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Amyloidosis: more books (79)

Amyloidosis of the external auditory canal and middle ear: unusual ear tumor.: An article from: Ear, Nose and Throat Journal by Heitham Gheriani, Rajesh Tewary, et all 2007-02-01
Comprehensive Summaries of Uppsala Dissertations from the Faculty of Medicine, Volume 758: Polysaccharides in Alzheimer's Disease and Inflammation-associated Amyloidosis by Birgitta Lindahl, 1998
Amyloidosis: An entry from Gale's <i>Gale Encyclopedia of Medicine, 3rd ed.</i> by Maureen Haggerty, 2006
Amyloidosis; cause and manifestation of senile deterioration by Philip Schwartz, 1970
CUTANEOUS AMYLOIDOSES (AMYLOIDOSIS). Clinics in Dermatology. April-June, 1999, V by Chu-Kwan and Stephen M. Breathnach (Guest Editors). WONG, 1990
Localized amyloidosis of cardiac and skeletal muscle: investigate promptly where it manifests.(Letter to the editor): An article from: Southern Medical Journal by Claudia Stollberger, Christina Steger, et all 2006-01-01
Amyloidosis: Webster's Timeline History, 1944 - 2007 by Icon Group International, 2010-03-10
Lichen amyloidosis: in-office procedure cuts pain.(Dermatologic Surgery): An article from: Skin & Allergy News by Betsy Bates, 2005-03-01
Lost in Amyloidosis by Steve Keller, 2008-02-26
Deaths From Amyloidosis: David Lange
Hypertrophic cardiomyopathy and symptomatic conduction system disease in cardiac amyloidosis.(Case Report)(Clinical report): An article from: Southern Medical Journal by Praveen Garg, Ruchi Gupta, et all 2006-12-01
Surgical rehabilitation for primary laryngeal amyloidosis.: An article from: Ear, Nose and Throat Journal by Sofia Avitia, Jason S. Hamilton, et all 2007-04-01
Amyloidosis and its impact on patients with ESRD.(Continuing Education)(End-Stage Renal Disease): An article from: Nephrology Nursing Journal by Sandra D. Copeland, 2006-01-01
Deaths From Amyloidosis: Transmissible Spongiform Encephalopathies, Prion, Fatal Familial Insomnia, Creutzfeldt-jakob Disease, Robert Jordan

lists with details

Dermatlas: Online Dermatology Image Library Dermatology Image,amyloidosis, Bullo
Dermatlas Dermatology Images dermatology image,amyloidosis,amyloidosis,amyloidosis,amyloidosis,amyloidosis,amyloidosis,amyloidosis,amyloidosis,amyloidosis
http://dermatlas.med.jhmi.edu/derm/result.cfm?Diagnosis=-609213408
Amyloidosis
amyloidosis related to plasma cell dyscrasia is not curable. The role of chemotherpay, and cytokine therapy is discussed. amyloidosis.
http://www.clevelandclinic.org/myeloma/amyloidosis.htm

Extractions: PREVALENCE AND INCIDENCE OF AMYLOIDOSIS Amyloidosis is a rare disease. About two-thirds of patients with amyloidosis have primary (where no specific cause or disease is related to the abnormal protein deposits), less than 5% have secondary (associated with another chronic disease, often in multiple myeloma), less than 5% familial (inherited) and less than 5% have senile (occurring secondary to old age) amyloidosis. In patients with primary amyloidosis, 95% are over the age of 40 and 66% are men.
Amyloidosis Menu
amyloidosis Menu. These are articles related to amyloidosis issues. Please feel free to browse ATTENTION information! New amyloidosis Web Site!
http://neuro-www.mgh.harvard.edu/neurowebforum/AmyloidosisMenu.html
Amyloidosis
amyloidosis. by George Jones. amyloidosis is the presence of abnormal amyloid protein deposited throughout an animals body. amyloidosis is fatal.
http://www.barkbytes.com/medical/med0018.htm

