amyloid polyneuropathy, familial amyloid cardiomyopathy, and senile systemic amyloidosis; aggregation- ... Molecular Tweezers Targeting Transthyretin Amyloidosis. Neurotherapeutics. 2014; 11: 450-461. G Herzog, MD Shmueli, L Levi, L ...
Shar Peis can be affected by glomerular amyloidosis caused by deposition of amyloid in the kidneys and occurs secondary to Shar ... Familial renal disease is an uncommon cause of kidney failure in dogs and cats. Most causes are breed-related (familial) and ... A list of familial kidney diseases by dog and cat breeds is found below. Basenjis can be affected by a type of kidney tubular ... Lees G, Helman R, Homco L, Millichamp N, Hunter J, Frey M (1998). "Early diagnosis of familial nephropathy in English cocker ...
Nephrol Dial Transplant 22(1):272-5. Kiuru S. (1998) Gelsolin-related familial amyloidosis, Finnish type (FAF), and its ... In addition to the classic manifestations of Finnish type Familial Amyloidosis, cutis laxa, progressive peripheral neuropathy ... 2007) Amyloidosis-related nephrotic syndrome due to a G654A gelsolin mutation: the first report from the Middle East. ... Hereditary gelsolin amyloidosis has originally been reported by Finnish ophthalmologist Jouko Meretoja and is known as Meretoja ...
"Amyloidosis in familial Mediterranean fever patients: correlation with MEFV genotype and SAA1 and MICA polymorphisms effects". ... "The contribution of genotypes at the MEFV and SAA1 loci to amyloidosis and disease severity in patients with familial ... Some evidence suggests that another gene, called SAA1, can further modify the risk of developing amyloidosis among people with ... Fever and inflammation in the abdomen, chest, joints, or skin are signs of familial Mediterranean fever. Pyrin forms an ...
Familial renal amyloidosis or AA amyloidosis, a kidney disorder due to a mutation in the AA amyloid protein gene, has been seen ... Niewold TA, van der Linde-Sipman JS, Murphy C, Tooten PC, Gruys E (September 1999). "Familial amyloidosis in cats: Siamese and ...
... while classified as a form of systemic amyloidosis, almost exclusively manifests clinically as renal amyloidosis. No familial ... LECT2 amyloidosis can be distinguished from AL amyloidosis, the most common form of amyloidosis (~85% of total cases), by ... the first and second most common forms the disorder were AL amyloidosis and AA amyloidosis, respectively. Amyloidosis is a ... LECT2 Amyloidosis (ALECT2) is a form of amyloidosis caused by the LECT2 protein. It was found to be the third most common (~3% ...
Prevention of amyloidosis is sometimes used in dogs with recurring episodes of Shar Pei fever. Colchicine and dimethyl ... Shar Pei fever (also called familial Shar Pei fever or FSF) is a condition seen in Shar Pei characterized by recurring fever ... It is similar to familial Mediterranean fever in humans. The cause is unknown, but it is thought to be inherited. Shar Pei ... The prognosis is guarded for Shar Pei that develop amyloidosis. Ettinger, Stephen J.; Feldman, Edward C. (1995). Textbook of ...
... hereditary transthyretin amyloidosis, familial amyloid polyneuropathy (FAP), and familial amyloid cardiomyopathy (FAC). TTR ... Zeldenrust SR, Benson MD (2010). "Familial and senile amyloidosis caused by transthyretin". In Ramirez-Alvarado M, Kelly JW, ... GeneReviews/NIH/NCBI/UW entry on Familial Transthyretin Amyloidosis (Articles with short description, Short description is ... Treatment of familial (hereditary) TTR amyloid disease has historically relied on liver transplantation as a crude form of gene ...
Volanesorsen was approved by the European Medicines Agency (EMA) for the treatment of familial chylomicronaemia syndrome in May ... Inotersen received FDA approval for the treatment of hereditary transthyretin-mediated amyloidosis in October 2018. The ... In January 2013 mipomersen (marketed as Kynamro) was approved by the FDA for the treatment of homozygous familial ... familial chylomicronemia syndrome, frontotemporal dementia, Fuchs' dystrophy, hepatitis B, hereditary angioedema, hypertension ...
