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Journal of Nuclear Medicine

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Meeting ReportRadiopharmaceutical Chemistry: New Radiopharmaceuticals-Broader/General Applications

Imaging the biodistribution of systemic AA amyloidosis in mice using 125I-labeled protamine

Jonathan Wall, Tina Richey, Alan Stuckey, Robert Donnell, Emily Martin, Alan Solomon and Stephen Kennel
Journal of Nuclear Medicine May 2010, 51 (supplement 2) 1484;
Jonathan Wall
1Dept. Medicine, University of Tennessee Graduate School of Medicine, Knoxville, TN
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Tina Richey
1Dept. Medicine, University of Tennessee Graduate School of Medicine, Knoxville, TN
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Alan Stuckey
1Dept. Medicine, University of Tennessee Graduate School of Medicine, Knoxville, TN
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Robert Donnell
2Dept. Pathobiology, University of Tennessee College of Veterinary Medicine, Knoxville, TN
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Emily Martin
1Dept. Medicine, University of Tennessee Graduate School of Medicine, Knoxville, TN
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Alan Solomon
1Dept. Medicine, University of Tennessee Graduate School of Medicine, Knoxville, TN
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Stephen Kennel
1Dept. Medicine, University of Tennessee Graduate School of Medicine, Knoxville, TN
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Abstract

1484

Objectives Amyloid deposits in brain and peripheral organs contain in addition to protein fibrils a high concentration of heparan sulfate proteoglycans (HSPG). Data suggest that the chemical structure of amyloid-associated heparan sulfate differs from that found ubiquitously in the extra-cellular matrix of all normal tissues rendering it a potential new biomarker for these pathologic deposits. Therefore, we have studied the biodistribution of the heparin-binding peptide protamine as a novel agent for amyloid imaging.

Methods Synthetic protamine was purified by HPLC and the amino acid sequence confirmed by MS. 125I-labeled protamine (125I-protamine) was administered to mice with systemic AA amyloidosis or to amyloid-free animals and allowed to circulate for 1, 2, 4, 8 or 24 h. At each time point microSPECT/CT images were acquired and the tissue distribution of the radioactivity determined by gamma counting. Finally, 6 µm-thick tissue sections were prepared for autoradiography and histological evaluation.

Results In disease-free mice the 125I-protamine was rapidly dehalogented and 125I- sequestered by the stomach which, with the thyroid was visible in SPECT images up to 8 h post-injection. In contrast, 125I-protamine when injected into AA mice was observed by SPECT within the liver, kidney, pancreas and spleen (sites of AA amyloid), where tissue:muscle ratios were at least 2-fold greater in mice with amyloid as compared to the WT animals, indicating specific retention of the p48 peptide by AA deposits. Micro-autoradiography confirmed that 125I-protamine preferentially associated with the AA amyloid deposits. In amyloid-free mice there was little accumulation of 125I-protamine in any organ or tissue.

Conclusions These data indicate that even though HS is expressed in normal tissue, the heparin-reactive peptide protamine may be used for specific imaging of amyloid diseases.

Research Support Supported by USPHS grant 1R01DK079984

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Journal of Nuclear Medicine
Vol. 51, Issue supplement 2
May 2010
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Imaging the biodistribution of systemic AA amyloidosis in mice using 125I-labeled protamine
Jonathan Wall, Tina Richey, Alan Stuckey, Robert Donnell, Emily Martin, Alan Solomon, Stephen Kennel
Journal of Nuclear Medicine May 2010, 51 (supplement 2) 1484;

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Imaging the biodistribution of systemic AA amyloidosis in mice using 125I-labeled protamine
Jonathan Wall, Tina Richey, Alan Stuckey, Robert Donnell, Emily Martin, Alan Solomon, Stephen Kennel
Journal of Nuclear Medicine May 2010, 51 (supplement 2) 1484;
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