Rare Disease Database

rarediseases.org/rare-diseases/amyloidosis/

Amyloidosis

NORD gratefully acknowledges Vaishali Sanchorawala, MD, Director of Amyloidosis Center,

Boston University School of Medicine and Boston Medical Center, for assistance in the
preparation of this report.

Subdivisions of Amyloidosis

AL amyloidosis
ATTR amyloidosis – ATTRm or ATTRwt amyloidosis
AA amyloidosis
dialysis-related beta2-microglobulin amyloidosis (ABM2)

General Discussion

Amyloidosis is a systemic disorder that is classified into several types. The different
types of amyloidosis are classified as systemic or localized. AL (immunoglobulin light
chain, historically known as primary) amyloidosis is the most common type of systemic
amyloidosis. AL amyloidosis results from an abnormality (dyscrasia) of a type of white
blood cell called plasma cells in the bone marrow, and is closely related to multiple
myeloma. AA (historically known at secondary) amyloidosis is derived from the
inflammatory protein serum amyloid A. AA amyloidosis occurs in association with
chronic inflammatory disease such as the rheumatic diseases, familial Mediterranean
fever, chronic inflammatory bowel disease, tuberculosis or empyema. Hereditary
amyloidosis is a rare type of amyloidosis that is caused by an abnormal gene. There are
several abnormal genes that can cause hereditary amyloidosis, but the most common
type of hereditary amyloidosis is called ATTR and caused by mutations in the
transthyretin (TTR) gene. Age related amyloidosis, in which the amyloid is derived from
wild-type (normal) transthyretin, is a slowly progressive disease that affects the hearts of
elderly men and is called ATTRwt amyloidosis. Amyloid deposits may occasionally occur
in isolation without evidence of a systemic disease; isolated bladder or tracheal
amyloidosis are the most common such presentations. Dialysis-related beta2-
microglobulin amyloidosis is a type of systemic amyloidosis that can occur in individuals
who have experienced long-term kidney dialysis to remove accumulated impurities or
wastes in the blood by mechanical filtration. This form of amyloidosis, also known as

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ABM2 (amyloid associated with the beta-2m protein), is associated with the aggregation
of beta2-microglobulin, a type of amyloid protein that is cleared in the normally-
functioning kidney. Dialysis-related beta2-microglobulin amyloidosis occurs in patients
with near end-stage renal disease. It does not affect individuals with normal or mildly
reduced renal function or patients with a functioning renal transplant.

Signs & Symptoms

Amyloidosis is usually a multisystem disease resulting in a wide spectrum of clinical

presentations. Consequently, a patient may present to, or be referred to, one of several
subspecialists, most commonly a nephrologist, cardiologist or neurologist. Recent
advances in therapy have rendered early and precise diagnosis critical if the patient is to
fully benefit. Most patients have more than one organ involved and therefore the finding
of a combination of any of the features below should heighten the suspicion of
amyloidosis:

The kidney is the organ most commonly involved in AL amyloidosis and AA amyloidosis,
however, rarely involved in hATTR amyloidosis. Excessive amounts of protein in the
urine (proteinuria) is the usual manifestation of renal involvement and is commonly
heavy, resulting in the nephrotic syndrome. Less commonly, amyloid causes an excess
of urea and other nitrogenous wastes in the blood (progressive azotemia) as the initial
manifestation of renal disease. An abnormal accumulation of fluid (edema), such as
swelling of the legs and abdomen, in the absence of heart failure is a feature of
nephrotic syndrome, as is the presence of excess cholesterol in the blood
(hypercholesterolemia) that may be profound. The kidneys often become small, pale and
hard, but in amyloidosis, large kidneys are commonly seen as well.

