Widespread occurrence of AP in amyloidotic tissues

Springer Science and Business Media LLC - Tập 48 - Trang 197-206 - 1985
Tsuranobu Shirahama1,2,3, Martha Skinner1,2,3, Jean D. Sipe1,2,3, Alan S. Cohen1,2,3
1Arthritis Center, Boston University School of Medicine, Boston, USA
2The Thorndike Memorial Laboratory, Boston, USA
3The Division of Medicine, Boston City Hospital, Boston, USA

Tóm tắt

Plasma (P)-component of amyloid (AP or SAP), while not an integral part of the amyloid fibril, has been considered to be intimately associated with virtually every different type of amyloid. In the present study, we evaluated the distribution of AP in the organs frequently involved in two forms of human systemic amyloidosis (AA and AF) and in mouse AA amyloidosis, by use of immunohistochemistry with anti-AP. Although the amyloid deposits generally showed moderate reactions with anti-AP, they were not always clearly distinguished from the surrounding non-amyloid tissue elements which often stained as well. The basement membrane often showed even stronger reaction to anti-AP than the adjacent amyloid deposits, and liver sections demonstrated such a high overall reaction to anti-AP that the anti-AP reaction on the amyloid deposits was often obscurred. The present results suggest that the binding between AP and the amyloid fibril may not be monospecific, that AP by this technique occurs rather widely throughout the body, and therefore that anti-AP may not be considered as specific a marker for amyloid deposits in immunohistochemical and perhaps other studies as well.

Tài liệu tham khảo

Baltz ML, Dyck RF, Pepys MB (1980) Amyloid P-component in mice injected with casein: identification in amyloid deposits in the cytoplasm of hepatocytes. Immunology 41:59–66 Benditt EP, Cohen AS, Costa PP, Franklin EC, Glenner GG, Husby G, Mandema E, Natvig JB, Osserman EF, Sohar E, Wegelius O, Westermark P (1980) Guidelines for nomencalture. In: Glenner GG, Costa PP, Freitas AF (ed) Amyloid and Amyloidosis. Excerpta Medica, Amsterdam, pp XI-XII Breathnach SM, Bhogal B, Dyck RF, de Beer FC, Black MM, Pepys MB (1981) Immunohistochemical demonstration of amyloid P component in skin of normal subjects and patients with cutaneous amyloidosis. Br J Dermatol 105:115–124 Breathnach SM, Melrose SM, Bhogal B, de Beer FC, Black MM, Pepys MB (1982) Immunohistochemical studies of amyloid P component in dosorders of cutaneous elastic tissue. Br J Dermatol 107:443–452 Cathcart ES, Camerford FR, Cohen AS (1965) Immunologie studies on a protein extracted from human secondary amyloid. New Engl J Med 273:143–146 de Beer FC, Baltz ML, Holford S, Feinstein A, Pepys MB (1981) Fibronectin and C4-binding protein are selectively bound by aggregated amyloid P component. J Exp Med 154:1134–1149 Dyck RF, Lockwood CM, Kershaw M, McHugh N, Duance VC, Blatz ML, Pepys MB (1980) Amyloid P-component is a constituent of normal human glomerular basement membrane. J Exp Med 152:1162–1174 Hamon MD, Walker F (1982) The distribution of amyloid P component in normal human skin. Virchows Arch [Cell Pathol] 40:411–415 Hind CRK, Collins PM, Renn D, Cook RB, Caspi D, Baltz ML, Pepys MB (1984) Binding specificity of serum amyloid P component for the pyruvate acetal of galactose. J Exp Med 159:1058–1069 Hsu S-M, Raine L (1984) The use of avidin-biotin-peroxidase complex (ABC) in diagnostic and research pathology. In: De Lellis RA (ed) Advances in immunohistochemistry. Masson Publiching, New York, pp 31–42 Pepys MB, Baltz ML (1983) Acute phase proteins with special reference to C-reactive protein and related proteins (pentaxins) and serum amyloid A protein. Adv Immunol 34:141–212 Pepys MB, Baltz ML, de Beer FC, Dyck RF, Holford S, Breathnach SM, Black MM, Tribe CR, Evans DJ, Feinstein A (1982) Biology of serum amyloid P component. Ann NY Acad Sci [USA] 389:286–297 Puchtler H, Sweat F, Levine M (1962) On the binding of Congo red by amyloid. J Histochem Cytochem 10:355–364 Schneider H-M, Loos M (1978) Amyloid P component — a special type of collagen? Virchow Arch [Cell Pathol] 29:225–228 Shirahama T, Cohen AS (1980) Redistribution of amyloid deposits. Am J Pathol 99:539–550 Shirahama T, Skinner M, Cohen AS (1981) Immunocytochemical identification of amyloid in formalin-fixed paraffin sections. Histochemistry 72:161–171 Shirahama T, Cohen AS, Skinner M (1984) Immunohistochemistry of amyloid. In: DeLellis RA (ed) Advances in immunohistochemistry. Masson Publishing, New York, pp 277–302 Sipe JD, Ignaczak TF, Pollock PS, Glenner GG (1976) Amyloid fibril protein AA: purification and properties of the antigenically related serum component as determined by solid phase radioimmunoassay. J Immunol 116:1151–1156 Skinner M, Cohen AS (1981) The prealbumin nature of the amyloid protein in familial amyloid polyneuropathy (FAP) — Swedish variety. Biochem Biophys Res Commun 99:1326–1332 Skinner M, Cohen AS, Shirahama T, Cathcart ES (1974) P-component (pentagonal unit) of amyloid: isolation, characterization, and sequence analysis. J Lab Clin Med 84:604–614 Skinner M, Shirahama T, Benson MD, Cohen AS (1977) Murine amyloid protein AA in casein-induced experimental amyloidosis. Lab Invest 36:420–427 Skinner M, Sipe JD, Yood RA, Shirahama T, Cohen AS (1982) Characterization of P-component (AP) isolated from amyloidotic tissue: half-life studies of human and murine AP. Ann NY Acad Sci [USA] 389:190–198 Skinner M, Shirahama T, Cohen AS, Deal CL (1983) The association of amyloid P-component (AP) with the amyloid fibril: an updated method for amyloid fibril protein isolation. Prep Biochem 12:461–476 Spark EL, Shirahama T, Skinner M, Cohen AS (1978) The identification of amyloid P-component (protein AP) in normal cultured human fibroblasts. Lab Invest 38:556–559 Sternberger LA (1979) Immunocytochemistry, 2nd ed. John Wiley and Sons, New York, p 354 Tatsuta E, Sipe JD, Shirahama T, Skinner M, Cohen AS (1983) Different regulatory mechanisms for serum amyloid A and serum amyloid P synthesis by cultured mouse hepatocytes. J Biol Chem 258:5414–5418 Westermark P, Shirahama T, Skinner M, Cameron R, Cohen AS (1982) Immunohistochemical evidence for the lack of amyloid P component in some intracerebral amyloids. Lab Invest 46:457–460