During his second term, Governor Casey was diagnosed with Appalachian familial amyloidosis, a rare and usually fatal liver ... during Casey's lengthy battle with amyloidosis and subsequent multiple organ transplant. Singel was born in Johnstown, ...
"Familial amyloidosis, Finnish type: G654----a mutation of the gelsolin gene in Finnish families and an unrelated American ... type II or Finnish type amyloidosis: associated with manifestations of systemic amyloidosis due to accumulation of gelsolin. ... type III is also described which has an onset at age 70 to 90 years and is not associated with systemic amyloidosis. In the ... Kiuru-Enari S, Keski-Oja J, Haltia M (February 2005). "Cutis laxa in hereditary gelsolin amyloidosis". Br. J. Dermatol. 152 (2 ...
It is also used in the treatment of familial Mediterranean fever, in which it reduces attacks and the long-term risk of ... and amyloidosis. Research regarding the efficacy of colchicine in many of these diseases has not been performed. ... URL Pharma also received seven years of market exclusivity for Colcrys in the treatment of familial Mediterranean fever, under ... On 30 July 2009, the FDA approved colchicine as a monotherapy for the treatment of three different indications (familial ...
Familial renal amyloidosis is a form of amyloidosis primarily presenting in the kidney. It is associated most commonly with ... March 2005). "Underdiagnosed amyloidosis: amyloidosis of lysozyme variant". Am. J. Med. 118 (3): 321-2. doi:10.1016/j.amjmed. ... January 2006). "Lysozyme amyloidosis: report of 4 cases and a review of the literature". Medicine (Baltimore). 85 (1): 66-73. ... August 1992). "Apolipoprotein AI mutation Arg-60 causes autosomal dominant amyloidosis". Proc. Natl. Acad. Sci. U.S.A. 89 (16 ...
Amyloidosis is a disorder of protein folding in which normally soluble proteins undergo a conformational change and are ... encoded search term (Familial Renal Amyloidosis) and Familial Renal Amyloidosis What to Read Next on Medscape ... Familial renal amyloidosis. Progression of amyloid deposits in a patient with amyloidosis associated with fibrinogen A alpha- ... Familial renal amyloidosis. An extended kindred with hereditary amyloidosis associated with fibrinogen A alpha-chain Glu526Val ...
Hereditary amyloidosis is a condition in which abnormal protein deposits (called amyloid) form in almost every tissue in the ... Hereditary amyloidosis is a condition in which abnormal protein deposits (called amyloid) form in almost every tissue in the ... Hereditary amyloidosis is passed down from parents to their children (inherited). Genes may also play a role in primary ... Amyloidosis. In: Firestein GS, Budd RC, Gabriel SE, Koretzky GA, McInnes IB, ODell JR, eds. Firestein & Kelleys Textbook of ...
ATTR Amyloidosis: Familial Vs Wild-Type Episode ATTRv-PN: A Complicated Disease With a Poor Prognosis Episode ...
Familial Mediterranean fever. 277.31. E85.0; M04. Amyloidosis NEC. 277.39. E85.1; E85.3; E85.8. ...
Increased soluble FAS suggests delayed apoptosis in familial Mediterranean fever complicated with amyloidosis. Sedat Kiraz, ... sex coupled with articular manifestations cause a 4-fold increase in susceptibility to amyloidosis in patients with familial ...
She is a member of the Indiana University Amyloidosis Research Group led by Dr. Merrill Benson. She has appointments in both ... Her clinical and research interests include cardiac amyloidosis, cardiac imaging, heart disease in women, and medical education ... Familial wild-type transthyretin cardiomyopathy. Benson MD; Berk JL; Connors LH; Dasgupta NR; Amyloid : the international ... She is a member of the Indiana University Amyloidosis Research Group led by Dr. Merrill Benson. She has appointments in both ...
