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07-SEPTEMBER-2008 03:17:44 - Amyloidosis Amyloidosis Classification and external resources Small bowel duodenum with amyloid deposition congo red 10X ICD-10 E85. ICD-9 277.3 DiseasesDB 633 eMedicine med/3377 med/3888 MeSH D000686 In medicine, amyloidosis refers to a variety of conditions in which amyloid proteins are abnormally deposited in organs and/or tissues, causing disease. A protein is amyloid if, due to an alteration in its secondary structure, it takes on a particular insoluble form, called the beta-pleated sheet.1 The term amyloidosis refers to a histological finding occurring in several different disease processes that have little in common with each other, and without additional information, the finding is of limited clinical use.2 Contents 1 Diagnosis 2 Classification of amyloid 3 Classification of amyloidosis 3.1 Systemic amyloidosis 3.2 Organ-specific amyloidosis 4 Famous People who have contracted Amyloidosis 5 Additional images 6 References 7 External links Diagnosis Amyloid can be diagnosed on microscopic examination of affected tissue. Amyloid deposits can be identified histologically by Congo red staining3 and viewing under polarized light where amyloid deposits produce a distinctive 'apple green birefringence'. Further, specific tests are available to more precisely identify the amyloid protein. Biopsies are taken from affected organs for example, the kidney, or often in the case of systemic amyloid, from the rectum, gingiva, or omentum anterior abdominal adipose tissue. 4 In addition, all amyloid deposits contain serum amyloid P component SAP,5 a circulating protein of the pentraxin family. Radionuclide SAP scans have been developed which can anatomically localize amyloid deposits in patients. Classification of amyloid Approximately 25 different proteins are known that can form amyloid in humans. Most of them are constituents of the plasma. Different amyloidoses can be systemic affecting many different organ systems or organ-specific. Some are inherited, due to mutations in the precursor protein. Other forms are due to different diseases causing overabundant or abnormal protein production-such as with over production of immunoglobulin light chains in multiple myeloma termed AL amyloid, or with continuous overproduction of acute phase proteins in chronic inflammation which can lead to AA amyloid. There are at least 15 biologically distinct forms of amyloid, some more clinically significant than others. Following is a brief description of the more common types of amyloid: Abb. Amyloid type Description AL amyloid light chain Contains immunoglobulin light-chains λ,κ derived from plasma cells AA amyloid associated Non-immunoglobulin protein made in the liver Aβ β amyloid Found in Alzheimer disease brain lesions ATTR Transthyretin A mutant form of a normal serum protein that is deposited in the genetically determined familial amyloid polyneuropathies. TTR is also deposited in the heart in senile systemic amyloidosis.6 Aβ2 m β2 microglobulin Not to be confused with Aβ, β2m is a normal serum protein, part of major histocompatability complex MHC Class 1 molecules. Can occur in long term haemodialysis. PrP Prion related protein In Prion diseases, misfolded prion proteins deposit in tissues and resemble amyloid proteins. OMIM includes the following: OMIM Gene Name Number 176300 TTR Senile systemic amyloidosis type 1 105120 GSN Finnish type amyloidosis type 5 105150 CST3 Cerebral amyloid angiopathy, Icelandic type type 6 105210 TTR Leptomeningeal amyloidosis type 7 105200 APOA1, FGA, LYZ Familial visceral amyloidosis type 8 105250 OSMR Primary cutaneous amyloidosis type 9 176500 ITM2B Cerebral amyloid angiopathy, British type - 609065, 605714 APP Dutch type / Italian type / Iowa type - Classification of amyloidosis The amyloidoses can be classified as systemic or localised, primary or secondary, or according to which type of amyloid is deposited. By convention, a combination of these approaches are used clinically. Systemic amyloidoses are those which affect more than one body organ or system. Localised amyloidoses affect only one body organ or