caa a22 4500 475774108 CHVBK 20180406123625.0 cr unu---uuuuu 170329e20001201xx s 000 0 eng 10.1007/s004180000216 doi (NATIONALLICENCE)springer-10.1007/s004180000216 Immunohistochemical evaluation of endomannosidase distribution in rat tissues: evidence for cell type-specific expression [Elektronische Daten] [Zhizhong Dong, Christian Zuber, Mary Jane Spiro, Robert G. Spiro, Jürgen Roth] Abstract.: Asparagine-linked oligosaccharides of glycoproteins are subject to a series of trimming reactions by glucosidases and mannosidases in the endoplasmic reticulum which result in the removal of all three glucose residues and several of the nine mannose residues. At present, endomannosidase represents the only processing enzyme which cleaves internally and provides an alternate deglucosylation pathway. However, in contrast to the endoplasmic reticulum residential proteins glucosidaseI and II, endomannosidase is primarily situated in the Golgi apparatus of rat liver hepatocytes and hepatocyte cell lines. We have performed a confocal immunohistochemical study to investigate endomannosidase in various rat tissues and used a monoclonal antibody against Golgi mannosidaseII as a marker for the Golgi apparatus. Although immunofluorescence for both endomannosidase and Golgi mannosidaseII was detectable in the epithelia of many tissues, renal proximal tubular cells, cortex and medulla of adrenal gland, gastric mucosa, and Leydig cells of testis were unreactive for endomannosidase. Furthermore, the endothelia in all studied tissues were unreactive for endomannosidase but positive for Golgi mannosidaseII. It is concluded that by immunohistochemistry endomannosidase exhibits a cell type-specific expression in rat tissues. Springer-Verlag, 2000 Endomannosidase Immunohistochemistry Endothelia Rat nationallicence Dong Zhizhong Division of Cell and Molecular Pathology, Department of Pathology, University of Zürich, CH-8091 Zürich, Switzerland aut Zuber Christian Division of Cell and Molecular Pathology, Department of Pathology, University of Zürich, CH-8091 Zürich, Switzerland aut Spiro Mary Jane Departments of Biological Chemistry and Medicine, Harvard Medical School, and the Joslin Diabetes Center, Boston, MA02215, USA aut Spiro Robert G. Departments of Biological Chemistry and Medicine, Harvard Medical School, and the Joslin Diabetes Center, Boston, MA02215, USA aut Roth Jürgen Division of Cell and Molecular Pathology, Department of Pathology, University of Zürich, CH-8091 Zürich, Switzerland aut https://doi.org/10.1007/s004180000216 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/s004180000216 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Dong Zhizhong Division of Cell and Molecular Pathology, Department of Pathology, University of Zürich, CH-8091 Zürich, Switzerland aut NATIONALLICENCE 700 1- Zuber Christian Division of Cell and Molecular Pathology, Department of Pathology, University of Zürich, CH-8091 Zürich, Switzerland aut NATIONALLICENCE 700 1- Spiro Mary Jane Departments of Biological Chemistry and Medicine, Harvard Medical School, and the Joslin Diabetes Center, Boston, MA02215, USA aut NATIONALLICENCE 700 1- Spiro Robert G. Departments of Biological Chemistry and Medicine, Harvard Medical School, and the Joslin Diabetes Center, Boston, MA02215, USA aut NATIONALLICENCE 700 1- Roth Jürgen Division of Cell and Molecular Pathology, Department of Pathology, University of Zürich, CH-8091 Zürich, Switzerland aut Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer