Abstract
Using a sensitive, quantitative, and non-invasive in vivo method, based on the specific binding of serum amyloid P component to amyloid fibrils, we have directly documented the spontaneous resolution of AA amyloid deposits in mice, and the prolonged existence thereafter of a primed state of enhanced susceptibility to further amyloid deposition. These results may have important implications for understanding and management of amyloidosis in humans.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amyloid / metabolism
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Amyloidosis / immunology
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Amyloidosis / metabolism*
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Amyloidosis / pathology
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Animals
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Antigen-Antibody Complex / immunology
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Female
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Glycoproteins
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Humans
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Iodine Radioisotopes
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Liver / metabolism
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Mice
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Mice, Inbred CBA
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Remission, Spontaneous
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Serum Amyloid P-Component / metabolism
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Serum Amyloid P-Component / pharmacokinetics
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Spleen / metabolism
Substances
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Amyloid
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Antigen-Antibody Complex
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Glycoproteins
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Iodine Radioisotopes
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Serum Amyloid P-Component
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amyloid enhancing factor