Broadly speaking, amyloidosis (pronounced ‘am-uh-loy-
doh-sis’) is one class in a growing list of protein folding dis-
orders. While there are many distinct types of amyloidosis,
in all cases the misfolded proteins, called amyloid (meaning
‘starch-like’), take on a particular shape that makes it diffi-
cult for the body to break down. Because of this misfolding,
the amyloid proteins bind together to form rigid, linear fibers
(or fibrils) that accumulate in our body’s organs and tissues.
Depending on where the amyloid builds up, such as in the
kidney, heart and nerves, different symptoms and potentially
life-threatening conditions become manifest.
While amyloidosis has been known since the 19th century, it
is only within the last few decades that our understanding of
it has matured. Presently, there are over 25 different proteins
that have been identified as contributing to amyloidosis (the
major forms of which are described in the next section). Ad-
ditional types of precursor proteins that can lead to amyloid
formation continue to be discovered through ongoing re-
search.
Certainly, amyloidosis is a rare condition and often over-
looked. Each year, an estimated 50,000 people worldwide
will become afflicted with the disease, with more than 3,000
people being diagnosed in North America alone. This is
about 1/5 of the incidence of multiple myeloma, and of
similar incidence to that of Hodgkin’s disease or chronic my-
elogenous leukemia. Because of its rarity, medical students