... as a treatment for the familial amyloidotic cardiomyopathy manifestation of ATTR that's associated with heart failure, in ... is being studied as a potential treatment for thefamilial amyloidotic polyneuropathy form of transthyretin-mediated amyloidosis ...
Amyloidosis - Etiology, pathophysiology, symptoms, signs, diagnosis & prognosis from the MSD Manuals - Medical Professional ... AF (familial amyloidosis) AF amyloidosis (familial amyloidosis) Amyloidosis is any of a group of disparate conditions ... AL (primary amyloidosis) AL amyloidosis (primary amyloidosis) Amyloidosis is any of a group of disparate conditions ... AA (secondary amyloidosis) AA amyloidosis (secondary amyloidosis) Amyloidosis is any of a group of disparate conditions ...
... which has been implicated in diseases including senile systemic amyloidosis, familial amyloid polyneuropathy, and familial ...
... and fatal familial insomnia (FFI), rare familial disorders. With the exception of FFI, all of these disorders have been ... TSEs are transmissible amyloidoses in which the host-encoded protein has the propensity to acquire a beta-sheet conformation ... Different mutations in this gene are responsible for various phenotypes of TSE in its familial form, and a polymorphism at ... Some recent advances in our understanding of motoneuron death in familial ALS (fALS) and sporadic ALS (sALS) are reviewed, with ...
Overview of amyloidosis, a condition where abnormal proteins called amyloid build up in organs and tissues, and how the ... If you have familial Mediterranean fever, your health care professional may use a medicine called colchicine to treat the ... How common is kidney-related amyloidosis?. Amyloidosis is rare. AL amyloidosis is the most common type of amyloidosis in the ... Clinical Trials for Amyloidosis & Kidney Disease. What is amyloidosis?. Amyloidosis is a rare disease that occurs when amyloid ...
... and Board of Directors of the Chinese Shar-Pei Club of America supports research for Familial Shar-Pei Fever and amyloidosis. ... Renal amyloidosis has hit the Shar-Pei fancy in recent years and left many of us feeling helpless as we watch young Shar-Pei ... There is a real danger in the Shar-Pei to blame every kidney problem on renal amyloidosis and fail to pursue other causes of ... The kidney biopsy is the definitive diagnosis of renal amyloidosis and the decision to biopsy should be made early in the ...
Is bullous skin lesion a risk factor for renal amyloidosis in patients with familial mediterranean fever?. ...
99m)Tc-pyrophosphate scintigraphy for differentiating light-chain cardiac amyloidosis from the transthyretin-related familial ... Ultimately, tracer uptake equal to or greater than bone was 100% sensitive and specific for TTR amyloidosis in the study ... B. Myocardial retention of bone-seeking radiotracers is nonspecific for cardiac amyloidosis because it may also be present in ... showed significantly increased bone tracer uptake in TTR amyloidosis in comparison to older adults with other causes of LVH. ...
It appears that the process of Aβ-amyloidosis begins ~10-15 years prior to the onset of symptoms in both sporadic AD and FAD. ... 2022a) found a correlation between the age of onset in familial AD caused by different PS1 mutants and the ratio of short ... Wolfe, M. S. (2021). Targeting γ-secretase for familial Alzheimers disease. Med. Chem. Res. 30, 1321-1327. doi: 10.1007/s00044 ... 2012). The mechanism of γ-Secretase dysfunction in familial Alzheimers disease. Embo. J. 31, 2261-2274. doi: 10.1038/emboj. ...
Restrictive Myopathy: Amyloidosis. Restrictive Myopathy: Sarcoidosis. Restrictive Myopathy: Endocardial Fibrosis. Restrictive ... Dilated Myopathy: Familial. Dilated Myopathy: Adriamycin. Dilated Myopathy: Viral. Dilated Myopathy: Alcoholic ...