Extractions: Amyloidosis by George Jones Amyloidosis is the presence of abnormal amyloid protein deposited throughout an animals body. When inflammation occurs, specific chemicals are produced and released into the dogs blood stream. These chemicals are called Acute Phase Reactant Proteins (APP). Once the inflammation has cleared, the APPs are broken down by the body and excreted. In a dog with amyloidosis the body can not break the APPs into an excretable form. The partial break down results in the conversion of APPs into Amyloid AA. Amyloid AA is not excretable by the body. Amyloid AA is deposited outside the cells but remains within the body. With repeated bouts of inflammation the Amyloid AA is progressively built up until the deposits start compressing adjacent cell walls. These compressed cells can not properly function. The resulting damage or disease will be dependent upon the locations involved in Amyloid AA deposits. The kidneys are most commonly affected by Amyloidosis. Unlike other cells within the body, when a kidney cell is damaged, it dies. However, kidney cells can not be replaced. The kidneys do not generate new cells. For this reason the amyloid protein most often causes kidney failure first. Amyloidosis is fatal. Deaths have be reported ranging from eight months of age to 12 years. The most common ages being between 3 and 5 years old.
Amyloidosis
Blood/Lymphatic System. Hemophilia. Mononucleosis. amyloidosis. Note All links within content go to MayoClinic.com. Diseases and Conditions. amyloidosis.
http://www.cnn.com/HEALTH/library/DS/00431.html

Extractions: Blood/Lymphatic System Hemophilia Mononucleosis Amyloidosis INFORMATION CENTERS: Pick a category Health Centers Family Health Men's Health Women's Health Children's Health Seniors' Health Working Life Pain Management Condition Centers Immune System Allergy Alzheimer's Arthritis Respiratory System Cancer Endocrine System Digestive System Heart and Blood Infectious Disease Mental Health Note: All links within content go to MayoClinic.com Diseases and Conditions Amyloidosis From MayoClinic.com Overview Amyloidosis is a rare and potentially fatal disease that occurs when amyloid proteins build up in your body's organs. Amyloid is an abnormal protein produced by cells in your bone marrow that can deposit in any of your body's tissues or organs. Amyloidosis occurs when enough amyloid protein builds up in one or more organs to cause the organ or organs to malfunction. The disorder frequently affects the heart, kidneys, liver, spleen, nervous system and gastrointestinal tract. Amyloidosis may be associated with certain forms of cancer (multiple myeloma, Hodgkin's disease) and the intestinal disorder, familial Mediterranean fever. In other cases, it may occur as a result of kidney disease in people who have undergone long-term dialysis therapy.
Amyloidosis
amyloidosis. General Considerations. (Note Amyloid can be studied in the context of cell injury or immunological diseases. Pathogenesis of amyloidosis.
http://chemo.net/newpage1.htm

Extractions: Amyloid Protein Amyloidosis 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 -- ECureMe.com
amyloidosis, more about amyloidosis, In primary amyloidosis (called AL) the protein fibrils are made up of the light chain portions of antibodies.
http://www.ecureme.com/emyhealth/data/Amyloidosis.asp

