title: Staining of pancreatic centroacinar cells, liver bile canaliculi and testicular Leydig cells with a monoclonal antibody against adrenocortical cells.
abstract: The immunoreactivity of a monoclonal antibody against cell suspensions from guinea pig adrenal glands was examined at light- and electron-microscopic levels. In addition to the cell surface membrane of adrenocortical cells, the antibody labeled specific sites in the pancreas, liver and testis, but did not label any of the other tissues examined. In the pancreas, microvilli-like processes and the cell surface membrane of centroacinar cells were immunoreactive to the antibody. The microvilli of interlobular duct cells and pancreatic duct cells were also immunoreactive. In the liver, bile canalicular microvilli of hepatocytes were exclusively labeled. Membrane structures of cell organelles, mainly mitochondria, in testicular Leydig cells were also labeled. Immunoblot analysis showed that the monoclonal antibody bound to two common bands at molecular weights of approximately 62 kDa and 110 kDa in the pancreas, liver, testis, and adrenal gland. The two bands reacted with the digoxigenin-conjugated lectin, Sambucus nigra agglutinin (SNA), which recognizes sialic acid linked alpha (2-6) to galactose. Reaction patterns of SNA in the pancreas, liver and testis were similar to those of the monoclonal antibody; pancreatic centroacinar cells and interlobular duct cells, hepatocyte bile canaliculi and testicular Leydig cells were densely stained with SNA. Thus, the monoclonal antibody recognizes two common membrane glycoproteins containing sialic acids in the pancreas, liver, testis and adrenal cortex.
authors.affiliation: Department of Anatomy, Kitasato University School of Medicine, Kanagawa, Japan.
authors.forename: Y
authors.initials: Y
authors.lastname: Kameda
authors.forename: C
authors.initials: C
authors.lastname: Hirota
authors.forename: R
authors.initials: R
authors.lastname: Miyauchi
mesh_terms: D000302:Adrenal Cortex / Q000166:cytology* / Q000276:immunology*; D000818:Animals; D000911:Antibodies, Monoclonal / Q000032:analysis / Q000276:immunology*; D001648:Bile Canaliculi / Q000737:chemistry / Q000166:cytology* / Q000648:ultrastructure; D004076:Digoxigenin; D004591:Electrophoresis, Polyacrylamide Gel; D006168:Guinea Pigs; D015151:Immunoblotting; D007150:Immunohistochemistry; D037102:Lectins; D007985:Leydig Cells / Q000737:chemistry / Q000166:cytology* / Q000648:ultrastructure; D008297:Male; D008562:Membrane Glycoproteins / Q000032:analysis; D051379:Mice; D008807:Mice, Inbred BALB C; D008854:Microscopy, Electron; D008871:Microvilli / Q000737:chemistry / Q000648:ultrastructure; D009439:Neuraminidase / Q000494:pharmacology; D015388:Organelles / Q000737:chemistry / Q000648:ultrastructure; D010179:Pancreas / Q000737:chemistry / Q000166:cytology* / Q000648:ultrastructure; D037121:Plant Lectins; D054788:Ribosome Inactivating Proteins
chemical_list: D000911:Antibodies, Monoclonal; D037102:Lectins; D008562:Membrane Glycoproteins; D037121:Plant Lectins; C050600:Sambucus nigra lectins; D009439:Neuraminidase; D054788:Ribosome Inactivating Proteins; D004076:Digoxigenin