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Pathogenesis and Therapy

Stephen M. Breathnach, MA, MD, MRCP

Arch Dermatol. 1985;121(4):470-475.

	Since this article does not have an abstract, we have provided the first 150 words of the full text PDF and any section headings.

The term amyloidosis refers to the extracellular deposition of an abnormal protein material with characteristic tinctorial properties and ultrastructural features.¹ Under the electron microscope, amyloid deposits consist largely of a loose network of 7.5 to 10-nm rigid, linear, nonbranching, aggregated, paired fibrils of indefinite length and with hollow cores on profile.² Infrared spectroscopy and X-ray diffraction crystallography have revealed that amyloid fibrils are usually composed of polypeptide chains arranged perpendicularly to the long axis of the fibril with the conformation of a meridional, antiparallel, β-pleated sheet.^3,4 During the course of purification of extracted amyloid fibril preparations, a further amyloid tissue protein, quite separate from the fibrillar component of amyloid deposits, was identified.⁵ This novel amyloid tissue protein, termed amyloid P (plasma) component (AP) because of its antigenic identity to an -globulin in the blood of normal individuals,⁶ may represent up to 14% by weight of extracted amyloid material.¹ . . . [Full Text PDF of this Article]

Author Affiliations
Bethesda, Md

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