Summary
The localization of amyloid P-components is demonstrated by immunofluorescence microscopy in normal human tissue (kidney, spleen, liver). The relation to collagen and to amyloidosis is discussed.
References
Kefalides, N.A.: A collagen of unusual composition and a glytoprotein isolated from canine glomerular basement membrane. Biochem. Biophys. Res. commun.22, 26–32 (1966)
Rojkind, M.: Reticulins. In: The biochemistry of disease, Vol. 3, Molecular pathology of connective tissue. (R. Perez-Tamayo, M. Rojkind, eds.), p. 76. New York: Marcel Dekker 1973
Sainte-Marie, G.: A Paraffin embedding technique for studies empolying immunofluorescence. J. Histochem. Cytochem.10, 250–256 (1962)
Skinner, M., Cohen, A.S.: Aspects of the Amyloid P-component. In: Amyloidosis. (O. Wegelius, A. Pasternak, eds.), p. 339. London-New York-San Francisco: Academic Press 1976
Spark, E.L., Shirahama, T., Skinner, M., Cohen, A.S.: The identification of amyloid P-component (protein AP) in normal cultured human fibroblasts. Lab. Invest.38, 556–559 (1978)
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Supported by the Deutsche Forschungsgemeinschaft
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Schneider, H.M., Loos, M. Amyloid P component — A special type of collagen?. Virchows Arch. B Cell Path. 29, 225–228 (1978). https://doi.org/10.1007/BF02899355
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DOI: https://doi.org/10.1007/BF02899355