Center of expertise:

Center of expertise

Mission

The early recognition and treatment of amyloidosis in order to minimise the effects of decline in health. Our focus is therefore on the improvement of diagnosis and treatment of patients with amyloidosis. In addition, we offer information to patients, physicians and other individuals involved.


Who we are

The Groningen Amyloidosis Center of Expertise is a collaboration of various disciplines at the University Medical Center Groningen, engaged in diagnosis and treatment of systemic and localised amyloidosis. The department of Internal Medicine has a coordinating role.

The team consists of:

Medical specialists Internal Medicine

Medical specialists Hematology

Medical specialists Cardiology

Medical specialist Gastrointestinal and Liver Diseases

Medical specialists Nephrology

Medical specialist Throat, Nose and Ear Surgery

Pathology Department

Medical specialists Nuclear Medicine

Medical specialists Ophthalmology

Medical specialists Neurology/Clinical Neurophysiology

Laboratory Medicine Department, Medical Immunology

Clinical Genetics

Healthcare administration

Researchers


Our history in the UMCG

Our center originated from an interest in amyloidosis on the part of the Groningen Professor of Internal Medicine, Enno Mandema, during the mid-1960s.
With his colleagues, the internist Jan Scholten and the biochemist Luuk Ruinen, he began research into this disease. This resulted in a collaboration with the American researcher and professor, Alan Cohen. Together they organized the first International Symposium on Amyloidosis in Groningen from 24-28 September 1967 (1). This symposium met the need for collaborative research into the field and became a tradition. Later symposiums were organized all over the world. In May 2012 the symposium returned to Groningen (2). The 17th symposium will be held in Barcelona in the summer of 2020.

In the 1980s the research was taken over by the Professor of Rheumatology Martin van Rijswijk (3), along with the biochemist Jan Marrink, Professor of Biochemistry Piet Limburg and the internist Sven Janssen (4).
To mark the occasion of Mandema’s retirement as Professor of Internal Medicine, an international course on amyloidosis was once again held in Groningen on the 10-11 October 1986 (5).

From the late 1980s until July 2018 further care for patients with amyloidosis and research in this field was coordinated by the Rheumatologist Bouke Hazenberg, with the support of research technician Johan Bijzet. During this period, diagnostics were improved, making it possible to distinguish different types of systemic amyloidosis from the early 1980s. These diagnostics have since been further refined, increasing their reliability. In addition, diagnosis has become easier and now places less burden on the patient. Hazenberg and Bijzet further developed diagnostics based on fat aspiration biopsies to a level at which the amyloid in fat tissue can be accurately typed and quantified (6, 7).

Since it became possible to distinguish the different types of amyloidosis, the focus of the research shifted to determining the source of the amyloid. The different precursor proteins – the proteins that are the building blocks for the amyloid – were discovered and techniques were developed to establish the presence of, and measure levels of these proteins in the blood. The implementation of these techniques enabled effective follow-up during the course of the disease. Progress in the field of genetics enabled DNA-testing within families, making it possible to establish the presence or absence of specific mutations.
Through the deeper understanding of the background of the different types of amyloidosis in the 1990s research could be directed to the most important aspect for the patient, the treatment.

Since the different precursor proteins had been discovered, treatments were able to be directed at suppressing the production of these proteins. Chemotherapy, sometimes followed by stem cell transplantation, proved to be effective in the treatment of AL amyloidosis. In recent decades various drugs have become available which have appeared useful in the treatment of these patients and improved survival. An interventional trial with the drug daratumumab is currently being conducted, which the UMCG is proud to be part of. This drug has been developed to specifically target the malignant cells that produce the protein that then deposits as amyloid.

In the 1990s liver transplantation was introduced as treatment of hereditary ATTR amyloidosis. In 2013 drugs to inhibit progression of the disease made their appearance. The Center of Expertise also participated in the development of treatments that make use of the principle of “gene silencing”. Since 1 January 2019 the drug patisiran which works via this principle, has been available in the Netherlands.

With AA amyloidosis, effective treatment of the underlying inflammation remains the foundation of the treatment. The arrival of drugs called biologicals, that inhibit targeted inflammatory processes, has led to AA amyloidosis occurring much less frequently.

When treating amyloidosis, it is also very important to have good measuring instruments to record the effect of the treatment. In the early 1990s, Pepys and Hawkins developed the SAP scan for this purpose in London. Hazenberg has also introduced the SAP scan in Groningen in collaboration with Pepys and Hawkins (6). Although the SAP scan is not equally as informative for every patient, and certainly not for every type of amyloidosis, it appears to be of great value in some cases to visualize the course of the disease. In addition, in many cases it provides insight into possible involvement of the liver, spleen, kidneys, adrenal glands, bone marrow and joints. Unfortunately, this scan does not help to identify involvement of the heart, gastrointestinal tract, thyroid gland, tongue or nerves.

In contrast, bone scans appear to be very suitable for the detection of amyloid deposits in the walls of the heart in ATTR amyloidosis (9).

Over the past decade, care pathways have been formalized, multidisciplinary discussions have been set up and the team has been expanded with relevant medical specialists. There is close cooperation with Stichting Amyloidose Nederland (SAN) established in 2013. This foundation, set up by patients, represents the interests of patients with amyloidosis on all fronts.

In 2015, Groningen received recognition from the Dutch Federation of University Medical Centers as a national expertise center for amyloidosis and since 2017, the center has been part of the European reference network RITA (Rare Immunodeficiency, Autoinflammatory and Autoimmune Disease Network).

In recent years, Hans Nienhuis, internist-immunologist, has been trained by Hazenberg in the field of amyloidosis. In July 2018, after more than 33 years of dedication to patients with amyloidosis, Hazenberg transferred his task as coordinator of the Expertise Center to Nienhuis. The Expertise Center was then transferred to the Internal Medicine Department, where Nienhuis and two other internists now focus on the care of patients with amyloidosis.

As amyloidosis treatment staff at the UMCG, we hope that with the arrival of effective but above all safe means, amyloid accumulation in every patient can be brought to a halt or even completely cleared up. We hope that the focus can then be more on the quality of life of patients with amyloidosis.

The Center of Expertise will continue to work closely with SAN to best serve the interests of patients.

