• Amyloid · Mar 2013

    A novel method for quantifying peripheral tissue amyloid load by using the radiolabeled amyloidophilic peptide, p5.

    • Jonathan S Wall, Tina Richey, Sally Macy, Eric Heidel, Craig Wooliver, and Stephen J Kennel.
    • Department of Medicine, University of Tennessee Graduate School of Medicine, Knoxville, TN 37920, USA. jwall@utmck.edu
    • Amyloid. 2013 Mar 1; 20 (1): 21-6.

    AbstractQuantitation of peripheral amyloid deposits by non-invasive molecular imaging can be useful for diagnosis, prognostication and monitoring response to therapy. In order to obtain reliable quantitative data, it is necessary to show a linear positive correlation between the uptake of the molecular probe and the tissue amyloid load. The transgenic H-2/IL-6 mouse model of AA amyloidosis was used to generate animals with varied stages of visceral amyloid disease. The mice were injected with 125I-labeled peptide p5 and tissues analyzed 2 h post-injection using Congo red (CR) staining, radioisotope biodistribution and micro-autoradiography (ARG). Micro-ARG confirmed that 125I-p5 was deposited at all amyloid deposits and sites of Congophilia but not at amyloid-free sites within the tissues evaluated. Furthermore, biodistribution studies revealed that the amount of 125I deposited in liver and spleen correlated with the amount of CR birefringence (expressed as 0-4+ or as tissue area [µm2]) in these tissues with correlation coefficients of r > 0.7 (p < 10(-6)). Deposition of 125I-p5 is a quantitative measure of the amount of AA amyloid in liver and spleen in this mouse model. The p5 peptide has potential as a quantitative amyloid imaging agent in human disease.

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