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June 11, 2003
Renal amyloidosis worsens the Familial Mediterranean
Fever prognosis.
Study highlights need for specific therapy for AA amyloidosis.
- Neurochem, Inc. (TSX: NRM) - World Congress of Nephrology, Berlin, Germany - Data
presented today show that the occurrence of renal amyloidosis (RA) worsens the Familial
Mediterranean Fever (FMF) prognosis, according to Dr Hedi Ben Maïz from the
Department of Nephrology and Internal Medicine, Charles Nicolle Hospital, Tunisia.
The study examined 37 patients (36 Arabic and 1 Jewish) with FMF and proven RA with a
mean age of 25 years, 1 year from the time of kidney biopsy. Nephrotic syndrome was
observed in all 37 patients, high blood pressure in 6 patients and renal failure in
20 patients.1
FMF, one of a number of chronic inflammatory diseases, is a recessive disorder
characterised by acute attacks of fever and severe inflammation of tissues. The disease
affects certain groups, mainly Sepharadic, Jews, Armenians, Turks and Arabs. RA is the
most severe complication in 80% of cases, leading inevitably to chronic renal failure and
to death.2,6
Mortality and morbidity were compared amongst patients treated with colchicines. The study
reveals that while colchicines therapy seems to give some good results on confirmed renal
amyloidosis in a small proportion of patients, amyloid deposits are associated with an
overall poor prognosis.
"These data suggest that renal amyloidosis may increase mortality for patients
whose health is already compromised by Familial Mediterranean Fever", says Dr
Ben Maïz. "This study highlights vital concerns about the health impact of
renal amyloidosis. These data strengthen our need for a specific therapy to treat renal
amyloidosis."
Renal amyloidosis is a chronic and fatal disease marked by the deposit of amyloid fibrils
in the kidney. When caused by an inflammatory disease such as FMF the deposited fibrillar
material is of the Amyloid A (AA) type and the condition in this instance is known as AA
amyloidosis.
AA amyloidosis can be caused by a number of chronic inflammatory conditions including
rheumatoid arthritis, Crohn's disease and Familial Mediterranean Fever. It is part of a
large family of diseases, called amyloidosis, which are all linked by abnormal Amyloid
protein deposits including the amyloid plaques and lesions of Alzheimer's disease.
Abnormal amyloid deposits linked to AA amyloidosis mainly accumulate in the liver, spleen,
kidney and GI tract, leading to organ dysfunction and death in 42% of patients within 4
years of diagnosis.2
There is currently no specific treatment, or treatment protocols for AA amyloidosis.
Clinical management is limited to control of the underlying inflammatory disease, or to
the management of organ dysfunction. The only therapeutic option in many cases is dialysis
or renal transplantation for patients with end-stage renal disease.4,7
"Dr Ben Maïz's study highlights the current unmet need in a specific treatment
for AA amyloidosis," says Denis Garceau, Ph.D., Vice President Drug Development of
Canadian firm Neurochem, specialists in the development of therapeutics for neurological
disorders and many diseases related to amyloid. "Physicians need to consider the
potential presence of AA amyloidosis, especially in at-risk patients with chronic
inflammatory conditions, including FMF. A strong and international effort will soon work
towards developing both therapeutic and diagnostic guidelines for AA
Amyloidosis."
Notes to editors:
Potential future hope
Neurochem Inc. is developing a class of unique small organic molecules which have been
shown to control amyloid deposits associated with diseases such as Alzheimer's
disease, haemorrhagic stroke due to cerebral amyloid angiopathy, type II diabetes and AA
amyloidosis. Neurochem researchers have designed, synthesised and screened thousands of
compounds. Currently three programs have advanced to clinical trials: Fibrillex™, in
a pivotal phase II/III clinical trial, and Cerebril™ and Alzhemed™, both in
phase II clinical trials.
For an amyloid fibril to form, complex carbohydrates known as glycosaminoglycans (GAGs)
attach to amyloid precursor proteins. Neurochem's developmental compounds mimic the action
of natural GAGs by binding to the amyloid proteins, and hence prevent the formation, build
up and associated toxicity of amyloid deposits.
Fibrillex™ appears to be a potent, orally-active anti-AA amyloid agent, with a good
safety and tolerability profile. Fibrillex™ was granted "Orphan Drug
Designation" by the US Food and Drug Administration (FDA) in 1999 and
"Orphan Medicinal Product" designation in Europe in October 2001, normally
associated with seven and ten years of market exclusivity respectively.
Fibrillex™ is currently undergoing a pivotal phase II/III clinical trial.
All of the statements contained in this news release, other than statements of fact which
are independently verifiable at the date hereof, are forward-looking statements. Such
statements, based as they are on the current expectations of management, inherently involve
numerous risks and uncertainties, known and unknown. Some examples of known risks are: the
impact of general economic conditions, general conditions in the pharmaceutical industry, changes
in the regulatory environment in the jurisdictions in which Neurochem does business, stock
market volatility, fluctuations in costs, and changes to the competitive environment due to
consolidation or otherwise. Consequently, actual future results may differ materially from
the anticipated results expressed in the forward-looking statements.
1- Ben Maïz H, et al. Renal amyloidosis in patients
with Mediterranean Fever. World Congress of Nephrology presentation (W247), Wednesday 11
June, 10:00am CET
2- Cunnane G, Whitehead A. Amyloid precursors and
amyloidosis in rheumatoid arthritis. Baillières Best Pract Res Clic Rheumatol
1999;13:615-28
3- Falk R, et al. The systemic amyloidosis. N Engl J Med
1997;337:898-909
4- Mayo reference services. Communiqué
September 2002:7
5- Garceau D, et al. Safety, tolerability and
pharmacokinetic profile of Fibrillex™ (anti-AA amyloid agent) in healthy and renal
impaired subjects. Proceedings from the IXth International Symposium on Amyloidosis 2001,
Budapest, Hungary
6- Joss N., et al. Presentation, survival and prognostic
markers in AA amyloidosis. QJM 2000;93:535-42
7- Ben Maïz H, et al. Renal replacement therapy for
end-stage renal disease related to AA amyloidosis. World Congress of Nephrology
presentation (M655), Monday 9 June, 10:00am CET
For further Information, please contact:
Dr. Lise Hébert
Vice President, Corporate Communications
lhebert@neurochem.com
275 Armand-Frappier
Laval (Quebec)
H7V 4A7
Tel: (450) 680-4500
Fax: (450) 680-4501
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