Literature

  1. Mandema E, Ruinen L, Scholten JH en Cohen AS. Amyloidosis. Proceedings of the First Intenational Symposium on Amyloidosis, Universiteit Groningen, 1967.
  2. Hazenberg BPC en Bijzet J. Proceedings of the XIIIth International Symposium on Amyloidosis “From Misfolded Proteins to Well-designed Treatment”, Universiteit Groningen, 2013.
  3. van Rijswijk MH. Amyloidosis. Dissertation, Universiteit Groningen, 1981.
  4. Janssen S. Clinical and Diagnostic Features of Amyloidosis. Dissertation, Universiteit Groningen, 1985.
  5. Marrink J en van Rijswijk MH. Amyloidosis. International Course, Universiteit Groningen, 1986.
  6. Hazenberg BPC. Diagnostic Studies in Amyloidosis. Dissertation, Universiteit Groningen, 2007.
  7. van Gameren II. Diagnostic and Therapeutic Modalities in Systemic Amyloidosis. Dissertation, Universiteit Groningen, 2009.
  8. Rutten KHG, Raymakers RAP, Hazenberg BPC, Nienhuis HLA, Vellenga E & Minnema MC. Haematological response and overall survival in two consecutive Dutch patient cohorts with AL amyloidosis diagnosed between 2008 and 2016. Amyloid 2018; 25(4):227-233.
  9. Glaudemans AWJM. Nuclear Medicine Strategies to Image Infectious and Inflammatory Diseases. Dissertation, Universiteit Groningen, 2014.

Historical developments in a nutshell

General
1639 – First description of a “sago spleen” by Nicholaus Fontanus (Fonteyn)
1789 – Description of a lardaceous liver by Antoine Portal. Later he also describes an enlarged liver in an 8-year-old boy with tuberculosis
1842 – Gray “lardaceous-gelatinous” material in the liver of patients with tuberculosis, syphilis and mercury poisoning described by Karl Rokitansky
1856 – Probably the first description of a patient with “primary” amyloidosis by Samuel Wilks. In 1865 he described five similar cases
1872 – W. Adams and T.S. Dowse describe amyloid in patients with multiple myeloma
1932 – Benno Ostertag describes the first family with hereditary amyloidosis (of the kidneys)
1945 – Sheppard Siegal describes patients with familial benign paroxysmal peritonitis, currently known as familial Mediterranean fever (FMF). In this disease, amyloidosis is a frequent (in about 40% of cases) late complication.
1952 – Corine Andrade describes 74 patients, members of many families all originating from the same area around Povoa de Varzim, a small coastal village in Portugal – all suffering from a familial amyloidotic polyneuropathy (FAP)
1956 – John Rukavina describes familial amyloid polyneuropathy in Indiana
1967 – First International Symposium on Amyloid and Amyloidosis, held in Groningen, organized by Enno Mandema, Luuk Ruinen, Jan Scholten and Alan Cohen

1967 – Jan Scholten describes a Dutch family with hereditary amyloidotic polyneuropathy in The Netherlands
1968 – In Finland, Jouko Meretoja describes a hereditary form of systemic amyloidosis characterized by cornea lattice dystrophy, cutis laxa, and a cranial neuropathy
1968 – In Japan, Shukuro Araki describes familial amyloidotic polyneuropathy
1969 – Maurice van Allen describes a family with renal amyloidosis in Iowa
1970 – In Sweden Rune Andersson describes familial amyloidotic polyneuropathy
1975 – David Warren describes a high frequency of carpal tunnel syndrome (CTS) in patients who are ondergoing long-term dialysis therapy. A while later, in fact only in 1984, it becomes clear that deposition of amyloid is the cause of the CTS as well as of other joint problems
1975 – John Wright and Evan Calkins describe a series of 100 autopsies of people of 60 years and older and they find amyloid in the heart in 10 of them, with high levels of amyloid in two of them
1983 – Gibbons Cornwell again draws attention to the high frequency of amyloid in the heart (25%, and in most cases also showing amyloid in the lung and rectum) in a series of 85 successive autopsies of people of 80 years and older
1986 – The first Iinternational course on amyloidosis takes place in Groningen to mark the retirement of Enno Mandema
1993 – Alan Cohen becomes editor-in-chief of a new medical journal called AMYLOID, The International Journal of Protein Folding Disorders
2002 – Official founding of the International Society of Amyloidosis (ISA) by Bob Kyle, the first president of the ISA. A collaborative network of amyloidologists, who organized international symposiums and took care of the nomenclature, had already existed informally since 1967
2010 – Per Westermark succeeds Alan Cohen as editor-in-chief of AMYLOID
2012 – Bouke Hazenberg and Johan Bijzet organize the XIIIth ISA-symposium, returning to Groningen, 45 years after the first symposium