Amyloidosis frequently involves the heart. The heart is commonly involved in AL and
ATTRm amyloidosis and is the most common phenotype of ATTRwt amyloidosis.
Amyloid infiltration of the heart results in ventricular wall thickening and the development
of heart failure. Rapidly progressive congestive heart failure with thick ventricular walls is
the classical presentation of AL cardiac amyloidosis. The heart is invariably involved in
senile amyloidosis, often in TTR amyloidosis and almost never in the secondary
amyloidosis. Common symptoms of heart involvement include: an enlarged heart
(cardiomegaly); an irregular heartbeat (arrhythmias); and abnormalities of the heart seen
on electrocardiograms (for example: low voltage). Congestive heart failure is the most
common cardiac complication of amyloidosis. Nodular deposits of amyloid may be
present on the membranous sac that surrounds the heart (pericardium) and on the lining
of the heart chambers or heart valves (endocardium).

Although less common than renal or cardiac involvement, neuropathy may be a

significant problem in amyloidosis. Occasionally, it is the presenting and predominant
feature of AL amyloidosis. In specific mutations of hereditary amyloidosis (particularly
V30M originally known as familial amyloid polyneuropathy), it is the primary feature of
the disease. The neuropathy is often painless and sensorimotor in nature although
neuropathic pain may be occasionally significant. These symptoms may include:

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sensory neuropathy with numbness and tingling sensations in the feet that progresses to
the legs and eventually the upper extremities; motor neuropathy with loss of motion
beginning in the feet and extending upward. Carpal tunnel syndrome is commonly seen,
not due to direct nerve involvement, but rather to soft tissue infiltration causing median
nerve compression. In hATTR amyloidosis, the peripheral neuropathy is frequently
accompanied by an autonomic neuropathy characterized by diarrhea and a decrease in
the amount of sweat production (hypohidrosis), a sudden drop in blood pressure when
the patient stands up (postural hypotension) and, in the male, erectile dysfunction.
Postural hypotension may be profound and result in recurrent fainting (syncopal)
episodes. Systemic amyloidosis does not involve the central nervous system, and is
unrelated to Alzheimer disease.

Amyloidosis may affect the liver and the spleen. Amyloid involvement in the spleen
increases the risk of spontaneous rupture of that organ. Some degree of hepatic
involvement is common in AL amyloidosis. It is also common in AA amyloidosis but is
not seen in hATTR amyloidosis. In most patients, hepatic involvement is asymptomatic.
An enlarged liver (hepatomegaly) and an enlarged spleen (splenomegaly) are the most
notable signs. Generally, the amyloid-infiltrated liver feels very hard, and elevated liver
enzymes (particularly alkaline phosphatase) and other liver function abnormalities may
be detected early. Generally, the function of the liver is not significantly affected until late
in the course of the disease. Elevation of bilirubin is an ominous sign and may portend
hepatic failure. Hepatic amyloidosis rarely occurs in isolation and is usually associated
with organ involvement elsewhere.

Amyloidosis may also affect the gastrointestinal (digestive) system. Amyloid

accumulation in the gastrointestinal tract may cause a lack of movement (motility) in the
esophagus and the small and large intestines. Malabsorption, ulceration, bleeding, weak
gastric activity, pseudo-obstruction of the gastrointestinal tract, protein loss, and diarrhea
may also occur. Loss of taste, and a difficulty eating solid foods because of enlargement
of the tongue (macroglossia) from amyloid infiltration, may contribute to weight loss, or
weight loss may be a non-specific manifestation of the systemic disease. In patients with
autonomic neuropathy, gastric emptying is impaired, resulting in a sensation of early
satiety.

The skin is frequently involved in primary amyloidosis. Dermatologic involvement is

almost exclusively limited to AL amyloidosis and consists of soft tissue, skin and
vascular abnormalities. Periorbital purpura is a result of capillary fragility and may
appear after coughing, sneezing, or straining for a bowel movement. Not infrequently,
purpuric lesions may arise after such simple actions as rubbing the eyelids. Soft tissue
infiltration may cause macroglossia and hoarseness, although examination of the vocal
cords may appear normal. Lesions of the skin may be visible or may be so small that
they may be seen only with a microscope. Waxy-looking papular lesions may appear on
the face and the neck. They may also occur under the arms (axillary region), near the
anus and the groin. Other areas that may be affected are the mucous areas such as the

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ear canal or tongue. Areas of swelling, hemorrhages under the skin (purpura), hair loss
(alopecia), inflammation of the tongue (glossitis) and a dry mouth (xerostomia) may also
be present.