Biopsy plus genetic testing Types of familial amyloid polyneuropathy: Transthyretin amyloidosis Apolipoprotein A-I Gelsolin ... Familial amyloid polyneuropathy FAP Synonyms: a.k.a. Familial amyloidotic polyneuropathy FAP, a.k.a. Hereditary amyloid ... Synonyms: formerly familial rectal pain syndrome Diagnosis: A type of channelopathy Genetics: Autosomal dominant SCN9A gene. ... Tangier disease: Familial alpha-lipoprotein deficiency Synonyms: High density lipoprotein HDL deficiency, Clinical features: ...
A combination of pharmacophore and in silico approaches for identification of potential transthyretin amyloidosis inhibitors. ... A combination of pharmacophore and in silico approaches for identification of potential transthyretin amyloidosis inhibitors. ...
Furin initiates gelsolin familial amyloidosis in the Golgi through a defect in Ca(2+) stabilization. EMBO J. 2001 Nov 15. 20(22 ... Central Nervous System Amyloidoses and Other Localized Amyloidoses. Central nervous system amyloidoses. Beta protein amyloid ... Descriptive terms such as primary amyloidosis, secondary amyloidosis, and others (eg, senile amyloidosis), which are not based ... Systemic Amyloidoses. A amyloidosis (AA). The precursor protein is a normal-sequence apo-SAA (serum amyloid A protein) now ...
Familial Mediterranean Fever, Autosomal Dominant. Renal insufficiency, Proteinuria, Peritonitis, Renal amyloidosis, Erysipelas ...
A familial amyloidosis. Full barrier contraception as primary tumour. K, as a witnessed a spirit remeron use of different ...
Renal amyloidosis/ Amyloidosis; Renal Dysplasia/ RD; Progressive nephropathy (renal dysplasia)/ PNP; Ectopic Ureter/ EU; ... Kidney disease; Bladder Stones; Familial Nephropathy (FN)/ PNP/FN; Fanconi syndrome; glomerulonephritis; Juvenile Renal ... Renal amyloidosis/ Amyloidosis; Renal Dysplasia/ RD; Progressive nephropathy (renal dysplasia)/ PNP; Ectopic Ureter/ EU; ... Kidney disease; Bladder Stones; Familial Nephropathy (FN)/ PNP/FN; Fanconi syndrome; glomerulonephritis; Juvenile Renal ...
99mTc-Pyrophosphate scintigraphy for differentiating light-chain cardiac amyloidosis from the transthyretin-related familial ... amyloid immunoglobulin light chain amyloidosis; AS, aortic stenosis; ATTR, transthyretin amyloidosis; ATTR-CM, transthyretin ... When cardiac amyloidosis is suspected, Grade 2 or 3 myocardial uptake with concurrent testing to rule out AL is diagnostic of ... Written by a writing group of experts in cardiovascular imaging and amyloidosis, assembled by the American Society of Nuclear ...
Amyloidosis Familial Visceral Whats New Last Posted: Jan 01, 2011 * Amyloidosis familial visceral From NCATS Genetic and Rare ...
International Society of Amyloidosis) Sipe et al., 2016: "The terms "hereditary amyloidosis" and "familial amyloidosis" refer ... The term "familial amyloidosis" should be used when the syndrome occurs in a familial setting due to mutations in genes ... Familial amyloidosis in cats: Siamese and Abyssinian AA proteins differ in primary sequence and pattern of deposition Amyloid 6 ... Familial renal amyloidosis in Abyssinian cats. Vet Pathol 21:33-8, 1984. Pubmed reference: 6710810. DOI: 10.1177/ ...
The panel also includes familial amyloidosis genes and distal spinal muscular atrophy (forms not related to SMN1/SMN2). ... The test is indicated for individuals with clinical suspicion of familial adenomatous polyposis (FAP). The... Ver mais familial ... its also called transthyretin-related amyloidosis or simply TTR amyloidosis. More than 150 variants in TTR are associated with ... Hereditary Amyloidosis This test conducts the sequencing and evaluation of the number of copies (CNV) of TTR gene through the ...
