Amyloidosis

Amyloidoses are a group of different diseases, which the extracellular deposition non-soluble fibrils which consist of false aggregated proteins is common. These proteins can be deposited locally limited and thus prepare little problems or very extended in many organs spread and cause a severe multi-organ failure. Amyloidosis can de novo or secondary occur as a result of various infections, inflammation and malignant tumors. The diagnosis is made by biopsy of the affected tissue; the amyloidogenic protein is typed with a plurality immunohistological and biochemical techniques. Treatment depends on the type of amyloidosis.

Amyloid deposits consist of small (about 10 nm in diameter), insoluble fibrils which form ?-pleated sheets, which can be identified with an X-ray diffraction. In addition to the fibrillar amyloid proteins contain deposits amyloid P component and glycosaminoglycans. Amyloid fibrils consist of misfolded proteins aggregate into oligomers and fibrils. A variety of normal (wild type) and mutant proteins is susceptible to such misfolding and aggregation (amyloidogenic proteins), resulting in a wide variety of causes and types of amyloidosis. Thus amyloidosis developed, whether a failure of the normal disposal mechanisms for such misfolded proteins probably needs to be present alongside the production of amyloidogenic proteins. The amyloid deposits themselves are metabolically inert, organ function and structure affect but mechanical. However, some prefibrillar oligomers of amyloidogenic proteins have a direct cellular toxicity, an important component of the pathogenesis of the disease.