Analysis of the structure of amyloid
1854 – The term “amyloid” is coined by Rudolph Virchow to describe material deposited in tissue, based upon the color reaction with iodine and sulphuric acid (from brown to blue) similar to the colour reaction of starch (amylum)
1859 – Karl Friedreich and August Kekulé show that amyloid is composed of proteins rather than carbohydrates
1875 – Methylviolet staining proves more useful for the detection of amyloid than the iodine sulphuric acid test. This finding was described independently from each other by André-Victor Cornil (Paris), Richard Heschl (Vienna), and Rudolph Jürgens (Berlin)
1907 – Alois Alzheimer describes fibrillar argyrophil deposits in cortical neurons
1922 – Hermann Bennhold introduces the Congo red stain for amyloid. In 1927 Paul Divry describes the characteristic apple-green birefringence (e.g. in cortical neurons in Alzheimers’s disease)
1959 – Alan Cohen and Evan Calkins describe the fibrillar structure of amyloid when studied under the electron microscope
1961 – Joseph Ehrlich detects localised deposits of amyloid in the islets of Langerhans in the pancreas of patients with type 2 diabetes mellitus
1966 – Howard Bladen and George Glenner describe the pentagonal protein serum amyloïd P component
1968 – David Eanes and George Glenner show that the beta-pleated sheet is the basic structure of amyloid fibrils
1968 – Mordechai Pras introduces a method to extract proteins from fibrils with water. This method turned out to be a big step forward in the chemical characterization of amyloid proteins, as can be seen in the following years
1971 – George Glenner shows that some amyloid fibrils are derived from the variable portion of a kappa or lambda light chain
1972 – Earl Benditt describes AA amyloid as the newly characterized, distinctive protein in “secondary” amyloidosis
1973 – Edward Franklin and Mark Levin show the presence in blood of serum amyloid A protein (SAA), which later turns out to be an acute phase protein
1978 – Pedro Costa describes prealbumin (transthyretin) as the protein characteristic of amyloid in familial amyloidotic polyneuropathy
1980 – Knut Sletten describes prealbumin (transthyretin) as the protein characteristic of amyloid in a patient with senile systemic amyloidosis
1983 – Alan Cohen describes cystatin-C as the protein characteristic of amyloid in Icelandic familial cerebral amyloid angiopathy
1983 – Stanley Prusiner and George Glenner show the presence of amyloid fibrils in scrapie (prion disease)
1984 – Satoru Tawara and Shukuro Araki describe a point mutation in the transthyretin gene, resulting in a substitution of methionine instead of valine at position 30, in patients with familial amyloidotic polyneuropathy
1985 – Fumitake Gejyo describes β-2-microglobulin as the protein characteristic of amyloid in dialysis-related amyloid arthropathy
1988 – William Nichols and Merrill Benson describe apolipoprotein AI as the protein characteristic of amyloid in a familial form of systemic amyloidotic polyneuropathy in Iowa
1990 – Both Peter Maury and Blas Frangione describe gelsolin as the protein characteristic of amyloid in the Finnish form of hereditary amyloid polyneuropathy
1993 – Merrill Benson describes fibrinogen Aα chain as the protein characteristic of amyloid in a familial form of renal (as prominent manifestation of systemic) amyloidosis
1993 – Mark Pepys describes lysozyme as the protein characteristic of amyloid in a familial form of renal (as prominent manifestation of systemic) amyloidosis
1999 – Bouke Hazenberg and Johan Bijzet describe an ELISA method that can quantify the amount of AA amyloid in the fat tissue of patients with AA amyloidosis for both diagnosis and follow-up. Later, this ELISA method is extended to ATTR and AL (both kappa and lambda)
1999 – Batia Kaplan and Alan Solomon describe a proteomics method of micro-extraction and quantification of amyloid in formalin-fixed tissue biopsies followed by techniques such as mass spectrometry, to chemically analyze the amyloid protein involved
2001 – Merrill Benson describes apolipoprotein AII as the protein characteristic of amyloid in a familial form of renal (as prominent manifestation of systemic) amyloidosis
2003 – Roshini Abraham and Morie Gertz introduce a quantitative measurement of both kappa and lambda free light chains in the blood of patients with AL amyloidosis, resulting in a huge increase of detection of the involved light chain
2003 – Giovanni Palladini and Giampaolo Merlini introduce NT-proBNP as marker of the severity of cardiomyopathy as well as risk factor in patients with systemic AL amyloidosis
2004 – Angela Dispenzieri introduces troponin as a second marker of cardiomyopathy in addition to NT-proBNP and introduces a staging system for AL amyloidosis that is based upon these two cardiac biomarkers
2009 – Charles Murphy and Alan Solomon describe serum amyloid A4 protein (SAA4) as the protein characteristic of amyloid in a familial form of renal amyloidosis
2009 – Julie Vrana and Ahmet Dogan describe laser microdissection of amyloid in formalin-fixed clinical biopsies followed by mass spectrometry-based proteomics analysis, in order to characterize the involved amyloid protein
2010 – Charles Murphy and Alan Solomon describe leukocyte chemotactic factor 2 (LECT2) as the protein characteristic of amyloid in a form of renal systemic amyloidosis
2012 – Sophie Valleix and Vittorio Bellotti describe a hereditary variant of β-2-microglobulin as the protein characteristic of amyloid in a familial form of systemic amyloidosis characterized by autonomic neuropathy
2016 – Sadichhya Lohani and Sami Zarouk describe a hereditary variant of apolipoprotein CII as the protein characteristic of amyloid in a hereditary form of renal systemic amyloidosis
2016 – Sophie Valleix and Vittorio Bellotti describe a hereditary variant of apolipoprotein CIII as the protein characteristic of amyloid in a hereditary form of renal systemic amyloidosis
2019 – Matthias Schmidt and Marcus Fändrich use cryo-electron microscopy for visualizing AL and AA amyloid fibrils from human tissue with a resolution of 2.7 Angstrom

Evaluation and treatment
1986 – Dan Zemer shows that treatment of familial Mediterranean fever (FMF) with colchicine is not only effective in significantly reducing episodes of the disease, but also prevents AA amyloidosis as a late complication
1988 – Philip Hawkins and Mark Pepys introduce 123I-SAP scintigraphy as a clinical method to visualise the presence of amyloid in organs of patients with systemic amyloidosis
1991 – Gösta Holmgren introduces liver transplantation as potential treatment for patients with familial ATTR amyloidosis
1996 – Martha Skinner shows that the combination of prednisolone, melphalan, and colchicine has a beneficial effect on the survival of patients with AL amyloidosis compared to only colchicine
1996 – Ray Comenzo shows the promising first results of high dose melphalan followed by autologous stem cell support in patients with AL amyloidosis
1997 – Bob Kyle confirms Martha Skinner’s observation that the combination of prednisolone and melphalan has a beneficial effect on the survival of patients with AL amyloidosis, and finds that the addition of colchicine has no additional benefit in this group of patients
2001 – Julian Gillmore shows that effective reduction of the serum concentration of serum amyloid A protein (SAA) has a favourable effect on the disease course and survival of AA amyloidosis
2003 – David Seldin introduces thalidomide, the first immunomodulating drug (IMiD) against AL amyloidosis
2004 – Martha Skinner and Angela Dispenzieri both confirm the favorable effect of high dose melphalan with stem cell support in larger groups of patients with AL amyloidosis
2004 – Philip Hawkins en Helen Lachmann describe a very favorable effect of treatment with anti-IL1 on cryopyrin-associated autoinflammatory diseases
2005 – On behalf of a number of clinical research groups, Morie Gertz describes a common set of criteria for organ involvement and criteria for improvement and deterioration during treatment of patients with AL amyloidosis
2007 – Helen Lachmann describes that in patients with AA amyloidosis, reaching a stable target SAA value of < 4 mg/l reduces mortality within ten years to 10% 2007 – In a study of eprodisate (Fibrillex, Kiacta) in AA amyloidosis, Laura Dember shows a favorable effect on the decline of renal function. A second study, however, did not confirm the results of this study2007 – Arnaud Jaccard showed in a large comparative study that the results of autologous stem cell transplantation were not better than chemotherapy consisting of melphalan and dexamethasone 2007 – In a large comparative study, Arnaud Jaccard finds that the results of autologous stem cell transplantation are not more beneficial than chemotherapy consisting of melphalan and dexamethasone 2007 – The first proteasome inhibitor Bortezomib is introduced for treating AL amyloidosis 2009 – Ingrid van Gameren shows that amyloid in fat tissue can regress and even disappear in effectively treated patients with AL amyloidosis, although this is only the case in those patients who obtain a complete hematologic response 2012 – Shaji Kumar introduces a revised prognostic staging system for AL amyloidosis incorporating free light chains and cardiac biomarkers 2012 – Teresa Coelho shows that the tetramer stabilizer tafamidis very likely has a favorable effect, by slowing the gradually progressive polyneuropathy in patients with hereditary ATTR-Met30 amyloidosis 2013 – John Berk shows that the tetramer stabilizer diflunisal has a favorable effect by slowing the gradually progressive polyneuropathy in patients with hereditary ATTR amyloidosis 2016 – Julian Gillmore shows that ATTR amyloid of the heart can be detected using bone scintigraphy without the need of a biopsy, if there are no signs of a clonal plasma cell dyscrasia 2018 – Mathew Maurer shows that the tetramer stabilizer tafamidis has a favorable effect by slowing the gradually progressive cardiac failure in patients with cardiac ATTR amyloidosis 2018 – Merrill Benson shows that the gene-silencer inotersen has a clearly favorable and a strong slowing effect on the progression of polyneuropathy in patients with hereditary ATTR amyloidosis 2018 – David Adams finds that the gene-silencer patisiran has a clearly favorable, strong slowing and possibly even a stabilizing effect on the progression of polyneuropathy, as well as potentially on cardiomyopathy, in patients with hereditary ATTR amyloidosis


News and ongoing research

News

See for News the Newstab on the Homepage.