... amyloidosis and transthyretin-related (TTR) amyloidosis, as hereditary or acquired form. The heart involvement due to the ... Advances in the Management of Cardiac Amyloidosis,Special Issue Introduction:Systemic amyloidosis is a rare haematologic ... a comprehensive state-of-art of the current knowledge about cardiac amyloidosis; (2) to stimulate researchers to share their ... experience in this field, since the overall contributions could open new borders in such rare diseases, as cardiac amyloidosis. ...
Progressive disorder initiated by a form of myocardial injury either sudden (MI or myocarditis) or chronic insults (familial, ... Amyloidosis. *Connective tissue disease (SLE, polyarteritis nodosa, scleroderma, myositis, sarcoidosis). *Muscular dystrophies ... Familial storage disease (hemochromatosis, glycogen storage disease, Hurler syndrome, Anderson-Fabry disease) ...
Familial AmyloidosisFamilial HypercholesterolaemiaFamilial Mediterranean Fever (FMF)Familial hypocalciuric hypercalcaemia (FHH) ... Familial Amyloid: Liver transplantation may be lifesaving for familial forms of amyloidosis where the protein transthyretin ( ... Familial amyloidosis: Autosomal dominant mutation of the hepatically expressed protein transthyretin *Senile systemic ... Bradycardia with 2:1 or complete heart block is common in amyloidosis and is much more likely to occur with Digoxin About. * ...
  • Her clinical and research interests include cardiac amyloidosis, cardiac imaging, heart disease in women, and medical education. (iu.edu)
  • These findings were consistent with cardiac amyloidosis. (acc.org)
  • These findings were all consistent with the diagnosis of TTR cardiac amyloidosis. (acc.org)
  • 2) to stimulate researchers to share their experience in this field, since the overall contributions could open new borders in such rare diseases, as cardiac amyloidosis. (oaepublish.com)
  • It is associated most commonly with congenital mutations in the fibrinogen alpha chain and classified as a dysfibrinogenemia (see Hereditary Fibrinogen Aα-Chain Amyloidosis). (wikipedia.org)
  • Familial renal amyloidosis (FRA) is a group of hereditary disorders in which misfolded proteins-amyloid-accumulate in the kidneys, causing proteinuria and/or hypertension followed by progressive kidney failure. (medscape.com)
  • Most such patients have either reactive systemic (AA) amyloidosis or monoclonal immunoglobulin light-chain (AL) amyloidosis , but in the few remaining cases, the disease is hereditary. (medscape.com)
  • Hereditary amyloidosis is a condition in which abnormal protein deposits (called amyloid) form in almost every tissue in the body. (medlineplus.gov)
  • Hereditary amyloidosis is passed down from parents to their children (inherited). (medlineplus.gov)
  • Treatment to improve the function of damaged organs will help relieve some symptoms of hereditary amyloidosis. (medlineplus.gov)
  • There is a rare hereditary form of beta-2-microglobulin amyloidosis due to a mutation to the relevant gene. (msdmanuals.com)
  • Hereditary amyloidosis can be passed down from a parent to a child through rare gene mutations . (nih.gov)
  • Hereditary amyloidosis is more common in people who have a family member with the condition. (nih.gov)
  • The chemical diversity of amyloid and amyloidosis has been evident since the mid-1970s and the number of known human amyloid proteins has steadily increased from two at that time to 36 at Amyloid deposition, either hereditary or acquired, is seldom benign and, when clinical symptoms appear, they are frequently life-threatening. (omia.org)
  • 2016: "The terms "hereditary amyloidosis" and "familial amyloidosis" refer to different entities. (omia.org)
  • The term "hereditary amyloidosis" should be used when there is a mutation in the fibril protein gene itself, e.g. (omia.org)
  • At least 30 different proteins have been reported to produce amyloid fibrils, but two types are more capable of affecting the heart, such as light-chain (AL) amyloidosis and transthyretin-related (TTR) amyloidosis, as hereditary or acquired form. (oaepublish.com)
