Imaging of experimental amyloidosis with <sup>131</sup>i‐labeled serum amyloid p component
Dan Caspithe Heller Institute, Sheba Medical CenterSamuel ZalzmanTel Aviv Medical Center, Ichilov Hospital, Tel Aviv University, Sackler School of Medicine, Tel Aviv, Israel; The Nuclear Research Center, The Negev, Israel; the Heller Institute, Sheba Medical Center; Tel Hashomer, Israel; and the MRC Acute Phase Protein Research Group, Immunological Medicine Unit, Royal Postgraduate Medical School, London, UKM BaratzSenior Lecturer in Pathology, Tel Aviv Medical Center, Ichilov Hospital, Tel Aviv University, Sackler School of MedicineZ. TeitelbaumTel Aviv Medical Center, Ichilov Hospital, Tel Aviv University, Sackler School of Medicine, Tel Aviv, IsraelMichael 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. Pepysthe MRC Acute Phase Protein Research Group, Immunological Medicine Unit, Royal Postgraduate Medical School, London, UK
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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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