The very first topic discussed at my very first class in Pathology at Thomas Jefferson Medical School was on the topic of amyloidosis. After the class was over, I asked the teacher why we were discussing amyloidosis first, when so many other medical conditions, such as heart disease or cancer, were much more prevalent. His answer: he was a researcher in on the topic of amyloidosis and that's what he knew best.

Amyloidosis is a rare plasma cell proliferative disorder and difficult to diagnose. The clinical syndromes at the time of presentation include protein in the urine with or without renal failure, heart failure, liver enlargement, and autonomic or peripheral neuropathy. The serum immunoglobulin free light chain assay has been an important step forward in classifying systemic amyloidosis as an immunoglobulin light chain form and in monitoring therapy. Recently, the importance of serum cardiac biomarkers in assessing outcome has been recognized.

Subscribe to a FREE Supplement Research Update newsletter. Twice a month you will receive an email with reviews of several studies on various supplements and natural medicine topics, including amyloidosis research, and their practical interpretation by Ray Sahelian, M.D.

Amyloidosis symptom
Amyloidosis is difficult to diagnose because the symptoms at presentation are vague and include shortness of breath, paresthesias (tingling sensations in the nerves), edema, weight loss, and fatigue. Many diseases can cause similar symptoms. The symptoms of amyloidosis depend on the organs affected by the deposits, which can include the tongue, intestines, skeletal and smooth muscles, nerves, skin, ligaments, heart, liver, spleen, and kidneys.

Primary amyloidosis
Primary amyloidosis is a disorder in which insoluble protein fibers are deposited in tissues and organs. The cause of primary amyloidosis is not known for certain, but primary amyloidosis is related to abnormal production of immunoglobulins by a type of immune cell called plasma cells.

Macular Amyloidosis disease
Primary localized cutaneous amyloidosis refers to deposition of amyloid in previously normal skin with no evidence of deposits in internal organs. There are three types of primary cutaneous amyloidosis: nodular cutaneous amyloidosis, macular amyloidosis and lichenoid amyloidosis. Macular and lichenoid forms of primary cutaneous amyloidosis occur relatively commonly and are associated with itching and friction. Macular amyloidosis is the commonest form of primary localized cutaneous amyloidosis. Macular amyloidosis is seen most frequently on the upper back.

Cardiac amyloidosis
Cardiac amyloidosis often occurs during primary amyloidosis. Primary amyloidosis is usually a consequence of multiple myeloma, a blood disease in which a large amount of a certain type of protein is made. This extra protein is deposited in the heart tissue and in other organs such as the kidney.

Renal amyloidosis
Kidney dysfunction is one of the most common presenting features of patients with systemic amyloidosis, and amyloid accumulation can occur leading to renal amyloidosis.

Amyloidosis treatment
New amyloidosis treatment options developed over the past few years include high-dose chemotherapy with stem cell reconstitution, combinations of alkylating agents with dexamethasone, and, most recently, thalidomide.

Amyloid, Obesity, and Alzheimer's Disease
As body fat increases, so do blood levels of a protein fragment linked to Alzheimer's disease, which may explain the reported association between obesity and the brain-wasting disease. Obesity by itself, even in otherwise healthy middle-aged people, is associated with elevated levels of the amyloid peptide that builds up and causes Alzheimer's. Amyloid is normally made all throughout the body at various lengths. Researchers at Edith Cowan University in Joondalup, Western Australia investigated whether levels of the peptide, plasma amyloid-beta 42,were related to body mass index (BMI) or fat mass in 18 healthy adults. As BMI rose, so did amyloid-beta 42 blood levels. The same was true for fat mass. But there was no relationship between BMI or fat mass and another peptide, amyloid-beta 40, which is not associated with disease. Obesity-linked conditions like diabetes and heart disease may also increase Alzheimer's risk, but when the team adjusted the data for levels of insulin, cholesterol, and inflammation in an attempt to account for their influence, the fat-amyloid-beta 42 relationship remained. This suggests that it's the fat itself -- not the diseases that excess weight can cause -- that may be increasing levels of the dangerous protein.

Amyloid Complex causes memory loss
Scientists have identified a substance in the brains of mice that causes memory loss. Using genetically engineered mice that developed memory loss similar to people with Alzheimer's, the researchers discovered that it was caused by a protein complex. Azheimer's is characterised by the build-up of protein deposits called amyloid plaques between nerve cells in the brain and tangles of a protein called tau inside nerve cells. But the tangles and plaques are not the major cause of memory loss. Memory problems can occur in people before they are diagnosed with Alzheimer's and before brain cells begin to die. The scientists hypothesised that there was something else in the brain that caused the memory decline. They found a form of the amyloid beta protein in the transgenic mice that displayed early signs of memory loss but which had no plaques or nerve cell loss. After isolating and purifying the protein complex, whose key component is called amyloid beta peptide which is thought to be linked to the development of Alzheimer's, and injecting it into healthy rats the rodents experienced a decline in their cognitive ability. The researchers believe the protein complex impairs memory independently of plaques or nerve loss and may contribute to the drop in cognitive function associated with Alzheimer's.

Amyloidosis from foie gras ?
Tests on mice suggest that foie gras  liver from force-fed geese, popular in French cuisine -- may cause amyloidosis in animals that have a genetic susceptibility to such diseases. Alan Solomon of the University of Tennessee used mice genetically engineered to be susceptible to amyloidosis, which can be inherited. When these mice were injected with or fed amyloid extracted from foie gras, the animals developed extensive systemic pathological deposits. Like CJD, mad cow disease, scrapie and related diseases, amyloidosis is marked by abnormal protein fragments. In the case of CJD, the proteins are called prions. In addition to foie gras, meat derived from sheep and seemingly healthy cattle may represent other dietary sources of this material.
   Of course, there are many other causes for amyloidosis since most Americans do not eat foie gras and stil get this condition.

Amyloidosis questions
Q. Do you think lipoic acid would be helpful in preventing amyloidosis?
   A. It's an interesting question, but I don't know.

Q. My father has primary amyloidosis and it has affected both his liver as well as the digestive system. Have you known of Tumeric and Curcumin to improve liver function. I respect the work that you do. Have a nice day.