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Researchers at IU School of Medicine have made significant scientific contributions to the field of amyloidosis.

Amyloid Research

What is amyloidosis?

The word amyloid means “starch-like (see Figure 1).” In 1854 a German pathologist Rudolph Virchow used the term amyloid to describe the deposits found in AA (reactive/secondary) amyloidosis. Since then scientists have found that many proteins can form amyloid fibrils and deposit extracellularly and causes organ and tissue dysfunction. The characteristics of proteins that can form amyloid fibrils include positive staining with Congo red dye, apple green refringence under polarized light, and a β-pleated sheet conformation. Essentially the type of amyloid is recognized by the specific protein which forms the basis of amyloid tissue deposits in each of the diseases called amyloidosis.

The recommended nomenclature to describe the different forms of amyloidosis includes the letter “A” for amyloid followed by the abbreviation of the parent protein. For example ATTR amyloidosis refers to amyloidosis caused by fibril deposition of the protein transthyretin (TTR) extracellularly in organs and tissues. AL amyloidosis is defined as the deposition of immunoglobulin light chain fibrils. The parent protein that forms the amyloid fibril determines the clinical course. ATTR and AL are the most common forms of systemic amyloidosis.

Left: Amyloid fibrils isolated from the liver from a patient with AL amyloidosis. Right: Amyloid fibrils isolated from the heart in a patient with ATTR amyloidosis.

Transthyretin Amyloidosis

Transthyretin amyloidosis (ATTR) is a disease caused by the abnormal accumulation of protein molecules in body tissues. These protein accumulations or "amyloid deposits" are made from a blood protein, transthyretin (TTR), which normally transports thyroid hormone and vitamin A to the body tissues. When an inherited defect in the TTR protein occurs, this abnormal form of TTR has the tendency to accumulate in tissues such as the heart, kidneys, nerves, and intestine. The presence of these deposits interferes with the normal functions of the organs. and as the deposits enlarge more tissue damage occurs and the disease (TTR amyloidosis) worsens.

Learn more about amyloidosis.

Indiana University Amyloidosis Center

History of the Indiana University Amyloidosis Center

Dr. Merrill Benson saw his first case of transthyretin amyloidosis in July 1973 at Boston University School of Medicine. Dr. Benson established the Indiana University Amyloid Center in July 1976. Between 1976-2020 there have been significant scientific contributions to the field of amyloidosis from the Indiana University Amyloid Center. Between 1979 to 2009, 25 hereditary mutations in transthyretin (TTR) were described by the research group at Indiana University. The genetic basis of several other mutations causing amyloidosis and other neurodegenerative diseases was also discovered including discovery of a mutation in the β amyloid gene which causes hereditary Alzheimer’s disease and was the basis of a transgenic model of Alzheimer’s disease. A mouse model was also developed for transthyretin amyloidosis (ATTR) which was used to develop a treatment of ATTR with specific antisense oligonucleotides (ASO). The working hypothesis was that a transthyretin (TTR) specific ASO would inhibit liver production of TTR and thus decreased amyloid production and end organ damage. Ionis Pharmaceuticals then developed and tested use of a transthyretin specific ASO, inotersen in humans. Inotersen was found to significantly inhibit progression of transthyretin familial polyneuropathy in the pivotal phase III NEURO-TTR study that was published in the New England Journal of Medicine in July 2018. Inotersen (Tegsedi™) was approved by the EU July 2018 and by the FDA October 2018 and is one of the breakthrough treatments for a previously fatal, debilitating disease.


10193-Kincaid, John

John C. Kincaid, MD

Kenneth L. and Selma G. Earnest Professor of Neurology

Performs neurologic assessment of peripheral nerves

Read Bio John C. Kincaid, MD

4996-Abonour, Rafat

Rafat Abonour, MD

Harry and Edith Gladstein Professor of Cancer Research

Diagnosis and treats immunoglobulin light chain amyloidosis

Read Bio Rafat Abonour, MD

5140-Dasgupta, Noel

Noel R. Dasgupta, MD

Associate Professor of Clinical Medicine

Diagnoses and treats all forms of amyloidosis with a focus on cardiac amyloidosis

Read Bio Noel R. Dasgupta, MD

Janna Hilligoss, LPN, CRCC, Senior Clinical Research Coordinator
Coordinates clinical research studies

Alisa Gumm, RN, Research Coordinator
Coordinates clinical research studies

Gabriela Riera
Research Associate

April Gregory-Snyder, RN-BSN, Clinical Research Coordinator
Coordinates clinical research studies

Connor Hoover
Research Associate

Contact Information

Common Office Phone: (317) 278-3428
Fax: (317) 274-4304

Location of Clinical Services

Indiana University Hospital
550 North University Boulevard AOC, Room 5014
Indianapolis, IN 46202

IU Health Cardiology
Methodist Hospital
1801 N. Senate, Suite 4000
Indianapolis, IN, 46202