Extractions: DisplayAd("468","60"); Select a Health Topic ADD/ADHD Allergy Alternative Medicine Arthritis Asthma Beyond Dieting Body Aches and Pains Breast Cancer Cancer Awareness Cardio Health Children's Health Colon Cancer Contraception COPD/Emphysema Dental Health Diabetes Elder Care Emergency Room Epilepsy Erectile Dysfunction Eye Care Fertility Fitness Gastrointestinal Health Glands and Hormones Gynecologic Health Hair Loss Headache Healthcare Today Healthy Aging HIV and AIDS Infectious Diseases Kidney Health Leukemia Liver Health Lung Cancer Lymphoma Multiple Sclerosis Men's Health Mental Health Nutrition Osteoporosis Parkinson's Disease Sexual Health Skin Health Sleep Disorders Special Events Stroke Surgeries and Procedures Teen Health Thyroid Health Urologic Health Vascular Disease Women's Health Workplace Health June 2, 2004 Resource Links Physician Search Your Questions, Amyloidosis is a condition in which amyloids, i.e., protein fibrils (minute fibers) not normally present in the body, become deposited in one or more sites, damaging the organs where they collect. Virtually any organ in the body may be affected. Symptoms are determined by the location of the buildup, and vary from mild to severe and life threatening. There are two forms of this condition: primary and secondary. In primary amyloidosis (called AL) the protein fibrils are made up of the light chain portions of antibodies. Typical sites of fibril pooling are the heart, lungs, skin, tongue, blood vessels, kidney, liver, and thyroid gland. The cause of this form is not known.
Amyloidosis
The term amyloidosis includes a group of disorders caused by abnormal folding, clumping, (aggregation) and/or accumulation of particular proteins (amyloids
http://www.bchealthguide.org/kbase/nord/nord22.htm

Extractions: It is possible that the main title of the report is not the name you expected. Please check the synonyms listing to find the alternate name(s) and disorder subdivision(s) covered by this report. Secondary Amyloidosis Transthyretin Methionine-30 Amyloidosis (Type I) Indiana Type Amyloidosis (Type II) Danish Cardiac Type Amyloidosis (Type III) Iowa Type Amyloidosis (Type IV) Finnish Type Amyloidosis (Type V) Icelandic Type Amyloidosis (Type VI) Ohio Type Amyloidosis (Type VII) Familial Visceral Amyloidosis (Type VIII) Familial Lichen Amyloidosis (Type IX) Appalachian Type Amyloidosis Analine 60 Amyloidosis Ashkenazi Type Amyloidosis Isoleucine 33 Amyloidosis Corneal Amyloidosis Amyloid Corneal Dystrophy Familial Cutaneous Amyloidosis Hemodialysis-Related Amyloidosis A Beta-2-Microglobulin Amyloidosis Amyloid Arthropathy of Chronic Hemodialysis Amyloidosis Illinois Type Amyloidosis Prealbumin Tyr-77 Amyloidosis Amyloidosis of Familial Mediterranean Fever Atypical Amyloidosis Cardiopathic Amyloidosis Hereditary Nephropathic Amyloidosis Idiopathic Amyloidosis Lichen Amyloidosis Macular Amyloidosis Neuropathic Amyloidosis Paramyeloidosis Pericollagen Amyloidosis Portuguese Type Amyloidosis
VETERINARY INFORMATION SERVICE
VETERINARY INFORMATION SERVICE. Familial amyloidosis in Abyssinian Cats. Most amyloidosis is etiopathic; that is no underlying cause can be found.
http://www.pressenter.com/~dvmvis/amyloid.htm
Amyloidosis
amyloidosis Primary amyloidosis is a plasma cell disorder and occasionally occurs with multiple myeloma. amyloidosis was first described in the 19th Century.
http://www.medical-library.net/sites/_amyloidosis.html

Extractions: by Ron Kennedy, M.D., Santa Rosa, California Amyloidosis was first described in the 19th Century. Recently significant advances been made in understanding the disease. Amyloidosis is now known to be a group of diseases in which one or more organ systems in the body accumulates protein deposits. There are three major types, all very different from each other. 1. Primary Amyloidosis Primary amyloidosis is a plasma cell disorder and occasionally occurs with multiple myeloma. This is the most common type of amyloidosis in the United States and is usually treated (conventionally) with chemotherapy. Primary amyloid is not associated with any other diseases. In primary amyloidosis, the organs most often involved include the heart, kidneys, nervous system, and gastrointestinal tract. Amyloid deposits in these organs cause shortness of breath, fatigue, edema (swelling of ankles and legs), dizziness upon standing, a feeling of fullness in the stomach (especially after eating), diarrhea, weight loss, enlarged tongue, numbness of the legs and arms, and protein in the urine. 2. Secondary Amyloidosis
Amyloidosis: Gastrointestinal Manifestations
amyloidosis gastrointestinal manifestations.
http://chorus.rad.mcw.edu/doc/00866.html
Amyloidosis: Bone Manifestations
amyloidosis bone manifestations. joint pain without radiographic findings; osteoporosis, esp. in axial skeleton; lytic lesions that
http://chorus.rad.mcw.edu/doc/01185.html
Amyloidosis
amyloidosis. amyloidosis is a progressive, incurable, metabolic disease characterized by abnormal deposits of protein in one or more organs or body systems.
http://www.chclibrary.org/micromed/00037170.html