Problems with the respiratory system that are associated with amyloidosis often parallel
cardiac symptoms. In the localized form of amyloidosis, air passages and ducts may be
obstructed by amyloid deposits in the nasal sinuses, voice box (larynx) and throat
(trachea) and bronchial tree. Fluid collecting in the pleural space (pleural effusion) is
quite common in patients with congestive heart failure due to amyloidosis, but large
recurrent pleural effusions disproportionate to the degree of heart failure suggest pleural
amyloidosis.

Joint abnormalities (arthropathy) occur in amyloidosis due to the accumulation of

amyloid deposits in the lining of joints (synovial membranes). This occurs in AL
amyloidosis and occasionally in dialysis-related amyloidosis. Articular cartilage or the
synovial membrane and fluid may become involved as well. Symptoms are similar to
those of rheumatoid arthritis. Amyloid deposits in muscle tissue may cause muscle
weakness and muscle changes (pseudomyopathy). Symptoms of amyloidosis may also
be manifested by bleeding disorders. These may result from deficiency of certain clotting
factors or small amyloid deposits in blood vessels within the skin.

bones and joints.
Dialysis-related beta2-microglobulin amyloidosis usually affects the
Initial symptoms include carpal tunnel syndrome, shoulder pain and inflammation of the
tendon sheaths of the hands. Case reports of severe pulmonary hypertension and heart
failure also exist.

Causes

Amyloidosis is caused by abnormal folding of normal soluble proteins leading to fibril

formation in one or more body organs, systems or soft tissues. These clumps of protein
are called amyloid deposits and the accumulation of amyloid deposits causes the
progressive malfunction and eventual failure of the affected organ. Normally, proteins
are broken down at about the same rate as they are produced, but these unusually
stable amyloid deposits are deposited more rapidly than they can be broken down.

The cause of AL amyloidosis is usually a plasma cell dyscrasia, an acquired abnormality

of the plasma cell in the bone marrow with production of an abnormal light chain protein
(part of an antibody). Usually an excess amount of antibody protein is produced and the
abnormal light chain portion or the whole antibody molecule accumulates in the body
tissues in the form of amyloid deposits.

AA amyloidosis is caused by the inflammatory disease process that is part of the

underlying disease. Approximately 50% of the people with secondary amyloidosis have
rheumatoid arthritis as the underlying disease.

Familial amyloidosis (hATTR) is caused by an abnormality in the gene for one of several
particular proteins. The most common form of hereditary amyloidosis is caused by an
abnormality (mutation) in the gene for transthyretin. More than 100 different mutations in

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the transthyretin gene have been reported and the most common mutation has been
termed V30M. Different TTR gene mutations are associated with amyloidosis that affects
different organ systems. Rarely, mutations in genes for proteins that cause amyloidosis
are fibrinogen A alpha chain, apolipoprotein A1 and A2, gelsolin, LECT2 and cystatin C.

All the hereditary amyloidoses follow autosomal dominant inheritance. Most genetic
diseases are determined by the status of the two copies of a gene, one received from
the father and one from the mother. Dominant genetic disorders occur when only a
single copy of an abnormal gene is necessary to cause a particular disease. The
abnormal gene can be inherited from either parent or can be the result of a new
mutation (gene change) in the affected individual. The risk of passing the abnormal gene
from an affected parent to an offspring is 50% for each pregnancy. The risk is the same
for males and females. Not every person getting the gene, however, will ultimately get
sick with amyloidosis.

