Geometry.Net - Health_Conditions: Amyloidosis

Amyloidosis
Detailed information about this disease by Robert C. Mellors, MD, Ph.D. of the Cornell University Category Health Conditions and Diseases amyloidosisImmunopathology. by Robert C. Mellors, MD, Ph.D. amyloidosis. GeneralConsiderations. (Note Pathogenesis of amyloidosis. amyloidosis
http://edcenter.med.cornell.edu/CUMC_PathNotes/Immunopathology/Immuno_04.html

Extractions: by Robert C. Mellors, M.D., Ph.D. General Considerations (Note: Amyloid can be studied in the context of cell injury or immunological diseases. For this reason, we have included the same material in both Cell Injury and Immunopathology.) A myloidosis is not a single disease entity but rather a diverse group of disease processes characterized by extracellular tissue deposits, in one or many organs, of protein materials which are generically termed amyloid. Amyloid is distinguished grossly by a starch-like staining reaction with iodine (thus the term amyloid), microscopically by its extracellular distribution and tinctorial and optical properties when stained with Congo red, and by its protein fibril structure as shown by electron microscopy and x-ray crystallography (see Table-1). Table-1 Amyloid deposition may be either a primary (idiopathic) process without known antecedent or secondary to some other condition and may be localized to one specific site or generalized throughout the body (systemic), usually with fatal consequences. Although considerable overlap is seen in the organ distribution of various forms of amyloid, primary amyloidosis tends to involve mesodermal tissues, most frequently affecting peripheral nerves, skin, tongue, joints, heart, and liver while secondary amyloidosis mainly affects parenchymatous organs, such as spleen, kidneys, liver, and adrenals. Amyloid deposits typically contain three components. Amyloid protein fibrils account for about 90% of the amyloid material and comprise one of several different types of proteins with the capacity to fold into what are called "beta-pleated" sheet fibrils, a unique protein configuration with binding sites for Congo red. In addition, amyloid deposits are intimately associated with the amyloid P (pentagonal) component (AP), a glycoprotein related to normal serum amyloid P (SAP), and are closely associated with sulfated glycosaminoglycans (GAG), complex carbohydrates of connective tissue.
Amyloidosis
light chain, is called AL and occurs in primary amyloidosis and in amyloidosis associated with multiple myeloma.
http://www.silcom.com/~sblc/amyloid.html

Extractions: Click to subscribe to amyloidosis Return to the Resource List Did you come to this page first? Check out our features on the Resource List and the Main Menu ! Also, visit our bookstore ! And please post on our Message Board Share your favorite links with us so we can add them to this page! E-mail us at sblc@silcom.com Tell us what you liked and didn't like about any links or our page in general. Fill out a Comment Card or e-mail us Find any BUGS on our pages? Something go to the wrong place, misspelled, out-of-date, or otherwise need fixing? Please let us know! Fill out a
Amyloidosis Support Network
Provide complete, integrated, easy-to-reach support and information to existing information and referrals Category Health Conditions and Diseases amyloidosisamyloidosis Support Network The Network's primary function is to link those affectedby amyloidosis, to further support resources, and to educate the public
http://amyloidosis.org/

Extractions: Please help... Your donation will go for research to help find a cure... learn more! Mission Statement The Network's primary function is to "link those affected by amyloidosis to further support resources" and to educate the public and professionals so that the disease can be recognized earlier and appropriately treated. This web page is intended to streamline this support network and provide complete, integrated, easy-to-reach, direct access links to existing information and referrals for other sources of help, primarily for patients/families struggling with the disease. What is Amyloidosis? Amyloidosis is a group of diseases in which one or more organ systems in the body accumulate deposits of abnormal proteins. The name "amyloidosis" was first used more than 100 years ago but cases were described over 300 years ago. However, only within the past 20 years have physicians understood the specific make-up and structure of amyloid protein. Although amyloidosis is not cancer, it is very serious. It is disabling or life threatening. However, growing awareness of the condition seems to be leading to substantial new research and treatment alternatives. Click here for a more detailed description of the main types of Amyloidosis Click here for an overview of Primary Systemic AL Amyloidosis
Redirect Page For "/mmgrg/rst/aapamph.htm"
Explains what causes the abnormal protein buildup that leads to bone marrow disease. Gives symptoms, diagnosis, and treatment options. comes from cells in your bone marrow. amyloidosis (pronounced am-i-loy-do'-sis) results when enough amyloid protein
http://www.mayo.edu/mmgrg/rst/aapamph.htm
AL Primary Cutaneous Amyloidosis
UC Davis case study of a form of the disease limited to the skin. With photographs. (6) Longterm AL primary amyloidosis. A case report
http://matrix.ucdavis.edu/DOJvol1num2/amyloidosis/amyloidosis.html

Extractions: Volume 1, Number 2 This is a case report of AL primary amyloidosis with involvement limited to the skin for more than twenty years before the development of internal organ involvement. The clinical features suggested the systemic form of amyloidosis, rather than that found with nodular cutaneous amyloidosis. Longstanding lesions of nodular amyloidosis even in the face of a negative workup for internal involvement, can be consistent with systemic disease. This is an example of a patient who had extensive cutaneous amyloidosis for twenty years before developing cardiac involvement which then lead to her death. Patients who present with cutaneous features of amyloidosis usually undergo an evaluation to categorize the disease. Skin biopsy with ultrastructural immunohistochemical stains can help confirm the presence and subtype of amyloid. Once a patient has been found to have cutaneous amyloidosis, an extensive workup must be done to evaluate patients for the possibility of systemic involvement. Workup for systemic disease includes: serum and urine immunoelectrophoresis, rectal mucosal or abdominal fat biopsy, bone marrow biopsy, CBC, chemistry panel, and skull and spine X-rays. The origin of the amyloid and the extent of internal involvement are used to determine the approach to treatment.
THE MERCK MANUAL, Sec. 2, Ch. 18, Amyloidosis
The Merck Manual A discussion about amyloid production, the different types of this disease and their Category Health Conditions and Diseases amyloidosis amyloidosis. Topics. amyloidosis Accumulation in the tissues of various insolublefibrillar proteins (amyloid) in amounts sufficient to impair normal function.
http://www.merck.com/pubs/mmanual/section2/chapter18/18a.htm

Extractions: This Publication Is Searchable The Merck Manual of Diagnosis and Therapy Section 2. Endocrine And Metabolic Disorders Chapter 18. Amyloidosis Topics [General] [General] Amyloidosis: Accumulation in the tissues of various insoluble fibrillar proteins (amyloid) in amounts sufficient to impair normal function. Etiology, Pathophysiology, and Classification The cause of amyloid production and its deposition in tissues is unknown. In the different biochemical types of amyloidosis, etiologic mechanisms may vary. For example, in secondary amyloidosis (see below Three major types of amyloid and several less common forms have been defined biochemically. The first type, which has an N-terminal sequence that is homologous to a portion of the variable region of an immunoglobulin light chain, is called AL and occurs in primary amyloidosis and in amyloidosis associated with multiple myeloma. The second type has a unique N-terminal sequence of a nonimmunoglobulin protein called AA protein and occurs in patients with secondary amyloidosis. The third type, which is associated with familial amyloid polyneuropathy, is usually a transthyretin (prealbumin) molecule that has a single amino acid substitution. Other hereditary amyloids have been found to consist of mutant gelsolin in some families, mutant apolipoprotein A-I in several others, and other mutant proteins in hereditary cerebral artery amyloid. In the amyloid associated with chronic hemodialysis, -microglobulin has constituted amyloid protein. Amyloid associated with aging in skin and with endocrine organs may represent other biochemical forms of amyloidosis. The amyloid found in the histopathologic lesions of Alzheimer's disease consists of
Head And Neck Manifestations Of Amyloidosis
Written by J. Cary Moorhead, MD for the Baylor College of Medicine.
http://www.bcm.tmc.edu/oto/grand/4992.html

Extractions: The information contained within the Grand Rounds Archive is intended for use by doctors and other health care professionals. These documents were prepared by resident physicians for presentation and discussion at a conference held at The Baylor College of Medicine in Houston, Texas. No guarantees are made with respect to accuracy or timeliness of this material. This material should not be used as a basis for treatment decisions, and is not a substitute for professional consultation and/or peer-reviewed medical literature. HEAD AND NECK MANIFESTATIONS OF AMYLOIDOSIS April 9, 1992 Amyloidosis is not a specific disease per se, but rather is the result of a number of unrelated disease processes leading to deposition of extracellular protein in tissues throughout the body. This disease frequently presents with head and neck manifestations. Amyloidosis is typified by extracellular deposition of insoluble proteinaceous material which has typical staining properties and electron microscopic appearance. Its hallmark is an apple green birefringence under polarized microscopy. Under the electron microscope, amyloid appears as a mass of rigid, nonbranching fibrils. X-ray crystallography reveals that these fibrils have a regular, antiparallel, beta-pleated sheet configuration. Amyloidosis can affect virtually any organ or tissue in the body. The most common presenting symptoms are fatigue or weakness, weight loss, ankle edema, dyspnea, paresthesias, and light-headedness or syncope. The most common physical findings are hepatosplenomegaly, edema, macroglossia, orthostatic hypotension and purpura. A number of associated syndromes are frequently seen, including carpal tunnel syndrome, peripheral neuropathy, nephrotic syndrome, congestive heart failure and sprue. The most significantly involved organ systems are the kidneys and heart. Failure of these two systems also constitutes the two leading causes of death.
Atlas Of Pathology
Picture of the heart affected by amyloidosis by the Urbana Atlas of Pathology.
http://www.med.uiuc.edu/PathAtlasf/Atlas69.html

Extractions: Back to Previous Image Arrow 1 depicts the peripherally located nuclei in the cross section of cardiac muscle . Notice the wide spacing between the cardiac muscle cells. This is due to the deposition of amyloid seen for example at arrow 2. This is being viewed with non-polarized light. With this stain the amyloid is a light salmon pink. Click for image To Next Image To Table of Contents To Alphabetical Index To Start
Symptoms Of Amyloidosis
Ask the doctor medical forum for patients hosted by Med Help. A brief look at this disease and the symptoms.
http://www.medhelp.org/perl6/neuro/archive/4773.html
Amyloidosis
Join the discussion on all forms of the bone marrow disease covering the latest medical research and individual case studies. amyloidosis Menu. This is a webforum to discuss and comment on amyloidosis.
http://neuro-www.mgh.harvard.edu/forum/AmyloidosisMenu.html

Extractions: This is a webforum to discuss and comment on Amyloidosis. Click here to Enter a new Neurology WebForum article... This Web Forum is not moderated in any sense. Anyone on the Internet can post articles or reply to previously posted articles, and they may do so anonymously. Therefore, the opinions and statements made in all articles and replies do not represent the official opinions of MGH and MGH Neurology. Neither is MGH or MGH Neurology responsible for the content of any articles or replies. No messages are screened for content. - Very Important Message! - Please Click Here to Read Current Posts: Oct 10, 1997 to Present Useful Websites can be found and posted here! IMPORTANT: If this page seems to be missing recently added documents, click the "Reload Page" button on your Web Browser to update the menu. Return to the main Neurology WebForum Page. These forums are maintained by the Department of Neurology at Massachusetts General Hospital
Atlas Of Pathology
A gross specimen of a liver by Urbana Atlas of Pathology.
http://www.med.uiuc.edu/PathAtlasf/Atlas67.html