 

Ongoing research

HELIOS-B study
Heart failure due to amyloidosis (ATTR cardiomyopathy) occurs when the protein transthyretin (which is made in the liver) breaks down into loose pieces. These loose pieces will stick together and amyloid is formed. In ATTR cardiomyopathy, this amyloid gets stuck between the heart muscle cells, making the heart less able to squeeze and relax. The HELIOS-B study is looking at whether a drug that inhibits the production of transthyretin in the liver is beneficial for the heart
Aim: The aim of the study is to determine whether vutrisiran has a favorable effect on the prognosis
Study design: Worldwide approximately 600 participants will be recruited and divided into 2 groups; half will receive placebo (fake medicine) throughout the study and the other half will receive the active substance (vutrisiran). The medication must be given once every 3 months; this is a subcutaneous injection. Using tafamidis at the same time is not allowed in most cases
Participation: People with symptoms of heart failure (including shortness of breath and fluid retention) due to ATTR amyloidosis can participate in this study
Status: The study is open for inclusion of patients in the UMCG and UMCU
For more information, please contact Prof. Dr. P. van der Meer, cardiologist; p.van.der.meer@umcg.nl or Dr. H.L.A. Nienhuis, internist; h.l.a.nienhuis@umcg.nl in UMCGroningen or Dr. M.I.F.J. Oerlemans, cardiologist; m.oerlemans@umcutrecht.nl in UMCUtrecht
No results are yet available from this study

 

NEURIMMUNE study
Heart failure due to amyloidosis (ATTR cardiomyopathy) is caused by the protein transthyretin breaking down into loose pieces. These loose pieces will stick together and amyloid is formed. In ATTR cardiomyopathy, this amyloid sits between the heart muscle cells, making the heart less able to squeeze and relax. This research is looking at whether the body could clean up this amyloid itself with a new drug
Aim: Find out if this new treatment is safe and effective to break down amyloid in the heart
Study design: During one year, 36 participants will be recruited and divided into 2 groups: half will receive placebo (fake medicine) for the first year and the other half will receive the active substance. After six months, both groups will receive the active agent
Participation: Patients with symptoms of heart failure (including shortness of breath and fluid retention) due to ATTR amyloidosis can participate in this study
Status: The study is open for inclusion in 5 centers in Europe until 36 patients have been enrolled. The study is open to the inclusion of patients in the UMCG
For more information, please contact Prof. Dr. P. van der Meer, cardiologist; p.van.der.meer@umcg.nl
There are no results available for this study

 

ATTR-ACT extensionstudy (tafamidis)
Tafamidis is a drug that inhibits the formation of amyloid. A recent study has shown that tafamidis has beneficial effects in patients with ATTR amyloidosis with heart involvement. This international study examines the long-term effects of tafamidis on patients with ATTR amyloidosis with cardiac involvement (cardiomyopathy)
Aim: To obtain data on long-term effects of tafamidis
Study design: Each participant in this study receives treatment with the drug tafamidis. 1,400 subjects in 48 research centers spread over 16 different countries will be included. The duration of the study is a maximum of 60 months. If tafamidis is registered in the Netherlands for the treatment of people with ATTR amyloidosis and heart involvement, the study will be concluded and patients will receive tafamidis through their treating specialist. During the study, patients come to the University Medical Center Groningen at least 11 times (every six months)
Participation:Patients with ATTR amyloidosis (both acquired and hereditary form) with cardiac involvement (cardiomyopathy) are eligible for this study. Exclusion criteria: other types of amyloidosis, pregnancy, liver and/or heart transplantation, use of certain medicines
Status:The study is open for participation. You can ask your doctor for more information. There are no results available for this study

 

THAOS: a global registry for patients with hereditary or wild-type ATTR amyloidosis
Hereditary and wild-type ATTR amyloidosis are rare diseases. This register has been set up to collect data from patients with these diseases from all over the world
Aim:To better understand and characterize the natural course of the condition and to obtain safety and efficacy data from patients taking tafamidis. The data can also be used in formulating new treatment guidelines and recommendations, as well as informing and educating practitioners about the treatment of this condition
Study design: Data from patients obtained during the evaluations at the hospital can be entered anonymously in the register with the patient’s consent. The data can be used to answer research questions
Participation:All patients with hereditary or wild-type ATTR amyloidosis, regardless of their treatment status, can participate in this program. Asymptomatic carriers of TTR gene mutations can also participate in this program. The study is open for participation. You can ask your doctor for more information
Status:Several studies have already been published using data from the THAOS registry

 

HELIOS-A: a study of Vutrisiran (ALN-TTRSC02) in patients with hereditary ATTR amyloidosis and polyneuropathy
The symptoms of hereditary ATTR amyloidosis are caused by the accumulation of misfolded TTR protein. If the production of the TTR protein can be reduced, it can inhibit or even stop disease progression. Vutrisiran (ALN-TTRSC02) is a drug that can reduce the production of the TTR protein
Aim:The main aim of this clinical study is to determine whether the study drug, ALN-TTRSC02, is safe and effective for the treatment of neurological symptoms experienced by patients with hereditary ATTR amyloidosis. The study also evaluates any change in quality of life experienced by the study participants
Study design:During the first 18 months of the study, HELIOS-A participants are randomly assigned to 1 of 2 study treatment groups: 1. ALN-TTRSC02: There is a 75% chance that you will be assigned to this group (approximately 120 people). 2. Patisiran: there is a 25% chance of being assigned to this group (about 40 people). Because HELIOS-A is what is called an open-label study, both the participant and the research team know which treatment group the participant is assigned to. Neither the participant, nor their physician-researcher can choose the treatment group; this is done by a computer. From Month 19, all participants will receive ALN-TTRSC02 for an additional 18 months. After participants receive the last dose of ALN-TTRSC02, participants enter a 1-year follow-up period
Participation:People with neurological symptoms caused by hereditary ATTR amyloidosis can participate in this study. People who are wheelchair-bound, have had a liver transplant, have heart failure symptoms that significantly limit physical activity, who have (had) TTR-lowering treatment or who have had diabetes for more than 5 years cannot participate in the study
Status:The study is closed for participation
Results:There are no results available for this study

