Summary
Localization of protein AP, which is known to be associated with all amyloid-laden tissues in systemic amyloidoses, was studied by an immunocytochemical peroxidase-antiperoxidase staining method in a series of localized amyloidosis, i.e. islet amyloid, lichen amyloidosus, and nodular amyloidosis of the respiratory and urinary tracts. The amyloid fibrils of these localized amyloidoses are believed to be of three different chemical classes belonging to the AE, AD and AL type, respectively. The present study revealed that protein AP was present in amyloid deposits in all tissues examined, thus supporting that protein AP is present in amyloid deposits not only of all types of systemic amyloidosis but also different forms of localized amyloidosis.
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Supported by the Swedish Medical Research Council (Project No. B81-12X-05941-01), the Research Fund of King Gustaf V and grants from the United States Public Health Service, National Institute of Arthritis, Metabolism and Digestive Diseases (AM 04599 and AM 07014), National Institute of Health Multipurpose Arthritis Center (AM 20613), from the General Clinical Research Centers Branch of the Division of Research Resources, National Institutes of Health (RR 533), from the Massachusetts Chapter of the Arthritis Foundation and from the Arthritis Foundation
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Westermark, P., Shirahama, T., Skinner, M. et al. Amyloid P-component (protein AP) in localized amyloidosis as revealed by an immunocytochemical method. Histochemistry 71, 171–175 (1981). https://doi.org/10.1007/BF00507821
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DOI: https://doi.org/10.1007/BF00507821