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A 40-year-old man is being examined for exercise intolerance. The patient develops severe shortness of breath 5 minutes after exercising. The patient also complains of knee pain that worsens throughout the day and improves with rest. Family history is significant for an uncle with ulcerative colitis. Echocardiography reveals a thickening of the walls of both ventricles. ECG reveals low-voltage electrical activity. A biopsy of the heart is taken and reveals infiltration of the walls of the ventricles by inclusion that has apple green color under polarized light. Which of the following has most likely resulted in this patient’s cardiac abnormalities?  

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Age-related amyloidosis p. 218


cardiomyopathy with p. 308

carpal tunnel syndrome p. 449

classification p. 218

kidney deposition in p. 597

multiple myeloma p. 431

with rheumatoid arthritis p. 466

Atrial amyloidosis p. 218

Diabetes mellitus type p. -19, 352

amyloidosis p. 218

Dialysis-related amyloidosis p. 218

Hereditary amyloidosis p. 218

Localized amyloidosis p. 218

Multiple myeloma p. 431

amyloidosis p. 218

Primary amyloidosis p. 218, 697

Secondary amyloidosis p. 218

Systemic amyloidosis p. 218

Systemic senile amyloidosis p. 218

Thyroid cancer p. 343

amyloidosis in p. 218


In amyloidosis, “amyloid” refers to starch-like, and it goes back to an observation made by the German scientist Rudolf Virchow, who saw mysterious deposits in the tissue that stained blue with iodine, just like plant starch.

As it turns out, amyloids are actually just proteins that take on an abnormal shape, which makes them stick together and settle in tissues.

And amyloidosis is the name for the disease that develops as a result of the tissue damage from these protein deposits.

Normally, our cells produce thousands of proteins each and every moment, and these proteins need to fold into a particular shape in order to do their jobs properly.

If a protein folds incorrectly, it’s normally spotted right away and destroyed by proteases, which are enzymes that chop up larger proteins into tiny bits.

In amyloidosis, there are a few different ways that protein folding can go wrong.

One way is when normal proteins are produced in enormous amounts, and just a small fraction of them fold incorrectly.

A second option is that abnormal proteins with incorrect amino acid sequences are produced in normal amounts, and they fold incorrectly.

Either way, the misfolded proteins, called amyloids start to build up.

Sometimes there’s simply too many of them for the protease to handle, and other times, the way that they’re folded makes them tough to break down - a bit like a pistachio that doesn’t have an opening for your fingers to work with. Nightmare.

When the amyloid proteins get excreted out of the cell, they tend to clump together forming a rigid, insoluble structure called a β-sheet - like a folded sheet of paper.

These β- sheets then deposit in the extracellular space of tissues and cause damage.

So amyloidosis is a process where there are extra protein deposits, and there are many different proteins and diseases that follow that same underlying process.

In general, amyloidosis can be systemic, meaning that those protein deposits occur in multiple organ systems, or it can be localized, meaning that they occur in one organ.

Until recently, systemic amyloidosis was further broken down into primary amyloidosis, which is where amyloidosis was thought to be the main problem, and secondary amyloidosis, which is where there was another known disease process that resulted in the protein deposits.


  1. "Robbins Basic Pathology" Elsevier (2017)
  2. "Harrison's Principles of Internal Medicine, Twentieth Edition (Vol.1 & Vol.2)" McGraw-Hill Education / Medical (2018)
  3. "Pathophysiology of Disease: An Introduction to Clinical Medicine 8E" McGraw-Hill Education / Medical (2018)
  4. "CURRENT Medical Diagnosis and Treatment 2020" McGraw-Hill Education / Medical (2019)
  5. "The Systemic Amyloidoses" New England Journal of Medicine (1997)
  6. "Amyloidosis" Rheumatic Disease Clinics of North America (2013)
  7. "Protein Misfolding, Amyloid Formation, and Human Disease: A Summary of Progress Over the Last Decade" Annual Review of Biochemistry (2017)
  8. "Processing of synthetic pro-islet amyloid polypeptide (proIAPP) ‘amylin’ by recombinant prohormone convertase enzymes, PC2 and PC3, in vitro" European Journal of Biochemistry (2000)

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