 

EMN23: a retrospective study of treatment and results with AL amyloidosis in Europe
AL amyloidosis is a rare disease. Based on clinical studies, we know that certain drugs can be used effectively in selected patients. However, there are a few studies in which the effects of these drugs and their application in the “real world” have been investigated. There are only a few “real world” studies published on AL amyloidosis, so there is little knowledge about this
Aim:Obtaining “real world” data on treatment and results of treatment of patients with systemic AL amyloidosis in Europe. The hope is to improve the treatment of patients with AL amyloidosis
Study design:This study is designed in such a way that the required information is collected retroactively from the medical records of participating patients. Around 5,000 patients with systemic AL amyloidosis will be included in Europe
Participation:This study is open for participation. The condition for participation in the study is that first-line treatment was started between 1 January 2004 and 31 December 2018. You can ask your doctor for more information
Status:There are no results available for this study

 

The European register for auto-inflammatory diseases (EuroFever)
In auto-inflammatory diseases, the immune system is adjusted too strongly, causing inflammation in the body without an infection. Inflammation can cause AA amyloidosis, which is the accumulation of an inflammatory protein in the body. Because auto-inflammatory diseases are rare, relatively little is known about, among other things, the disease symptoms, response to treatment and complications of these diseases, such as AA amyloidosis
Aim: The purpose of this register is to gather information on the clinical manifestations, response to treatment and outcomes of auto-inflammatory diseases
Study design:Data from patients with auto-inflammatory diseases will be collected through a secured website, managed by the Pediatric Rheumatology International Trials Organization, a non-profit research network based in Genoa, Italy. Various research questions can be answered with the data collected
Participation:This study is open for participation. A condition for participation in this register/study is that you have an auto-inflammatory disease
Status: Various research has already been published using data from the EuroFever register

 

ATTRIBUTE-CM: AG10 in ATTR amyloidosis and cardiomyopathy
ATTR amyloidosis arises because the protein transthyretin breaks down into loose pieces (monomers), these monomers stick together and form amyloid. AG10 stabilizes the protein transthyretin and can thus slow down the formation of amyloid. This study will investigate whether further deterioration of cardiac function in cardiac ATTR amyloidosis can be inhibited with AG10 compared to placebo
Background: During the 30 months of the study, 510 participants are divided into two groups: 340 participants receive AG10 and 170 participants receive a placebo
Aim: The main purpose of this clinical trial is to determine whether AG10 is safe and effective for the treatment of cardiac symptoms experienced by persons with ATTR amyloidosis.
It looks at: the change in walking distance in 6 minutes after 12 months, the survival and the number of times that hospitalization has been required after 30 months. The study also evaluates any change in quality of life experienced by the study participants
Status: The study is closed for patient inclusion
Participation: People with symptoms of heart failure due to ATTR amyloidosis can participate in this study. People who have a different type of amyloidosis, severe kidney failure, very severe heart failure, heart failure from other causes, or who are already receiving treatment for ATTR amyloidosis cannot participate in the study
Planning: The study is closed to inclusion (international 510 participants)
Results: No results are available for this study yet

 


Publications

2021
Hill MM, Dasari S, Mollee P, Merlini G, Costello CE, Hazenberg BPC, Grogan M, Dispenzieri A, Gertz MA, Kourelis T, McPhail ED.
The Clinical Impact of Proteomics in Amyloid Typing.
Mayo Clin Proc. 2021 May;96(5):1122-1127. doi: 10.1016/j.mayocp.2020.12.002.

Louwsma J, Brunger AF, Bijzet J, Kroesen BJ, Roeloffzen WWH, Bischof A, Kuhle J, Drost G, Lange F, Kuks JBM, Gans ROB, Hazenberg BPC, Nienhuis HLA.
Neurofilament light chain, a biomarker for polyneuropathy in systemic amyloidosis.
Amyloid. 2021 Mar;28(1):50-55. doi: 10.1080/13506129.2020.1815696.

Adams D, Polydefkis M, González-Duarte A, Wixner J, Kristen AV, Schmidt HH, Berk JL, Losada López IA, Dispenzieri A, Quan D, Conceição IM, Slama MS, Gillmore JD, Kyriakides T, Ajroud-Driss S, Waddington-Cruz M, Mezei MM, Planté-Bordeneuve V, Attarian S, Mauricio E, Brannagan TH 3rd, Ueda M, Aldinc E, Wang JJ, White MT, Vest J, Berber E, Sweetser MT, Coelho T; patisiran Global OLE study group.
Long-term safety and efficacy of patisiran for hereditary transthyretin-mediated amyloidosis with polyneuropathy: 12-month results of an open-label extension study.
Lancet Neurol. 2021 Jan;20(1):49-59. doi: 10.1016/S1474-4422(20)30368-9.
Erratum: Lancet Neurol. 2021 Feb;20(2):e2. doi: 10.1016/S1474-4422(20)30458-0.

2020
Klaassen SHC, Veldhuisen van DJ, Nienhuis HLA, Berg van den MP, Hazenberg BPC, Meer van der P.
Cardiac Transthyretin-derived Amyloidosis: An Emerging Target in Heart Failure with Preserved Ejection Fraction?
Card Fail Rev. 2020 Aug 7;6:e21. doi: 10.15420/cfr.2019.16.

Brunger AF, Nienhuis HLA, van Rheenen RWJ, Korte MR, Bijzet J, Gans ROB, Hazenberg BPC.
Obesity-induced AA amyloidosis: A diagnosis of exclusion.
Int J Clin Rheum 2020 15(2):26-34.

Brunger AF, Nienhuis HLA, Bijzet J, Roeloffzen WWH, Vellenga E, Hazenberg BPC.
A Real-Life Cohort Study of Immunoglobulin Light-Chain (AL) Amyloidosis Patients Ineligible for Autologous Stem Cell Transplantation Due to Severe Cardiac Involvement or Advanced Disease.
Amyloid. 2020 Jun;27(2):119-127. doi: 10.1080/13506129.2020.1714581.

Groothof D, Nienhuis HLA, Bijzet J, Houwerzijl EJ, van den Berg MP, Glaudemans AWJM, Slart RHJA, Hazenberg BPC.
Regression of Bone-Tracer Uptake in Cardiac Transthyretin Amyloidosis.
Mayo Clin Proc 2020 95(2):417-418. doi.org/10.1016/j.mayocp.2019.10.036.

