The term ‘amyloid’ was used originally to describe
certain deposits found post-
mortem in organs and tissues, which gave a positive reaction when
stained with
iodine (Virchow, 1854). Only later was it realized that the material was
in fact
predominantly proteinaceous, although it is known to be associated with
carbohydrates, particularly glucosoaminoglycans, when obtained from many
ex
vivo sources. With the increasing precision in the definition of amyloid,
initially
from its characteristic green birefringence when stained with the dye Congo
Red
(Missmahl & Hartwig, 1953), and later from its particular appearance
under the
electron microscope (Cohen & Calkins, 1959) and its X-ray diffraction
pattern
(Eanes & Glenner, 1968), it has become evident that it is a specific
fibrillar protein
state, which can also be formed by some proteins when denatured in
vitro (Burke
& Rougvie, 1972), and by synthetic oligopeptides (Bradbury et al.
1960) that may
form amyloid spontaneously when placed in pure aqueous medium (Serpell,
1996). Although these latter may form useful experimental systems for the
study
of amyloid, its major interest at present is that it is associated with
a number of
prominent lethal diseases (Benson & Wallace, 1989; Pepys, 1994).