  • In addition to the acquired causes, inherited disorders like hereditary sensory-autonomic neuropathy (HSAN), familial amyloid polyneuropathy (FAP), Tangier disease, and Fabry disease also exist. (medscape.com)
  • Familial renal amyloidosis is a form of amyloidosis primarily presenting in the kidney. (wikipedia.org)
  • The amyloidogenic precursor proteins in patients with familial renal amyloidosis are thought to be less stable than their wild-type counterparts, causing them to populate intermediate, molten, globulelike states more readily. (medscape.com)
  • This article by Dr. Vidt presents a plan to monitor Shar-Pei with the goal of uncovering renal amyloidosis as early as possible and then instituting appropriate dietary and medical intervention. (drjwv.com)
  • Renal amyloidosis has hit the Shar-Pei fancy in recent years and left many of us feeling helpless as we watch young Shar-Pei sicken and die before our very eyes. (drjwv.com)
  • What I propose in this paper is based on the information available today about renal amyloidosis. (drjwv.com)
  • Remember, we are trying to uncover this condition at its earliest point - minor weight loss can indicate early renal amyloidosis. (drjwv.com)
  • Other types of amyloidosis are not inherited. (medlineplus.gov)
  • A number of normal (wild-type) and mutant proteins are susceptible to such misfolding and aggregation (amyloidogenic proteins), thus accounting for the wide variety of causes and types of amyloidosis. (msdmanuals.com)
  • Four types of amyloidosis most often affect the kidneys . (nih.gov)
  • 2 The other types of amyloidosis are even less common. (nih.gov)
  • An aggressive form of transthyretin amyloidosis. (iu.edu)
  • [ 1 ] Accumulation of these fibrils causes progressive disruption of the structure and function of tissues and organs, and the systemic (generalized) forms of amyloidosis are frequently fatal. (medscape.com)
  • Localized forms of amyloidosis appear to be caused by local production and deposition of an amyloidogenic protein (most often immunoglobulin light chains) within the affected organ rather than by deposition of circulating proteins. (msdmanuals.com)
  • Familial Amyloid: Liver transplantation may be lifesaving for familial forms of amyloidosis where the protein transthyretin (prealbumin) is produced in excess by the liver to make amyloid fibrils. (abcmedicalnotes.com)
  • Immunoglobulin light-chain amyloidosis (AL amyloidosis), or primary amyloidosis, affects the kidneys in about 2 out of 3 people with this condition. (nih.gov)
  • International Society of Amyloidosis ) Sipe et al. (omia.org)
  • Treatment varies with the type of amyloidosis. (msdmanuals.com)
  • Some people with kidney failure may experience another type of amyloidosis, known as dialysis-related amyloidosis. (nih.gov)
  • AL amyloidosis is the most common type of amyloidosis in the United States, and it affects approximately 40 out of every 1 million Americans. (nih.gov)
  • The risk factors for kidney-related amyloidosis depend on the type of amyloidosis. (nih.gov)
  • The syndrome of familial systemic amyloidosis with predominant nephropathy is inherited in an autosomal dominant manner and was first described in a German family by Ostertag in 1932. (medscape.com)
  • Synonyms: formerly familial rectal pain syndrome Diagnosis: A type of channelopathy Genetics: Autosomal dominant SCN9A gene. (learningneurology.com)
  • Familial mediterranean fever is an autosomal recessive inherited disorder characterized by recurrent episodic fever, serosal inflammation and pain in the abdomen, chest or joints. (lu.se)
  • This cross-sectional study investigated depression as the middle- (4 years) and long-term (7 and 10 years) psychological impact of pre-symptomatic testing (PST) for 3 autosomal dominant late-onset diseases: Huntington's disease (HD), Machado-Joseph disease (MJD) and familial amyloidotic poly- neuropathy (FAP) TTR V30M. (bvsalud.org)
  • Kidney dysfunction is one of the most common presenting features of patients with systemic amyloidosis , and amyloid accumulation is the major pathological finding in approximately 2.5% of all native kidney biopsies. (medscape.com)