Van der Bie MH, Louter L, Boots JMM, van Daele PLA, Klaassen SHC, Hazenberg BPC.
Erfelijke en verworven transthyretine-gemedieerde amyloïdose. (Dutch)
Ned Tijdschr Geneeskd 2020 164:D4099.

Feenstra JG, Nienhuis HLA, Bijzet J, van der Zwaag PA, van den Berg MP, Hazenberg BPC.
Coexistence of wild type and hereditary ATTR amyloidosis in one family.
Amyloid. 2020 27(1):71-72. doi: 10.1080/13506129.2019.1690444.

Brunger AF, Nienhuis HLA, Bijzet J, Hazenberg BPC.
Causes of AA amyloidosis: a systemic review.
Amyloid. 2020 27(1):1-12. doi.org/10.1080/13506129.2019.1693359.

2019
Slart RHJA, Glaudemans AWJM, Noordzij W, Nienhuis HLA, Hazenberg BPC.
99mTc-aprotinin imaging in cardiac amyloidosis. Make an old tool new again?
J Nucl Cardiol 2019 Oct 10. doi: 10.1007/s12350-019-01917-3.

Connolly MP, Panda S, Patris J, Hazenberg BPC.
Estimating the fiscal impact of rare diseases using a public economic framework: a case study applied to hereditary transthyretin-mediated (hATTR) amyloidosis.
Orphanet J Rare Dis. 2019 Sep 18;14(1):220. doi: 10.1186/s13023-019-1199-x.

Dorbala S, Ando Y, Bokhari S, Dispenzieri A, Falk RH, Ferrari VA, Fontana M, Gheysens O, Gillmore JD, Glaudemans AWJM, Hanna MA, Hazenberg BPC, Kristen AV, Kwong RY, Maurer MS, Merlini G, Miller EJ, Moon JC, Murthy VL, Quarta CC, Rapezzi C, Ruberg FL, Shah SJ, Slart RHJA, Verberne HJ, Bourque JM.
ASNC/AHA/ASE/EANM/HFSA/ISA/SCMR/SNMMI Expert Consensus Recommendations for Multimodality Imaging in Cardiac Amyloidosis: Part 1 of 2-Evidence base and standardized methods of imaging.
J Card Fail. 2019 Aug 6. pii: S1071-9164(19)31397-1. doi: 10.1016/j.cardfail.2019.08.001.

Dorbala S, Ando Y, Bokhari S, Dispenzieri A, Falk RH, Ferrari VA, Fontana M, Gheysens O, Gillmore JD, Glaudemans AWJM, Hanna MA, Hazenberg BPC, Kristen AV, Kwong RY, Maurer MS, Merlini G, Miller EJ, Moon JC, Murthy VL, Quarta CC, Rapezzi C, Ruberg FL, Shah SJ, Slart RHJA, Verberne HJ, Bourque JM.
ASNC/AHA/ASE/EANM/HFSA/ISA/SCMR/SNMMI Expert Consensus Recommendations for Multimodality Imaging in Cardiac Amyloidosis: Part 2 of 2-Diagnostic Criteria and Appropriate Utilization.
J Card Fail. 2019 Aug 29. pii: S1071-9164(19)31398-3. doi: 10.1016/j.cardfail.2019.08.002.

Dorbala S, Ando Y, Bokhari S, Dispenzieri A, Falk RH, Ferrari VA, Fontana M, Gheysens O, Gillmore JD, Glaudemans AWJM, Hanna MA, Hazenberg BPC, Kristen AV, Kwong RY, Maurer MS, Merlini G, Miller EJ, Moon JC, Murthy VL, Quarta CC, Rapezzi C, Ruberg FL, Shah SJ, Slart RHJA, Verberne HJ, Bourque JM.
ASNC/AHA/ASE/EANM/HFSA/ISA/SCMR/SNMMI Expert consensus recommendations for multimodality imaging in cardiac amyloidosis: Part 2 of 2-Diagnostic criteria and appropriate utilization.
J Nucl Cardiol. 2019 Aug 29. doi: 10.1007/s12350-019-01761-5.

Dorbala S, Ando Y, Bokhari S, Dispenzieri A, Falk RH, Ferrari VA, Fontana M, Gheysens O, Gillmore JD, Glaudemans AWJM, Hanna MA, Hazenberg BPC, Kristen AV, Kwong RY, Maurer MS, Merlini G, Miller EJ, Moon JC, Murthy VL, Quarta CC, Rapezzi C, Ruberg FL, Shah SJ, Slart RHJA, Verberne HJ, Bourque JM.
ASNC/AHA/ASE/EANM/HFSA/ISA/SCMR/SNMMI Expert Consensus Recommendations for Multimodality Imaging in Cardiac Amyloidosis: Part 1 of 2-Evidence base and standardized methods of imaging.
J Nucl Cardiol. 2019 Aug 29. doi: 10.1007/s12350-019-01760-6.

Liberta F, Rennegarbe M, Räsler R, Bijzet J, Wiese S, Hazenberg BPC, Fändrich M.
Morphological and primary structural consistency of fibrils from different AA patients (common variant).
Amyloid. 2019 Sep;26(3):164-170. doi: 10.1080/13506129.2019.1628015.

Slart RHJA, Glaudemans AWJM, Noordzij W, Bijzet J, Hazenberg BPC, Nienhuis HLA.
Time for new imaging and therapeutic approaches in cardiac amyloidosis.
Eur J Nucl Med Mol Imaging. 2019 Jul;46(7):1402-1406. doi: 10.1007/s00259-019-04325-4.

Minnema MC, Nasserinejad K, Hazenberg B, Hegenbart U, Vlummens P, Ypma PF, Kröger N, Wu KL, Kersten MJ, Schaafsma MR, Croockewit S, de Waal E, Zweegman S, Tick L, Broijl A, Koene H, Bos G, Sonneveld P, Schönland S.
Bortezomib based induction followed by stem cell transplantation in light chain amyloidosis: results of the multicenter HOVON 104 trial.
Haematologica. 2019 Mar 28. pii: haematol.2018.213900. doi: 10.3324/haematol.2018.213900.

Liberta F, Loerch S, Rennegarbe M, Schierhorn A, Westermark P, Westermark GT, Hazenberg BPC, Grigorieff N, Fändrich M, Schmidt M.
Cryo-EM fibril structures from systemic AA amyloidosis reveal the species complementarity of pathological amyloids.
Nat Commun. 2019 Mar 7;10(1):1104. doi: 10.1038/s41467-019-09033-z.