The exact cause of dialysis-related beta2-microglobulin amyloidosis is not fully

understood. A normally-functioning kidney can clear out beta 2-microglobulin. In some
individuals on long-term dialysis or some individuals on continuous ambulatory
peritoneal dialysis (CAPD), the kidneys’ inability to function properly leads to the
abnormal retention and accumulation of the beta2-microglobulin protein. Some
individuals with near end-stage renal failure have also developed this form of
amyloidosis. Although this retention and accumulation is believed to be the main
underlying factor, additional factors are required for the disorder to develop, which is why
only a percentage of individuals on dialysis develop dialysis-related beta2-microglobuin
amyloidosis.

Affected Populations

It is estimated that there are approximately 4000 new cases of AL amyloidosis annually
in the United States, though actual incidence may be somewhat higher as a result of
under-diagnosis. While the incidence is thought to be equal in males and females, about
60% of patients referred to amyloid centers are male. AL amyloidosis has been reported
in individuals as young as 20 years of age but is typically diagnosed at about age 50-65.

Individuals at risk for AA amyloidosis include those with chronic inflammatory diseases
such as rheumatic arthritis, psoriatic arthritis, chronic juvenile arthritis, ankylosing
spondylitis in children, inflammatory bowel disease, and familial Mediterranean fever.
People with chronic infectious diseases such as tuberculosis, leprosy, bronchiectasis,
chronic osteomyelitis, and chronic pyelonephritis are also at risk. Secondary amyloidosis
(AA) occurs in less than 5% of individuals with these conditions.

Familial amyloidosis caused by a transthyretin mutation occurs in approximately 1 in

100,000 Caucasians in the U.S, and more commonly in African Americans
(approximately 4% in that population). This condition is prevalent in Portugal, Sweden,
Japan, Ireland, Spain, France, Finland, Germany and Greece. Symptoms usually begin
between 40 and 65 years of age.

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Though both familial and AA amyloidosis are probably less common than AL
amyloidosis, ATTRwt amyloidosis is probably more common, but considerably
underdiagnosed.

Related Disorders

The following disorders may be associated with amyloidosis. Amyloidosis may appear in
conjunction with or as a result of the following disorders:

Multiple myeloma, Hodgkin lymphoma, lymphoma, medullary carcinoma of the thyroid,

Whipple disease, Crohn disease, osteomyelitis, rheumatoid arthritis, ankylosing
spondylitis, Reiter syndrome, psoriatic arthritis, tuberculosis, leprosy, familial
Mediterranean fever, early onset Alzheimer disease and Waldenstrom
macroglobulinemia (For more information on these disorders, search for them in the
Rare Disease Database.)

Diagnosis

Particularly in the case of AL amyloidosis, early diagnosis is the key to survival and post
treatment regaining of quality of life. The diagnosis of amyloidosis is suspected following
a detailed patient history and clinical evaluation but requires aspiration of abdominal fat
pad and/or biopsy of the involved organ. If the disease is suspected on clinical grounds,
a biopsy of the involved organ will give the highest yield. The biopsy material is
examined microscopically and is stained with a dye called Congo red that will produce a
green color when looked at in a polarizing microscope if amyloid is present. When
amyloidosis is diagnosed on a tissue biopsy it is essential that the affected individual be
further evaluated to determine what organs are affected.

Once a tissue biopsy of amyloidosis has been established, it is crucial to determine the
type of amyloidosis. In AL amyloidosis, manifestations of a plasma cell dyscrasia will be
found in 98% of the time. In 2% of cases, a B-cell lymphoma is identified as the cause of
AL amyloidosis. The specific tests that are used to make a diagnosis of the plasma cell
dyscrasia or B-cell clone are immunofixation and protein electrophoresis of the blood
and urine, bone marrow biopsy with immunochemical staining of plasma cells for kappa
and lambda light chains and a serum free light chain assay. The diagnosis of TTR
hereditary amyloidosis can be confirmed by performing molecular genetic testing for
mutations in the TTR gene on a blood sample. In the absence of mutations of
transthyretin, very rare forms of familial amyloidosis may be present.