  • In systemic amyloidosis, circulating amyloidogenic proteins form deposits in a variety of organs. (msdmanuals.com)
  • Systemic amyloidosis is a rare haematologic disorder where fibrils of misfolded proteins acquire a b-pleated sheet conformation, form amyloid fibril proteins, and begin to infiltrate tissues leading to organ failure. (oaepublish.com)
  • Most classification systems included primary (ie, in the sense of idiopathic) amyloidosis, in which no associated clinical condition was identified, and secondary amyloidosis, which is associated with chronic inflammatory conditions. (medscape.com)
  • [ 2 ] Research has shown that almost all patients with familial renal amyloidoses (FRA) are heterozygous for mutations in the genes for lysozyme, apolipoprotein AI, apolipoprotein AII, or fibrinogen A alpha-chain and that the amyloid fibrils in this condition are derived from the respective variant proteins. (medscape.com)
  • Amyloidosis is any of a group of disparate conditions characterized by extracellular deposition of insoluble fibrils composed of misaggregated proteins. (msdmanuals.com)
  • Amyloidosis is a clinical disorder caused by extracellular and/or intracellular deposition of insoluble abnormal amyloid fibrils that alter the normal function of tissues. (medscape.com)
  • Only 10% of amyloidosis deposits consist of components such as glycosaminoglycans (GAGs), apolipoprotein-E (apoE), and serum amyloid P-component (SAP), while nearly 90% of the deposits consist of amyloid fibrils that are formed by the aggregation of misfolded proteins. (medscape.com)
  • The modern era of amyloidosis classification began in the late 1960s with the development of methods to solubilize amyloid fibrils. (medscape.com)
  • Amyloid is the term for a misfolded protein that accumulates as insoluble fibrils in various organ and tissue sites to result in a clinical syndrome known as amyloidosis. (omia.org)
  • Cryo-EM structure of ex vivo fibrils associated with extreme AA amyloidosis prevalence in a cat shelter. (omia.org)
  • Amyloidosis is a disorder of protein folding in which normally soluble proteins undergo a conformational change and are deposited in the extracellular space in an abnormal fibrillar form. (medscape.com)
  • For amyloidosis to develop, in addition to production of amyloidogenic proteins, there is probably also a failure of the normal clearance mechanisms for such misfolded proteins. (msdmanuals.com)
  • Amyloidosis is a rare disease that occurs when amyloid proteins are deposited in tissues and organs. (nih.gov)
  • Dialysis-related amyloidosis causes amyloid proteins to build up in bones, joints, and tendons. (nih.gov)
  • The term "familial amyloidosis" should be used when the syndrome occurs in a familial setting due to mutations in genes expressing non-amyloid proteins, e.g. (omia.org)
  • Amyloidosis, which could mutations that can affect the MEFV gene ( 8,9 ). (who.int)
  • A report on the frequencies and can eventually result in amyloidosis, while FMF of MEFV mutations in these 2 populations revealed type 2 is identified by amyloidosis as the initial clinical the severity of 1 specific mutation ( M694V ) and 3 novel manifestation in an otherwise asymptomatic person mutations in the Lebanese group only ( 10 ). (who.int)
  • liver transplantation is potentially curative in patients with fibrinogen A alpha-chain FRA and, possibly, in some patients with apolipoprotein AI amyloidosis. (medscape.com)
  • Leukocyte cell-derived chemotaxin 2 (LECT2) amyloidosis is a recently discovered form of amyloidosis that most often affects the kidneys and liver. (nih.gov)
  • Defects in MEFV are the cause of familial mediterranean fever. (lu.se)
  • Familial mediterranean fever primarily affects ethnic groups living around the mediterranean basin north-african jews, armenians, arabs and turks. (lu.se)
  • Familial Mediterranean fever (FMF) is an autoinflammatory, multisystem disease affecting the populations of the Mediterranean basin. (who.int)
  • The amyloidoses are referred to with a capital A (for amyloid) followed by an abbreviation for the fibril protein. (medscape.com)
