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Immunological
Medicine Unit, Division of Medicine, ICSM, Hammersmith Hospital, London W12 0NN, UK
Correspondence to: Dr J D Gillmore.
| The first 150 words of the full text of this article appear below. |
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Introduction |
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Amyloidosis is a generic term for a heterogeneous group of disorders associated with deposition of protein in an abnormal fibrillar form.1 The diverse spectrum of amyloid related diseases is now recognised to include Alzheimer's disease, type II diabetes, and the transmissible spongiform encephalopathies. Amyloidosis can be hereditary or acquired, localised or systemic, and potentially lethal or merely an incidental finding.
Amyloid deposits consist mainly of protein fibrils, the varying peptide
subunits of which constitute the basis for its classification (table
1).2 Despite much heterogeneity among their respective precursor proteins, all amyloid fibrils have a remarkably similar adopted ultrastructure and share many physicochemical properties attributable to their acquired rich
-sheet content.3
Certain glycosaminoglycans (GAGs) are invariably associated with the
fibrils and, in addition, all amyloid deposits contain the normal
plasma protein serum amyloid P component (SAP). The specific binding interaction between SAP and all amyloid fibrils is the basis for
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