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  • Title: An immunohistochemical study of amyloid P component, apolipoprotein E and ubiquitin in human and murine amyloidoses.
    Author: Cui D, Hoshii Y, Takahashi M, Kawano H, Iwata T, Ishihara T.
    Journal: Pathol Int; 1998 May; 48(5):362-7. PubMed ID: 9704343.
    Abstract:
    Amyloid P component (AP) and apolipoprotein E (Apo E), which are known to be minor constituents of amyloid deposits, commonly are associated with almost all types of amyloid deposits. In this study, the distribution of AP-, Apo E- and ubiquitin (Ub)-immunoreactivity (IR) in amyloid deposits in the liver and spleen of human systemic amyloidosis (34 autopsy cases: 17 immunoglobulin light chain derived, 17 amyloid A protein derived) and experimental murine amyloidosis is examined using an immuno-histochemical technique. In human cases, all of the amyloid deposits examined showed colocalization of AP- and Apo E-IR with individual amyloid proteins. In experimental amyloidosis, AP-IR of amyloid deposits in the liver and spleen and Apo E-IR in the liver were seen uniformly throughout this experiment. In contrast, Apo E-IR in the spleen was not uniform at the phase of amyloid deposition. At 4 weeks and at 16 weeks after casein injection, Apo E-IR was unevenly distributed in amyloid deposits in the perifollicular area; however, from 6 to 12 weeks it was seen to be uniform. Ubiquitin-IR of amyloid deposits in human cases was seen in 22 of 34 livers and in 22 of 33 spleens. In experimental amyloidosis, Ub-IR of amyloid deposits was demonstrated in the space of Disse in all mice examined, and there appeared to be a gradual increase in intensity with the amount of amyloid deposition. However, in the spleen, amyloid deposits did not react with anti-Ub antibody in any phase of amyloid induction. These results suggest that Apo E and Ub are not always associated with the process of amyloid deposition and may appear in a deposit after the deposition.
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