  • Most of the distinct amyloidosis syndromes are named after the fibril forming protein, e.g. (omia.org)
  • AA amyloidosis is most common in people who have experienced a long-lasting infection or chronic inflammatory disorder. (nih.gov)
  • Amyloidosis can affect different organs and tissues in different people, and it can affect more than one organ at the same time. (nih.gov)
  • The symptoms and severity of amyloidosis depend on which organs and tissues are affected. (nih.gov)
  • Patisiran is being studied as a potential treatment for thefamilial amyloidotic polyneuropathy form of transthyretin-mediated amyloidosis (ATTR). (foxbusiness.com)
  • Next up, the biotech is forecasting another late-stage data readout for revusiran, as a treatment for the familial amyloidotic cardiomyopathy manifestation of ATTR that's associated with heart failure, in late 2018. (foxbusiness.com)
  • Familial wild-type transthyretin cardiomyopathy. (iu.edu)
  • Amyloidosis can occur de novo or be secondary to various infectious, inflammatory, or malignant conditions. (msdmanuals.com)
  • Amyloid A amyloidosis (AA amyloidosis), or secondary amyloidosis, is often associated with certain chronic inflammatory conditions. (nih.gov)
  • Descriptive terms such as primary amyloidosis, secondary amyloidosis, and others (eg, senile amyloidosis), which are not based on etiology, provide little useful information and are no longer recommended. (medscape.com)
  • With a focus on awareness, prevalence, causes, and risks of Familial Hypercholesterolemia (FH) this tool is especially helpful for those with or at risk for FH. (pcna.net)
  • What are the types of kidney-related amyloidosis? (nih.gov)
  • How common is kidney-related amyloidosis? (nih.gov)
  • Who is more likely to develop kidney-related amyloidosis? (nih.gov)
  • Risk of developing dialysis-related amyloidosis increases the longer you have been on dialysis, the older you are at the start of dialysis treatment, and the more your kidney function has declined. (nih.gov)
  • What are the complications of kidney-related amyloidosis? (nih.gov)
  • What are the symptoms of kidney-related amyloidosis? (nih.gov)
  • When amyloidosis affects your kidneys, the most common symptom is nephrotic syndrome -a group of symptoms that indicate kidney damage. (nih.gov)
  • Renal amyloid-A amyloidosis in cats: Characterization of proteinuria and biomarker discovery, and associations with kidney histology. (omia.org)
  • Nuclear scintigraphy, using both planar and SPECT imaging, is a non-invasive, commonly available diagnostic tool with high sensitivity and specificity for ATTR-CM when combined with testing to rule out AL amyloidosis. (pfizerpro.in)
  • A multicentre international study of scintigraphy at amyloidosis centres of excellence demonstrated 100% specificity for ATTR-CM using visual grade 2 or 3, with concurrent testing to rule out AL amyloidosis. (pfizerpro.in)
  • Owing to the development of sensitive biochemical and imaging biomarker technologies, it is possible to monitor the process of Aβ amyloidosis during disease progression. (frontiersin.org)
  • and Gerstmann-Sträussler-Scheinker disease (GSS) and fatal familial insomnia (FFI), rare familial disorders. (annualreviews.org)
  • This could be achieved with small-molecule treatments, providing cost-effective, patient/user-friendly oral therapies that would be fit for purpose as a chronic preventive treatment paradigm in people with emerging amyloidosis who are otherwise unaffected by the disease. (frontiersin.org)
  • It appears that the process of Aβ-amyloidosis begins ~10-15 years prior to the onset of symptoms in both sporadic AD and FAD. (frontiersin.org)
  • Some classification systems included myeloma-associated, familial, and localized amyloidosis. (medscape.com)
  • Amyloidosis caused by aggregation of beta-2-microglobulin can occur in patients on long-term hemodialysis, but the incidence has declined with use of modern high-flow dialysis membranes. (msdmanuals.com)

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