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Immunohistochemical and immunochemical study of amyloid in liver affected by systemic Aλ amyloidosis with antibodies against three different regions of immunoglobulin λ light chain
Author(s) -
Kiyama Makiko,
Hoshii Yoshinobu,
Cui Dan,
Kawano Hiroo,
Kanda Takashi,
Ishihara Tokuhiro
Publication year - 2007
Publication title -
pathology international
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.73
H-Index - 74
eISSN - 1440-1827
pISSN - 1320-5463
DOI - 10.1111/j.1440-1827.2007.02106.x
Subject(s) - amyloidosis , immunoglobulin light chain , amyloid (mycology) , antibody , pathology , immunohistochemistry , chemistry , biology , medicine , immunology
The purpose of the present paper was to investigate the heterogeneous nature of amyloid deposits in the liver, by immunohistochemical and immunochemical examination of liver samples from cases of immunoglobulin λ light chain amyloidosis (Aλ amyloidosis) with antibodies generated against the peptides corresponding to the three different regions of the λ light chain. Amyloid deposits in the hepatic artery tended to react better with anti‐λ(118–134) than with anti‐λ(159–175). Amyloid deposits in the space of Disse tended to react weakly or partially with anti‐λ(118–134) but well with anti‐λ(159–175). Amyloid deposits in the portal vein reacted relatively well with both antibodies. By western blotting of water‐extracted amyloid in which amyloid deposits were not stained with anti‐λ(118–134) immunohistochemically, the three antibodies detected 27 kDa bands consistent with the full‐length Ig λ chain and some smaller bands. These findings indicate that amyloid deposits may not be homogeneous in the liver of AL amyloidosis, and that molecular heterogeneity of amyloid fibril protein or a difference in the mode of deposition results in the histopathological heterogeneity of AL amyloid deposits even within a single patient.