If the patient is an elderly man with clinically isolated cardiac involvement, the most likely
diagnosis is ATTRwt amyloidosis a condition in which wild-type (normal) transthyretin is
deposited in the heart.

Specific immunostaining (for example, immunogold electron microscopy) of

appropriately preserved tissue is available at specialized centers and offers a high
specificity for determining the accurate type of amyloid. In difficult diagnostic cases,
mass spectrometry is able to determine precisely the molecular structure of the amyloid

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deposits– this technique is being used more and more frequently. A technique called
radiolabeled serum amyloid P (SAP) scanning is available in a few centers in Europe
that specialize in amyloidosis. This test is used to monitor and evaluate the extent of
accumulation of amyloid deposits.

In individuals on long-term dialysis or with end stage renal failure, lab tests may be
performed that can analyze blood or urine samples to detect increased levels B2M
protein.

Standard Therapies

Treatment

The type of treatment available is driven by the type of amyloidosis and the clinical state
of the patient. In AL amyloidosis, the cause is the abnormal plasma cells and as such,
chemotherapy aimed at eradicating those cells forms the cornerstone of treatment.
Various regimens have been studied but the ones with the most historical evidence are
Evomela (melphalan) and Dextenza (dexamethasone) given orally or high-dose
melphalan given intravenously with autologous stem cell transplantation. Both are
equally effective but the treatments and side effects are different. High dose melphalan
with stem cell transplantation is an involved treatment that often involves a 2-3 week
hospital stay and a few months of additional recovery time. The use of oral melphalan on
a monthly basis is less toxic, but is associated with a higher risk of treatment-related
leukemia. Newer agents active in multiple myeloma (another disease of abnormal
plasma cells), such as Velcade (bortezomib) or Revlimid (lenalidomide), are also very
effective in AL amyloidosis and have been shown to provide a benefit in patients with
relapsed disease. Often times, these drugs are incorporated into upfront treatment.
Currently, most patients not getting high dose melphalan with stem cell support
transplantation are having getting novel therapies upfront. The combination of
bortezomib, Cytoxan (cyclophosphamide) and dexamethasone is associated with good
tolerability and rapid responses. The specific treatment for any individual has to be
personalized to their unique situation.

The two most important determinants of long-term survival with AL are the presence and
extent of cardiac involvement and hematologic response to therapy.

Supportive therapy (treatment of congestive heart failure, attention to nutrition, treatment

of autonomic neuropathy etc.) is a very important concomitant measure. Given the
complexity of the disease, it is recommended that treatment be performed in a center
with experience in amyloidosis, or at least that the patient should have an initial
evaluation at such a center, with continued communication during treatment in the local
community.

Hereditary TTR amyloidosis is treated, if possible, by removal of the source of the

abnormal TTR production. Since the dominant source is the liver, liver transplantation is
performed in carefully selected patients whose disease is not too far advanced. Onpattro
(patisiran) and Tegsedi (inoteresen) are TTR gene silencers and have been approved by

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the Food and Drug Administration (FDA) for treatment of ATTRm amyloidosis with
peripheral neuropathy. In 2019, the FDA approved Vyndaqel (tafamidis meglumine) to
treat the cardiomyopathy (heart disease) caused by ATTR (ATTR-CM).

Genetic counseling is recommended for individuals with hereditary amyloidosis and their
family members.

In ATTRwt amyloidosis, therapy is supportive, but both for this disease and for ATTR,
pharmacologic therapies aimed at stabilizing the transthyretin molecule and thus
preventing amyloid formation are being actively investigated.

The mainstay of AA amyloidosis treatment is therapy of the underlying disease. Renal

transplantation has been performed successfully for renal disease due to AA
amyloidosis.

Eprodisate is a small molecule that inhibits the formation of amyloid fibrils, and which
seems to have a modest clinical effect in patients with AA amyloidosis.