Saelices L, Nguyen BA, Chung K, Wang Y, Ortega A, Lee JH, Coelho T, Bijzet J, Benson MD, Eisenberg DS.
A pair of peptides inhibits seeding of the hormone transporter transthyretin into amyloid fibrils.
J Biol Chem. 2019 Apr 12;294(15):6130-6141. doi: 10.1074/jbc.RA118.005257.

van den Berg MP, Mulder BA, Klaassen SHC, Maass AH, van Veldhuisen DJ, van der Meer P, Nienhuis HLA, Hazenberg BPC, Rienstra M.
Heart failure with preserved ejection fraction, atrial fibrillation, and the role of senile amyloidosis.
Eur Heart J. 2019 Apr 21;40(16):1287-1293. doi: 10.1093/eurheartj/ehz057.

Slart RHJA, Glaudemans AWJM, Hazenberg BPC, Noordzij W.
Imaging cardiac innervation in amyloidosis.
J Nucl Cardiol. 2019 Feb;26(1):174-187. doi: 10.1007/s12350-017-1059-9.

2018
Rutten KHG, Raymakers RAP, Hazenberg BPC, Nienhuis HLA, Vellenga E, Minnema MC.
Haematological response and overall survival in two consecutive Dutch patient cohorts with AL amyloidosis diagnosed between 2008 and 2016.
Amyloid. 2018 Dec;25(4):227-233. doi: 10.1080/13506129.2018.1536043.

Jonker DL, Hazenberg BPC, Nienhuis HLA, Slart RHJA, Glaudemans AWJM, Noordzij W.
Imaging cardiac innervation in hereditary transthyretin (ATTRm) amyloidosis: A marker for neuropathy or cardiomyopathy in case of heart failure?
J Nucl Cardiol. 2018 Oct 29. doi: 10.1007/s12350-018-01477-y.

Maurer MS, Schwartz JH, Gundapaneni B, Elliott PM, Merlini G, Waddington-Cruz M, Kristen AV, Grogan M, Witteles R, Damy T, Drachman BM, Shah SJ, Hanna M, Judge DP, Barsdorf AI, Huber P, Patterson TA, Riley S, Schumacher J, Stewart M, Sultan MB, Rapezzi C; ATTR-ACT Study Investigators.
Tafamidis Treatment for Patients with Transthyretin Amyloid Cardiomyopathy.
N Engl J Med. 2018 Sep 13;379(11):1007-1016. doi: 10.1056/NEJMoa1805689.

Boersema PJ, Melnik A, Hazenberg BPC, Rezeli M, Marko-Varga G, Kamiie J, Portelius E, Blennow K, Zubarev RA, Polymenidou M, Picotti P.
Biology/Disease-Driven Initiative on Protein-Aggregation Diseases of the Human Proteome Project: Goals and Progress to Date.
J Proteome Res. 2018 Dec 7;17(12):4072-4084. doi: 10.1021/acs.jproteome.8b00401.

Treglia G, Glaudemans AWJM, Bertagna F, Hazenberg BPC, Erba PA, Giubbini R, Ceriani L, Prior JO, Giovanella L, Slart RHJA.
Diagnostic accuracy of bone scintigraphy in the assessment of cardiac transthyretin-related amyloidosis: a bivariate meta-analysis.
Eur J Nucl Med Mol Imaging. 2018 Oct;45(11):1945-1955. doi: 10.1007/s00259-018-4013-4.

Clark CC, Mebius MM, de Maat S, Tielens AGM, de Groot PG, Urbanus RT, Fijnheer R, Hazenberg BPC, van Hellemond JJ, Maas C.
Truncation of ADAMTS13 by Plasmin Enhances Its Activity in Plasma.
Thromb Haemost. 2018 Mar;118(3):471-479. doi: 10.1055/s-0038-1627460.

Klaassen SHC, Tromp J, Nienhuis HLA, van der Meer P, van den Berg MP, Blokzijl H, van Veldhuisen DJ, Hazenberg BPC.
Frequency of and Prognostic Significance of Cardiac Involvement at Presentation in Hereditary Transthyretin-Derived Amyloidosis and the Value of N-Terminal Pro-B-Type Natriuretic Peptide.
Am J Cardiol. 2018 Jan 1;121(1):107-112. doi: 10.1016/j.amjcard.2017.09.029.

2017
Klaassen SHC, Lemmink HH, Bijzet J, Glaudemans AWJM, Bos R, Plattel W, van den Berg MP, Slart RHJA, Nienhuis HLA, van Veldhuisen DJ, Hazenberg BPC.
Late onset cardiomyopathy as presenting sign of ATTR A45G amyloidosis caused by a novel TTR mutation (p.A65G).
Cardiovasc Pathol. 2017 Jul – Aug;29:19-22. doi: 10.1016/j.carpath.2017.04.002.

van Rheenen RWJ, Hazenberg BPC, Dierckx RAJO, Glaudemans AWJM.
Clinical and 123I-SAP scintigraphy findings in three members from a family affected by AGel amyloidosis.
Amyloid. 2017 Mar;24(sup1):155-156. doi: 10.1080/13506129.2017.1284059.

Eelsing E, Bijzet J, Hazenberg B.
Diagnostic accuracy of new indirect ELISAs for free light-chain quantification in fat tissue of patients with AL amyloidosis.
Amyloid. 2017 Mar;24(sup1):46-47. doi: 10.1080/13506129.2017.1284058.

Koopman T, Niedlich-den Herder C, Stegeman CA, Links TP, Bijzet J, Hazenberg BPC, Diepstra A.
Kidney Involvement in Systemic Calcitonin Amyloidosis Associated With Medullary Thyroid Carcinoma.
Am J Kidney Dis. 2017 Apr;69(4):546-549. doi: 10.1053/j.ajkd.2016.09.027.

2016
Nienhuis HL, Bijzet J, Hazenberg BP.
The Prevalence and Management of Systemic Amyloidosis in Western Countries.
Kidney Dis (Basel). 2016 Apr;2(1):10-9. doi: 10.1159/000444206.

Hazenberg AJ, Hazenberg BP, Dikkers FG.
Long-term follow-up after surgery in localized laryngeal amyloidosis.
Eur Arch Otorhinolaryngol. 2016 Sep;273(9):2613-20. doi: 10.1007/s00405-016-4061-y.

Gillmore JD, Maurer MS, Falk RH, Merlini G, Damy T, Dispenzieri A, Wechalekar AD, Berk JL, Quarta CC, Grogan M, Lachmann HJ, Bokhari S, Castano A, Dorbala S, Johnson GB, Glaudemans AW, Rezk T, Fontana M, Palladini G, Milani P, Guidalotti PL, Flatman K, Lane T, Vonberg FW, Whelan CJ, Moon JC, Ruberg FL, Miller EJ, Hutt DF, Hazenberg BP, Rapezzi C, Hawkins PN.
Nonbiopsy Diagnosis of Cardiac Transthyretin Amyloidosis.
Circulation. 2016 Jun 14;133(24):2404-12. doi: 10.1161/CIRCULATIONAHA.116.021612.