Extractions: Amyloid proteins are manufactured by malfunctioning bone marrow. Amyloidosis, which occurs when accumulated amyloid deposits impair normal body function, can cause organ failure or death . It is a rare disease, occurring in about eight of every 1,000,000 people. It affects males and females equally and usually develops after the age of 40. At least 15 types of amyloidosis have been identified. Each one is associated with deposits of a different kind of protein. Types of amyloidosis The major forms of this disease are primary systemic, secondary, and familial or hereditary amyloidosis. There is also another form of amyloidosis associated with Alzheimer's disease Primary systemic amyloidosis usually develops between the ages of 50 and 60. With about 2,000 new cases diagnosed annually, primary systemic amyloidosis is the most common form of this disease in the United States. Also known as light-chain-related amyloidosis, it may also occur in association with multiple myeloma (bone marrow cancer).
VASCULITIS, AMYLOIDOSIS, IMMUNODEFICIENCY
VASCULITIS, amyloidosis, IMMUNODEFICIENCY (EXCEPT AIDS) Ed Friedlander, MD, Pathologist erf@uhs.edu. Recognize possible amyloidosis patients.
http://www.pathguy.com/lectures/imm-iii.htm

Extractions: scalpel_blade@yahoo.com Cyberfriends: The help you're looking for is probably here. Welcome to Ed's Pathology Notes, placed here originally for the convenience of medical students at my school. You need to check the accuracy of any information, from any source, against other credible sources. I cannot diagnose or treat over the web, I cannot comment on the health care you have already received, and these notes cannot substitute for your own doctor's care. I am good at helping people find resources and answers. If you need me, send me an E-mail at scalpel_blade@yahoo.com Your confidentiality is completely respected. Allan N. Spreen MD also handles internet questions at no charge, with a primary focus on nutrition. Dr. Spreen is also my former student and my close friend. DoctorGeorge.com is a larger, full-time service. There is also a fee site at myphysicians.com , and another at www.afraidtoask.com
Amyloidosis.
amyloidosis is an umbrella term that describes diseases caused by abnormal deposits in the body of the protein amyloid. amyloidosis.
http://www.betterhealth.vic.gov.au/bhcv2/bhcarticles.nsf/pages/Amyloidosis?open
Amyloidosis
amyloidosis. What is it? Who gets it? amyloidosis occurs in only eight of every one million people. Symptoms usually occur after age 40.
http://www.hmc.psu.edu/healthinfo/a/amyloidosis.htm
UCL Centre For Amyloidosis And Acute Phase Proteins
Welcome to The Centre for amyloidosis and Acute Phase Proteins The Centre conducts world leading research in all aspects of the pentraxin family of plasma
http://www.ucl.ac.uk/medicine/amyloidosis/

Extractions: The Centre conducts world leading research in all aspects of the pentraxin family of plasma proteins, and in amyloidosis, ranging from structural biology, through molecular, genetic, biochemical, physiological and pathological studies, to clinical diagnostics, patient management and new drug discovery. There are extensive collaborative links with scientists, clinicians and industry in many of these areas. The goal is to elucidate fundamental normal and pathobiological mechanisms in order to improve diagnosis, management and outcome of disease. Apart from all aspects of amyloidosis, for which the NHS National Centre is located in this Department, there are particular interests in coronary heart disease and atherothrombosis generally, and in inflammatory and autoimmune diseases. Centre Director: Professor Mark Pepys FRS Professor Philip Hawkins
National Amyloidosis Centre
NATIONAL amyloidosis CENTRE amyloidosis. Other rare forms of amyloidosis have a genetic basis, most of which can now be identified by DNA tests.
http://www.ucl.ac.uk/medicine/amyloidosis/nac/nac1.html

Extractions: The term amyloidosis describes a group of disorders caused by abnormal folding, aggregation and accumulation of certain proteins in the tissues. These unusually stable protein deposits are called amyloid and they progressively disrupt the function of affected organs. Normal proteins are cleared away at about the same rate that they are produced, but in amyloidosis, amyloid is deposited more rapidly than it can be broken down. Amyloid deposits can accumulate virtually anywhere in the body or can remain quite localised. They produce symptoms by interfering with the structure and function of normal tissues. Patients may develop problems involving many different organs or mainly a single organ, for example the kidneys or heart. Although several potential amyloid dispersing drugs are undergoing clinical trials, none as yet have been shown to be of benefit. However, existing treatments for the various conditions that underlie amyloidosis can stabilise or improve organ function, and greatly improve the outlook in general. Contrary to previous expectations, we have shown that amyloid deposits gradually diminish in most patients whose underlying conditions respond to treatment.
Arthritis Research Campaign | AA Amyloidosis
Table 1. Classification of amyloidosis. Amyloid Protein, Protein Precursor, Clinical. AA, SAA, Reactive (secondary). PATHOGENESIS OF REACTIVE amyloidosis.
http://www.arc.org.uk/about_arth/med_reports/series3/tr/6408/6408.htm

Extractions: (Muckle-Wells' syndrome). AL Immunoglobulin light chains Idiopathic (primary), myeloma or macroglobulinaemia-associated. ATTR Transthyretin (prealbumin) Familial amyloid polyneuropathy, Portuguese type; familial amyloid cardiomyopathy, Danish type. Familial amyloid polyneuropathy, Iowa type; Hereditary non-neuro pathic systemic amyloidosis (Ostertag-type). AGel Gelsolin Familial amyloidosis, Finnish type.
It Is Generally Considered That The Amyloidoses Share Common Pathogenic Mechanis
These mechanisms may include structural, metabolic, genetic and environmental factors which may be common to all forms of amyloidosis, but due to the sporadic
http://www.iupui.edu/~amyloid/primary.htm

Extractions: I Primary Amyloidosis Primary amyloidosis is a disease caused by the abnormal accumulation of protein molecules in body tissues. These proteins are fragments of immunoglobulin (antibody) molecules which are normally present in the blood to give protection against bacteria and other infectious agents. Normally, antibody molecules are constantly being synthesized by cells of the immune system and then, after a finite life span, degraded so that there is a balance between production and degradation. In this way our active immune system protects our bodies from a constantly changing array of infectious bacteria and viruses. In primary amyloidosis a defect occurs in the immune system. Excessive amounts of certain antibody molecules are produced and fragments of these molecules get deposited in tissues. These tissue deposits, as they enlarge, damage normal tissues and cause the disease that we know as primary amyloidosis. The cause of primary amyloidosis is unknown. Since the amyloid protein comes from immunoglobulin molecules, it is possible that some response of the immune system to an infectious bacteria, virus or other foreign substance may trigger the overproduction of antibody protein. So far this is only speculation, because amyloid has not been known to be associated with any particular infection. Indeed, there are no epidemiological data to suggest that amyloid occurs as result of infection. More is known about how the antibody molecules are deposited in tissue and lead to the disease. It is known that antibody molecules are made only by certain cells in the immune system called plasma cells. It is known that plasma cells can synthesize large amounts of antibody molecules but are usually under regulatory mechanisms that maintain a balance.

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