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Imaging of experimental amyloidosis with <sup>131</sup>i‐labeled serum amyloid p component

Dan CaspiIchilov Hospital, Tel Aviv University, Sackler School of Medicine, IsraelSamuel ZalzmanSpecialist in Nuclear Medicine, Nuclear Research CenterM BaratzSenior Lecturer in Pathology, Tel Aviv Medical Center, Ichilov Hospital, Tel Aviv University, Sackler School of MedicineZ. TeitelbaumRadiochemical Specialist, Nuclear Research CenterMichael YaronAssociate Professor of Medicine, Tel Aviv Medical Center, Ichilov Hospital, Tel Aviv University, Sackler School of MedicineMordechai PrasProfessor of Medicine, Heller Institute, Sheba Medical CenterM L BaltzSenior Research Officer, MRC Acute Phase Protein Research Group, Immunological Medicine Unit, Royal Postgraduate Medical SchoolMark B. PepysMRC Acute Phase Protein Research Group, Immunological Medicine Unit, Royal Postgraduate Medical School
Arthritis & Rheumatismjournal1987en
ABI

Abstract

131I-labeled human serum amyloid P component, which was injected into mice with experimentally induced systemic AA amyloidosis and into controls, became specifically localized and was retained in amyloidotic organs. In comparison, it was rapidly and completely eliminated from unaffected tissues and from control animals. Distinctive images of this amyloid-specific deposition of labeled serum amyloid P component were derived from whole body scanning, in vivo, of amyloidotic mice. These findings suggest that such imaging may have applications for the diagnosis and quantitation of amyloid deposits in humans.

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