tissue type. Primary amyloidoses arise from a disease with disordered immune cell function such as multiple myeloma and other immunocyte dyscrasias. Secondary reactive amyloidoses are those occurring as a complication of some other chronic inflammatory or tissue destructive disease. The different types of amyloid deposited see table, above may be either primary or secondary, systemic or localised. Systemic amyloidosis The common systemic amyloidoses: Category Amyloid type Precursor protein Amyloidosis Systemic acquired AL Immunoglobin light chains Bence Jones protein AL amyloidosis primary amyloidosis Systemic herary AA SAA AA amyloidosis secondary amyloidosis Systemic herary Aβ2 m β2 microglobulin Haemodialysis associated Systemic herary AA SAA Familial merranean fever Systemic herary ATTR transthyretin Familial amyloidotic polyneuropathies Systemic herary ATTR transthyretin Systemic senile amyloidosis Organ-specific amyloidosis Main article: Organ-limited amyloidosis In almost all of the organ-specific pathologies, there is significant debate as to whether the amyloid plaques are the causal agent of the disease or instead a downstream consequence of a common idiopathic agent. Famous People who have contracted Amyloidosis James Oliver Rigney, Jr. aka. Robert Jordan, author of the The Wheel of Time series David Lange, Prime Minister of New Zealand Richard Caliguiri, mayor of Pittsburgh, Pennsylvania Louis J. Tullio, mayor of Erie, Pennsylvania Bob Casey, Governor of Pennsylvania John Smith Additional images Amyloidosis, dystrophic calcification Small bowel duodenum with amyloid deposition 20X Amyloidosis, Node, Congo Red Amyloidosis, blood vessels, HE Amyloidosis, lymph node, HE Amyloidosis, lymph node, polarizer References ^ Atlas of Pathology. ^ Gertz MA June 2004. The classification and typing of amyloid deposits. Am. J. Clin. Pathol. 121 6: 787-9. doi:10.1309/TR4L-GLVR-JKAM-V5QT. PMID 15198347. ^ Satoskar AA, Burdge K, Cowden DJ, Nadasdy GM, Hebert LA, Nadasdy T June 2007. Typing of amyloidosis in renal biopsies: diagnostic pitfalls. Arch. Pathol. Lab. Med. 131 6: 917-22. PMID 17550319. ^ Kumar, Vinay; Abbas, Abul K.; Fausto, Nelson; Mitchell, Richard N. 2007. Robbins Basic Pathology 8th ed.. Saunders Elsevier. p.171 ISBN 978-1-4160-2973-1 ^ Togashi S, Lim SK, Kawano H, et al November 1997. Serum amyloid P component enhances induction of murine amyloidosis. Lab. Invest. 77 5: 525-31. PMID 9389795. ^ Hassan W, Al-Sergani H, Mourad W, Tabbaa R 2005. Amyloid heart disease. New frontiers and insights in pathophysiology, diagnosis, and management. Tex Heart Inst J 32 2: 178-84. PMID 16107109. External links Overview at Mayo Clinic Overview at Cleveland Clinic 1 Boston University Amyloid Treatment and Research Program www.amyloidosisaustralia.org Information, support and advice to anyone with Amyloidosis v d e Metabolic disease: amyloidosis E85, 277.3 Forms of amyloid Serum amyloid P component - Serum amyloid A - Transthyretin - Beta-2 microglobulin - Bence Jones protein/Multiple myeloma - Amyloid precursor protein/Beta amyloid - Amylin Systemic amyloidosis AL amyloidosis - AA amyloidosis - Haemodialysis-associated amyloidosis - Senile systemic amyloidosis - Finnish type amyloidosis - Familial Merranean fever Organ-limited amyloidosis heart: Cardiac amyloidosis brain: Familial amyloid neuropathy - Cerebral amyloid angiopathy - Alzheimer's disease kidney: Familial renal amyloidosis cutaneous: Primary cutaneous amyloidosis Retrieved from http://en..org/wiki/Amyloidosis Categories: Metabolic disorders | Diseases Views Article Discussion this page History Personal tools Log in / create account Navigation Main page Contents Featured content Current events Random article Search Go Search Interaction Community portal Recent changes Contact Donate to Help Toolbox What links here Related changes Upload file Special pages Printable version Permanent link Cite this page Languages العربية Dansk Deutsch Ελληνικά Español Eesti Suomi Français Bahasa Indonesia Italiano 日本語 Nederlands Polski Português РуÑ?Ñ?кий ä¸æ–‡ This page was last modified on 22 August 2008, at 05:23
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