Adams D; European Network for TTR-FAP (ATTReuNET).
Optimizing the management of transthyretin familial amyloid polyneuropathy in Europe: early diagnosis and effective care.
Curr Opin Neurol. 2016 Feb;29 Suppl 1:S1-2. doi: 10.1097/WCO.0000000000000294.

Adams D, Suhr OB, Hund E, Obici L, Tournev I, Campistol JM, Slama MS, Hazenberg BP, Coelho T; European Network for TTR-FAP (ATTReuNET).
First European consensus for diagnosis, management, and treatment of transthyretin familial amyloid polyneuropathy.
Curr Opin Neurol. 2016 Feb;29 Suppl 1:S14-26. doi: 10.1097/WCO.0000000000000289.

For the complete list of publications, download pdf file here.

 


Videos and presentations

Instructionfilm How to detect Amyloid by aspiration of subcutaneous fat tissue for taking and sending an abdominal subcutaneous fat tissue aspirate (GrACE)

An informational film made by Greg Singer “ Amyloidosis Awareness ” can be viewed here or a smaller version with Dutch subtitles via Youtube

A 3-part Dutch Documentary on Amyloidosis, the misunderstood disease in which doctors from the Amyloidosis Expertise Center (GrACE) talk about the history, diagnosis and treatment options of Amyloidosis.

These clips, including the trailer, can also be seen on the site herkenamyloidose.nl
Trailer Documentary Amyloidosis

Part 1: The history of amyloidosis

Part 2: Diagnosis

Part 3: Treatment

 

A Dutch talkshow organized by Pfizer about Amyloidosis, the misunderstood disease in which Amyloidosis experts from the UMCG and the UMCU discuss the problems around the different forms of Amyloidosis in the Netherlands.
These five clips can also be seen on the site herkenamyloidose.nl

Part 1: Amyloidosis in the Netherlands

Part 2: ATTR and hereditary

Part 3: Diagnosis

Part 4: Cardiac amyloidosis

Part 5: Center of Expertise

 

1st Multidisciplinary Symposium Systemic Amyloidosis:
From diagnostics to treatment

 
The first edition of the Symposium Systemic Amyloidosis took place in Utrecht on Friday 22 November 2019.
A multidisciplinary meeting with almost 100 hematologists, cardiologists, nephrologists, allergists / immunologists, pathologists, neurologists, rheumatologists, nursing specialists and others from the Netherlands and Belgium. A video report was made this day by Jasmine van Es

Amyloid cardiomyopathy – diagnosis and typing by Hans Nienhuis during the CVGK spring meeting Heart Failure on April 8, 2019

Treatment options for amyloid cardiomyopathy by Peter van der Meer during the CVGK spring meeting Heart Failure on April 8, 2019

Ten minutes of education by Ronald van Rheenen on the Contribution nuclear medicine for diagnosis of cardiac amyloidosis on November 20, 2019 (CVGK-site).

Meet and Learn by Ronald van Rheenen about Early detection of Amyloidosis with the EPD.


Presentations

Sep’21 3rd European ATTR meeting – Bouke Hazenberg

Sep’21 3rd European ATTR meeting – Hendrea Tingen Mrt’21 Patiëntendag SAN – Hans Nienhuis Nov’20 2e Systemische Amyloïdose Symposium – Hans Nienhuis

Nov’20 2e Systemische Amyloïdose Symposium – Paul van der Zwaag Aug’20 Alnylam online Symposium – Bouke Hazenberg Feb’20 patiëntendag SAN – Maarten vd Berg

Feb’20 patiëntendag SAN – Hans Nienhuis Feb’20 patiëntendag SAN – Paul vd Zwaag Jan’20 NVvKI – Hans Nienhuis

Dec’19 NVCC – Hans Nienhuis Dec’19 Werkgroep Cardiogenetica – Hans Nienhuis Dec’19 Workshop Nefrologie – Hans Nienhuis

Nov’19 1e Amyloidosis Symposium – Bouke Hazenberg Nov’19 1e Amyloidosis Symposium – Hans Nienhuis Nov’19 1e Amyloidosis Symposium – Ronald van Rheenen

Apr’19 NIV dagen – Hans Nienhuis Apr’19 NIV dagen – Friso Muntinghe & Hans Nienhuis Apr’19 Berlijn – Hans Nienhuis

Feb’19 ARiA Symp – Bouke Hazenberg Feb’19 ARiA Symp – Paul van der Zwaag 2018 – Bouke Hazenberg

 

Posters

2020 The ISA’s XVIIth International Symposium on Amyloidosis – Virtual meeting Tarragona, Spain

2018 The ISA’s XVIth International Symposium on Amyloidosis – Kumamoto, Japan

2016 The ISA’s XVth International Symposium on Amyloidosis – Uppsala, Sweden

2014 The ISA’s XIVth International Symposium on Amyloidosis – Indianapolis, USA

2012 The ISA’s XIIIth International Symposium on Amyloidosis – Groningen, The Netherlands

 

Support

The Amyloidosis Expertise Center conducts scientific research in the field of early recognition and typing of amyloid, mapping of organ manifestations, the possibilities for treatment and the monitoring of amyloidosis.

For the funding of this innovative research, our Center is almost completely reliant on donations and sponsorship. Your donation to the Amyloidosis Expertise Center will benefit research in the field of amyloidosis. For donations, the Center has its own reference number (Amyloid 4950202) within the Stichting Steunfonds of the UMCG.

Donate
You can make a donation to our bank account number NL21 ABNA 0423 1266 95, account name “Stichting Steunfonds UMCG”, with the reference “Amyloid 4950202”.

Leave a legacy gift in your will
You can also choose to leave money in your will. For this you can get in touch with a legal professional directly, or contact our fundraising department. It is important to include the correct name and details in your will: Stichting Steunfonds UMCG, Chamber of Commerce number: 63378949. In addition, you must include the reference: Amyloid 4950202

Tax exemption
The Stichting Steunfonds UMCG has been designated by the tax authorities as an ‘ANBI’ (Algemeen Nut Beogende Instelling). As a result, a donation to our department is exempt from gift and inheritance tax. Tax advantages also mean that a donation can be (partially) deducted from income tax.

Information
If you would like to discuss your donation, if you have a specific request or if you would like more information about a registered fund or a legacy gift, please contact Ms N.S. Eilander.

Would you like more information about the research we’re doing on Amyloidosis? Please feel free to contact the Amyloidosis Expertise Center: