Amyloid P-component and the skin

Autor: Helmut Hintner, Stephen M. Breathnach
Rok vydání: 1990
Předmět:
Zdroj: Clinics in dermatology. 8(2)
ISSN: 0738-081X
Popis: Amyloid deposits, regardless of clinicopathologic type or tissue involvement, are composed of a loose meshwork of 7.5- to 10-nm fibrils. 1 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. 2,3 This novel amyloid tissue protein was termed amyloid P (plasma)-component, or protein AP (AP), because of its antigenic identity to an α-globulin present in the blood of normal individuals. 4–6 AP is a glycoprotein found in tissue deposits of all forms of amyloid in which it has been sought, irrespective of the chemical nature of the amyloid fibril protein, with the single exception of certain intracortical amyloids. 7,8 AP is indistinguishable from, and derived from, the normal plasma glycoprotein serum amyloid P-component (SAP). 7,9,10 A protein which cross-reacts immunochemically with SAP has been shown to be a normal matrix glycoprotein of glomerular basement membrane; we have shown in immunohistochemical studies that this normal tissue form of amyloid P-component (TAP) is also invariably associated with elastic fiber microfibrils in normal, adult, human skin and other tissues. 11,12 This chapter will summarize and review our current knowledge of the biology of amyloid P-component, including its potential role in the maintenance of normal connective-tissue architecture, and the deposition of amyloid deposits.
Databáze: OpenAIRE