Amyloidoses are a group of different diseases, which the extracellular deposition non-soluble fibrils which consist of false aggregated proteins is common. These proteins can be deposited locally limited and thus prepare little problems or very extended in many organs spread and cause a severe multi-organ failure. Amyloidosis can de novo or secondary occur as a result of various infections, inflammation and malignant tumors. The diagnosis is made by biopsy of the affected tissue; the amyloidogenic protein is typed with a plurality immunohistological and biochemical techniques. Treatment depends on the type of amyloidosis. Amyloid deposits consist of small (about 10 nm in diameter), insoluble fibrils which form ?-pleated sheets, which can be identified with an X-ray diffraction. In addition to the fibrillar amyloid proteins contain deposits amyloid P component and glycosaminoglycans. Amyloid fibrils consist of misfolded proteins aggregate into oligomers and fibrils. A variety of normal (wild type) and mutant proteins is susceptible to such misfolding and aggregation (amyloidogenic proteins), resulting in a wide variety of causes and types of amyloidosis. Thus amyloidosis developed, whether a failure of the normal disposal mechanisms for such misfolded proteins probably needs to be present alongside the production of amyloidogenic proteins. The amyloid deposits themselves are metabolically inert, organ function and structure affect but mechanical. However, some prefibrillar oligomers of amyloidogenic proteins have a direct cellular toxicity, an important component of the pathogenesis of the disease. Amyloid deposits are stained with hematoxylin and eosin pink and contain carbohydrate moieties which are stained with periodic acid-Schiff-dye or with Alcian blue; However, the most characteristic apple green birefringence under polarized light microscopy after Congo red staining. At autopsy, the institutions concerned can act waxy. Etiology In systemic amyloidosis form circulating amyloidogenic proteins deposits in a variety of organs. The significant systemic forms include AL (primary amyloidosis) caused by an acquired over-expression of clonal immunoglobulin light chains AF (familial amyloidosis) caused by the inheritance of a mutant gene that encodes a tending to misfolding protein, mostly transthyretin (TTR) SSA ( senile systemic amyloidosis) caused by the misfolding and aggregation of wild-type TTR (therefore also referred to as ATTRwt) AA (secondary amyloidosis) caused by the aggregation of an acute phase reactant, serum amyloid a amyloidosis caused by an aggregation of ?2- caused microglobulin (ass2) may occur in patients who are receiving hemodialysis in the long term, occur, but the incidence has decreased with the use of modern high-flow dialysis membranes. Localized forms of amyloidosis seem to be caused within the affected organ, and not by the deposition of circulating proteins by local production and deposition of amyloidogenic protein (including immunoglobulin light chains). Frequently involved locations include the CNS (eg. As in Alzheimer’s disease), the skin, the upper or lower respiratory tract, the bladder and other parts. AL amyloidosis AL is caused by the overproduction of an amyloidogenic immunoglobulin light chain in patients with a monoclonal plasma cell or other lymphoproliferative B-cell disorder. Light chains can also non-fibrillar tissue deposits cause (d. E. Light chain deposition disease). In rare cases, immunoglobulin heavy chains form amyloid fibrils (AH). Preferably of amyloid deposits organs affected the skin, nerves, the heart, the gastrointestinal tract (including the tongue), kidney, liver, spleen and blood vessels. In the bone marrow slight plasmocytosis is in the rule, which is similar to that in multiple myeloma, although most patients have no real multiple myeloma (lytic bone defects, hypercalcemia, sinks renal tubules and anemia). However, 10-20% of all patients with multiple myeloma develop an AL amyloidosis Amyloidose.AA This shape can occur secondary to various infections, inflammation and malignant events and is caused by the aggregation of isoforms of the acute-phase serum amyloid A protein. Common causes include infections such as tuberculosis, bronchiectasis, osteomyelitis and leprosy. Inflammatory causes are rheumatoid arthritis, juvenile idiopathic arthritis (formerly juvenile rheumatoid arthritis), Crohn’s disease, hereditary periodic fever syndromes such as familial Mediterranean fever and Castleman’s disease. Inflammatory cytokines (eg., IL-1, tumor necrosis factor ?, IL-6) produced in these inflammations or ektotypisch of tumor cells, causing an increased hepatic synthesis of serum amyloid A. AA is preferably in the spleen, liver, kidneys, adrenal glands, and lymph nodes. An involvement of the heart and of the autonomic nervous system is selten.AF AF amyloidosis is caused by inheritance of a gene that encodes a mutant protein in the serum, which tends to aggregation; these are usually a protein that is produced in abundance in the liver. To the serum proteins, which can cause AF include transthyretin (TTR), Apolipoprotein A-1, lysozyme, fibrinogen, gelsolin and Cystatin C. A recently identified form, which is thought of that she is familiar, is the serum protein leukocyte chemotactic factor 2 causes (LECT2); However, no specific inherited gene mutation for this latter type has been clearly demonstrated. Amyloidosis caused by TTR (ATTR), is the most common form of AF. More than 100 mutations in the TTR gene have been associated with amyloidosis. The most common mutation V30M and often occurs in Portugal, Sweden and Japan; Moreover, there is a V122I mutation in about 4% of US blacks. The penetrance of the disease and the age of onset are very different, but consistent within families and ethnic groups. The ATTR causes peripheral sensory and autonomic neuropathy and cardiomyopathy. Often, carpal tunnel syndrome occurs. Glass deposits may due to the production of mutated TTR by the retinal epithelium also develop, while the production of mutated TTR cause in the choroid plexus cerebrovascular amyloid angiopathy kann.SSA amyloidosis SSA (by the aggregation and deposition of wild-type TTR especially in hearts) gives. SSA is increasingly seen as a cause of infiltrative cardiomyopathy in older men. The genetic and epigenetic factors that lead to SSA, are unknown. Because the SSA and AL amyloidosis both can cause cardiomyopathy and because monoclonal gammopathy that are not associated with amyloidosis, may be present in patients in this age group, it is important to typify the amyloid carefully to patients with SSA not are inappropriately treated with chemotherapy (which is used in AL) .Lokalisierte amyloidosis localized amyloidosis is outside the brain most commonly caused by deposits of clonal immunoglobulin light chains and in the brain from the Aß protein. Localized amyloid deposits usually affect the respiratory tract and the lung tissue, the bladder and the urethra, skin, chest and eyes. In rare cases other proteins produced locally cause amyloidosis, which can locally form deposits in the skin, such as keratin-isoforms. Aß protein deposits in the brain contribute to Alzheimer’s disease or cerebrovascular amyloid angiopathy. Other proteins that are produced in the CNS can form misfolding, aggregate and damage neurons, which leads to diseases neurodegenerative (eg. As Parkinson’s disease, Huntington’s disease). Clonal immunoglobulin light chains are produced by associated with mucosal lymphoid tissue in the GI tract the respiratory tract and the bladder can lead to localized AL in those organs. Symptoms and signs The symptoms and complaints of systemic amyloidosis are nonspecific, often resulting in the delay of diagnosis. The suspicion of amyloidosis should be enhanced in patients with a progressive multisystem disease process. Amyloid deposits in the kidneys typically occur in the glomerular membrane, resulting in proteinuria; in 15% of cases, the tubes are affected, causing azotemia with minimal proteinuria. These processes can proceed to nephrotic syndrome with severe hypoalbuminemia, edema and anasarca or a renal disease. Liver involvement leads to a painless hepatomegaly, which can be very pronounced. Liver function tests typically indicate an intrahepatic cholestasis with increase of the alkaline phosphatase, and thereafter towards bilirubin, but jaundice is rare. Occasionally, portal hypertension developed with esophageal varices and ascites. The involvement of the airways leading to dyspnea, wheezing, hemoptysis, or airway obstruction. The infiltration of the heart muscle causes restrictive cardiomyopathy, eventually leading to diastolic dysfunction and heart failure; a heart block or cardiac arrhythmia may occur. Hypotension is common. Peripheral neuropathy with paresthesia of the toes and fingers is a common first manifestation in AL and ATTR amyloidosis. Autonomic neuropathy can cause gastrointestinal motility orthostatic hypotension, erectile dysfunction, abnormal sweat and disorders. The cerebrovascular amyloid angiopathy most commonly caused spontaneous lobar hemorrhage, but some patients have short, transient neurological symptoms. Gastrointestinal motility disorders caused amyloid in the esophagus, small intestine and colon. Atony of the stomach, malabsorption, bleeding or pseudo-obstruction may occur. Macroglossia is common in an AL amyloidosis. Macroglossia © Springer Science + Business Media var model = {thumbnailUrl: ‘/-/media/manual/professional/images/588-macroglossia-s182-springer-high_de.jpg?la=de&thn=0&mw=350’ imageUrl: ‘/ ? – / media / manual / professional / images / 588-macroglossia-s182-springer-high_de.jpg lang = en & thn = 0 ‘, title:’ macroglossia ‘description:’ u003Ca id = “v37895343 ” class = “”anchor “” u003e u003c / a u003e u003cdiv class = “”para “” u003e u003cp u003eDieses photo shows a patient with systemic amyloid and Macroglossie. The tongue protrudes at the corners of the mouth and the depression of the teeth out

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