In 2015, the FDA authorized the use of a medical device called Lixelle Beta 2-
microglobulin apheresis column to treat dialysis-related beta2-microglobulin amyloidosis.
The device works by removing the beta 2m protein from the blood.

Investigational Therapies

Information on current clinical trials is posted on the Internet at www.clinicaltrials.gov. All

studies receiving U.S. government funding, and some supported by private industry, are
posted on this government web site.

For information about clinical trials being conducted at the NIH Clinical Center in
Bethesda, MD, contact the NIH Patient Recruitment Office:

Toll-free: (800) 411-1222

TTY: (866) 411-1010

Email: [email protected]

Some current clinical trials also are posted on the following page on the NORD website:

https://rarediseases.org/for-patients-and-families/information-resources/info-clinical-
trials-and-research-studies/

For information about clinical trials sponsored by private sources, contact:

www.centerwatch.com

For information about clinical trials conducted in Europe, contact:

https://www.clinicaltrialsregister.eu/

Amyloidosis Treatment Centers

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Medical centers that provide diagnosis and treatment for amyloidosis and conduct
research and clinical trials can be located here:

https://www.amyloidosissupport.org/

International Amyloid Centers

Italian center for the Study and Cure of Systemic Amyloidosis (Pavia, Italy)

www.amiloidosi.it

National Amyloidosis Center, London, UK.

https://www.ucl.ac.uk/amyloidosis/national-amyloidosis-centre

NORD Member Organizations

Amyloidosis Research Consortium, Inc.

320 Nevada Street
Newtonville, MA 02460 USA
Phone: (617) 467-5170
Email: [email protected]
Website: https://arci.org/
Amyloidosis Support Groups, Inc.
232 Orchard Drive
Wood Dale, IL 60191
Phone: (866) 404-7539
Toll-free: (866) 404-7539
Email: [email protected]
Website: http://www.amyloidosissupport.org

Other Organizations

Amyloidosis Foundation
7151 N. Main Street
Suite 2
Clarkston, MI 48346 USA
Phone: (248) 922-9610
Toll-free: (877) 269-5643
Email: [email protected]
Website: http://www.amyloidosis.org
Genetic and Rare Diseases (GARD) Information Center
PO Box 8126
Gaithersburg, MD 20898-8126
Phone: (301) 251-4925
Toll-free: (888) 205-2311
Website: http://rarediseases.info.nih.gov/GARD/

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 Mackenzie’s Mission
11602 Meadow Ridge Lane VA 22066
Great Falls, VA 22066
Phone: (571) 442-1262
Email: [email protected]
Website: https://mm713.org/

References

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Park KI, Ourednik J, Ourednik V, et al. Global gene and cell replacement strategies via
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Skinner M, Sanchorawala V, Seldin DC, Dember LM, Falk RH, Berk JL, Anderson JJ,
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Cunnane G. Amyloid precursors and amyloidosis in inflammatory arthritis. Curr Opin
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INTERNET

AMYLOIDOSIS AWARENESS: For patients and their support network, including

physicians, nurses and medical students. Amyloidosis Support Groups. October 2013.
http://www.amyloidosissupport.com/AmyloidAware_Booklet.pdf Accessed October 24,
2018.

Basu A, Bogdan CA, Matute R. Dialysis-Related Beta-2m Amyloidosis. Medscape.

Updated: Feb 03, 2017. Available at: http://emedicine.medscape.com/article/246542-
overview Accessed October 24, 2018.

What is Amyloidosis? Boston University Amyloid Treatment & Research Program.

http://www.bu.edu/amyloid/about/what/ Accessed October 24, 2018.

Amyloidosis. Mayo Foundation for Medical Education and Research. July 07, 2017.
http://www.mayoclinic.com/health/amyloidosis/DS00431 Accessed October 24, 2018.

Years Published

1984, 1985, 1986, 1987, 1988, 1989, 1990, 1991, 1992, 1995, 1996, 1997, 1998, 1999,
2001, 2002, 2003, 2006, 2007, 2010, 2013, 2016, 2018
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