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Radiology, Vol 181, 245-249, Copyright © 1991 by Radiological Society of North America
ARTICLES |
R Weissleder, AS Lee, AJ Fischman, P Reimer, T Shen, R Wilkinson, RJ Callahan and TJ Brady
Department of Radiology, Massachusetts General Hospital, Harvard Medical School, Charlestown 02129.
Human polyclonal immunoglobulin (Ig) G was attached to a monocrystalline iron oxide nanocompound (MION), a small superparamagnetic probe developed for receptor and antibody magnetic resonance (MR) imaging. The resulting complex, MION-IgG, had a slightly negative surface charge, a molecular weight of 150-180 kDa, and 0.36 microgram of IgG attached per milligram of iron. After intravenous administration of MION-IgG to normal rats, most of the compound localized in liver, spleen, and bone marrow. In an animal model of myositis, MION-IgG caused reduced signal intensity (most apparent on T2- weighted spin-echo and gradient-echo images) at the site of inflammation. No change in signal intensity existed after an injection of unlabeled MION. Site-specific localization of MION-IgG was corroborated with scintigraphic imaging with indium-111 IgG and MION-In- 111-IgG and was confirmed histologically with iron staining. These results indicate that antibody MR imaging is feasible in vivo. Target- specific and antibody MR imaging could be easily extended to other applications, including detection of cancer, infarction, and degenerative diseases.
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