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  • Title: Comparative analysis of peptide p5 and serum amyloid P component for imaging AA amyloid in mice using dual-isotope SPECT.
    Author: Wall JS, Richey T, Williams A, Stuckey A, Osborne D, Martin E, Kennel SJ.
    Journal: Mol Imaging Biol; 2012 Aug; 14(4):402-7. PubMed ID: 22042488.
    Abstract:
    PURPOSE: I-labeled human serum amyloid P component (SAP) is used clinically only in the UK for imaging visceral amyloidosis to assist with diagnosis, disease staging, and monitoring response to therapy. We compare a new amyloid-reactive probe, peptide p5, with SAP for imaging amyloidosis. PROCEDURES: Dual-energy SPECT/CT images were acquired of (125)I-labeled SAP and (99m)Tc-labeled p5 in mice with systemic AA amyloidosis (n = 3). Twelve organs and tissues were harvested for radiotracer biodistribution assessment and for micro-autoradiographic analysis. RESULTS: I-SAP and (99m)Tc-p5 localized equivalently in amyloid deposits in liver (∼10% injected dose (ID)/g) whereas (125)I-SAP was twofold higher in the spleen (∼20% ID/g; (99m)Tc-p5, ∼10% ID/g). In contrast, (99m)Tc-p5 was bound to pancreatic and intestinal amyloid approximately fivefold more efficiently as evidenced in biodistribution data. CONCLUSIONS: Radiolabeled p5 is an effective amyloid-imaging radiotracer as compared to SAP in the murine model of amyloidosis and may be rapidly translated for imaging patients with visceral amyloidosis in the USA.
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