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Subcellular localization of pyruvate dehydrogenase dihydrolipoamide acetyltransferase in human intrahepatic biliary epithelial cells
Author(s) -
Joplin Ruth,
Wallace Lorraine L.,
Johnson Gerald D.,
Lindsay J. Gordon,
Yeaman Stephen J.,
Palmer Jeremy M.,
Strain Alastair J.,
Neuberger James M.
Publication year - 1995
Publication title -
the journal of pathology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.964
H-Index - 184
eISSN - 1096-9896
pISSN - 0022-3417
DOI - 10.1002/path.1711760409
Subject(s) - dihydrolipoamide dehydrogenase , pyruvate dehydrogenase complex , chemistry , subcellular localization , biochemistry , enzyme , cytoplasm
In previous histological studies, biliary epithelial cells (BEC) in the liver of patients with primary biliary cirrhosis (PBC), but not controls, reacted strongly with antibodies specific for the major autoantigen associated with PBC, the E2 component of pyruvate dehydrogenase complex (PDC‐E2). In this study we have used transmission electron microscopy (TEM) to document the precise subscellular localization of PDC‐E2 in BEC. Two antibodies which recognize PDC‐E2 were used: affinity‐purified anti‐PDC‐E2 raised in rabbits; and human antibody from the serum of patients with PBC, affinity‐purified against human heart PDC. The intracellular localization of antibody binding was determined by laser scanning confocal microscopy and TEM. Both antibodies bound to the inner membrane of mitochondria in BEC isolated from both patients with PBC and controls, but binding to the external aspect of the plasma membrane was observed only in BEC from patients with PBC. Surface antigen expression in PBC may make BEC immunological targets.