Extractions: Back to Previous Image This is a gross specimen of a liver. In comparison to a normal liver, this one has a gray-red and glassy appearance. This is especially noticeable in the areas to the right and left of the "6" mark on the ruler. Had this liver been stained with Lugol's solution, (an iodine containing solution) the amyloid would have stained a mahogany brown. Click for image To Next Image To Table of Contents To Alphabetical Index To Start
Peripheral Neuropathy And Amyloidosis
Ask the doctor medical forum for patients hosted by Med Help.
http://www.medhelp.org/perl6/neuro/archive/10656.html
Amyloidosis Support Network - What Is Amyloidosis?
What Is amyloidosis? amyloidosis is a group of diseases in which one or moreorgan systems in the body accumulate deposits of abnormal proteins.
http://amyloidosis.org/whatisit.asp

Extractions: Please help... Your donation will go for research to help find a cure... learn more! What Is Amyloidosis? Amyloidosis is a group of diseases in which one or more organ systems in the body accumulate deposits of abnormal proteins. The name "amyloidosis" was first used more than 100 years ago but cases were described over 300 years ago. However, only within the past 20 years have physicians understood the specific make-up and structure of amyloid protein. Although amyloidosis is not cancer, it is very serious. It may be disabling or life threatening. However, growing awareness of the condition seems to be leading to substantial new research and treatment alternatives. There are three major types of amyloidosis that are all very different from each other: 1. PRIMARY AMYLOIDOSIS is a plasma cell disorder which originates in the bone marrow and is usually treated with chemotherapy. It is the most common type of amyloidosis in the United States, with estimates of up to 2000 cases diagnosed each year, and occasionally occurs with multiple myeloma. The deposits in this type of the disease are made up of immunoglobulin light chain proteins which may be deposited in any bodily tissues or organs. The disease results when enough amyloid protein builds up in one or more organs to cause the organ(s) to malfunction. The heart, kidneys, nervous system and gastrointestinal tract are most often affected.
Atlas Of Pathology
A picture of group of proteins arranged in a Bpleated sheet affecting a blood vessel.
http://www.med.uiuc.edu/PathAtlasf/CVAtlas020.html
Amyloidosis Support Network
Network's primary function is to "link those affected by amyloidosis to further support resources" and to educate the public
http://www.amyloidosis.org/

Extractions: Please help... Your donation will go for research to help find a cure... learn more! Mission Statement The Network's primary function is to "link those affected by amyloidosis to further support resources" and to educate the public and professionals so that the disease can be recognized earlier and appropriately treated. This web page is intended to streamline this support network and provide complete, integrated, easy-to-reach, direct access links to existing information and referrals for other sources of help, primarily for patients/families struggling with the disease. What is Amyloidosis? Amyloidosis is a group of diseases in which one or more organ systems in the body accumulate deposits of abnormal proteins. The name "amyloidosis" was first used more than 100 years ago but cases were described over 300 years ago. However, only within the past 20 years have physicians understood the specific make-up and structure of amyloid protein. Although amyloidosis is not cancer, it is very serious. It is disabling or life threatening. However, growing awareness of the condition seems to be leading to substantial new research and treatment alternatives. Click here for a more detailed description of the main types of Amyloidosis Click here for an overview of Primary Systemic AL Amyloidosis
Health And Medical Information: Diseases And Conditions, Medical Dictionary, Pro
MedicineNet.com With its definition, symptoms, diagnosis, and treatment.
http://www.medicinenet.com/Script/Main/Art.asp?li=MNI&d=51&cu=16583&
THE MERCK MANUALHome Edition, Sec. 12, Ch. 142, Amyloidosis
Chapter 142. amyloidosis. amyloidosis is a disease in which amyloid, an unusual proteinthat normally isn't present in the body, accumulates in various tissues.
http://www.merck.com/mrkshared/mmanual_home/sec12/142.jsp
AL Primary Cutaneous Amyloidosis
(6) Longterm AL primary amyloidosis. Patients who present with cutaneous featuresof amyloidosis usually undergo an evaluation to categorize the disease.
http://dermatology.cdlib.org/DOJvol1num2/amyloidosis/amyloidosis.html

Extractions: Volume 1, Number 2 This is a case report of AL primary amyloidosis with involvement limited to the skin for more than twenty years before the development of internal organ involvement. The clinical features suggested the systemic form of amyloidosis, rather than that found with nodular cutaneous amyloidosis. Longstanding lesions of nodular amyloidosis even in the face of a negative workup for internal involvement, can be consistent with systemic disease. This is an example of a patient who had extensive cutaneous amyloidosis for twenty years before developing cardiac involvement which then lead to her death. Patients who present with cutaneous features of amyloidosis usually undergo an evaluation to categorize the disease. Skin biopsy with ultrastructural immunohistochemical stains can help confirm the presence and subtype of amyloid. Once a patient has been found to have cutaneous amyloidosis, an extensive workup must be done to evaluate patients for the possibility of systemic involvement. Workup for systemic disease includes: serum and urine immunoelectrophoresis, rectal mucosal or abdominal fat biopsy, bone marrow biopsy, CBC, chemistry panel, and skull and spine X-rays. The origin of the amyloid and the extent of internal involvement are used to determine the approach to treatment.
Amyloidosis
Describes treatment and research that is being undertaken for this condition at the Boston Medical Center.
http://sunset.backbone.olemiss.edu/~lwaej/sharamli.html

Extractions: Published in the July/August 1993 issue of The Barker What is Amyloidosis? A generic term for a collection of diseases that result in the abnormal deposition of amyloid protein throughout the body. How is Amyloid Made? When inflammation occurs, certain chemicals are produced and released into the blood. These chemicals of inflammation are called the Acute Phase Reactant Proteins (APP). After the inflammation has gone away, the APP are broken down by the body and excreted. Dogs (or people) with amyloidosis can't break these APP down into excretable form and instead turn it into Amyloid AA and dump it outside the cells but still within the body. Why does the Amyloid make them sick? Amyloid is constantly deposited outside the cells. It builds up like a garbage heap in an alley vay until it starts to squeeze the adjacent cell walls. The compressed cells can't work properly. The damage or disease that results depends on what kinds of body cells are most severely damaged or killed. Kidncys can't heal themselves by growing new kidney cells. If a kidney cell dies, it is gone for good and can't be replaced. This is why the amyloid protein usually causes kidney failure first.
Biphasic Cutaneous Amyloidosis
Biphasic cutaneous amyloidosis Ming H. Jih Dermatology Online Journal 7(2)15. The pathogenesis of cutaneous amyloidosis is poorly understood.
http://dermatology.cdlib.org/DOJvol7num2/nyu2/5/5.html

Extractions: refs = new Array("References:","Brownstein MH, et al. Biphasic amyloidosis: link between macular and lichenoid forms. Br J Dermatol 88:25, 1973 ", "Bedi TR, et al. Diffuse biphasic cutaneous amyloidosis. Dermatologica 158:433, 1979 ", "Barnadas MA, et al. Papules in the auricular concha: lichen amyloidosis in a case of biphasic amyloidosis. Dermatologica 181:149, 1990 ", "Eswarammorthy V, et al. Macular amyloidosis: etiologic factors. J Dermatol 26:305, 1999 ", "Presenter: Ming H. Jih, M.D., Ph.D."); DOJ New York University Department of Dermatology This 25-year-old Malaysian man, who was evaluated at Bellevue Hospital Medical Center for diffuse cutaneous dyspigmentation of more than twenty years duration. He had recently moved to the United States and was admitted for pulmonary tuberculosis. He was born of a non-consanguinous conception with no cutaneous or other anomalies at birth, and there was no family history of skin disorders. During his childhood, he gradually developed hyperpigmentation of the entire upper and lower extremities as well as of portions of his back and shoulders. The lesions were asymptomatic, and he denied scratching or rubbing the affected areas. There also was no history of any preceding inflammation or trauma to the skin. Figure 1 Figure 2 Dyspigmentation consisting of both macular and papular hyper- and hypopigmentation was noted on the extremities with lesser involvement of the shoulders and back. There was sparing of the palms, soles, and oral mucosa.

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