caa a22 4500 397557701 CHVBK 20180308164807.0 cr unu---uuuuu 161202e199605 xx s 000 0 eng 10.1093/oxfordjournals.jbchem.a021323 doi (NATIONALLICENCE)oxford-10.1093/oxfordjournals.jbchem.a021323 Inhibition of Vesicle-Mediated Protein Transport by Nordihydroguaiaretic Acid [Elektronische Daten] [Mitsuo Tagaya, Nobuhiro Henomatsu, Tamotsu Yoshimori, Akitsugu Yamamoto, Yutaka Tashiro, Shoji Mizushima] Nordihydroguaiaretic acid (NDGA) blocks intra-Golgi protein transport in a cell-free system and prolactin secretion from GH3 cells [Tagaya, M., Henomatsu, N., Yoshimori, T., Yamamoto, A., Tashiro, Y., and Fukui, T. (1993) FEBS Lett 324, 201-204]. To determine which intracellular secretory pathway(s) is inhibited by NDGA, we investigated its effect on the transport of the vesicular stomatitis virus-encoded glycoprotein in BHK-21 cells. NDGA blocked protein transport from the endoplasmic reticulum to the Golgi apparatus, and from the trans-Golgi network to the plasma membrane. In addition, it retarded the brefeldin A-induced retrograde transport of mannosidase II to the endoplasmic reticulum. Although NDGA had an inhibitory effect on protein synthesis, it induced the expression of BiP, a chaperone located in the endoplasmic reticulum. The induction of BiP may be a consequence of the inhibition of protein transport by NDGA. © by the Journal of Biochemistry Regular Papers nationallicence brefeldin A nationallicence nordihydroguaiaretic acid nationallicence protein transport nationallicence secretion nationallicence vesicular stomatitis virus nationallicence Tagaya Mitsuo School of Life Science, Tokyo University of Pharmacy and Life Science 1432-1 Horinouchi, Hachioji, Tokyo 1920S aut Henomatsu Nobuhiro Department of Physiology, Kansai Medical University Moriguchi, Osaka 570 aut Yoshimori Tamotsu Department of Physiology, Kansai Medical University Moriguchi, Osaka 570 aut Yamamoto Akitsugu Department of Physiology, Kansai Medical University Moriguchi, Osaka 570 aut Tashiro Yutaka Department of Physiology, Kansai Medical University Moriguchi, Osaka 570 aut Mizushima Shoji School of Life Science, Tokyo University of Pharmacy and Life Science 1432-1 Horinouchi, Hachioji, Tokyo 1920S aut The Journal of Biochemistry Oxford University Press 119/5(1996-05), 863-869 0021-924X 119:5<863 1996 119 jbchem https://doi.org/10.1093/oxfordjournals.jbchem.a021323 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1093/oxfordjournals.jbchem.a021323 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Tagaya Mitsuo School of Life Science, Tokyo University of Pharmacy and Life Science 1432-1 Horinouchi, Hachioji, Tokyo 1920S aut NATIONALLICENCE 700 1- Henomatsu Nobuhiro Department of Physiology, Kansai Medical University Moriguchi, Osaka 570 aut NATIONALLICENCE 700 1- Yoshimori Tamotsu Department of Physiology, Kansai Medical University Moriguchi, Osaka 570 aut NATIONALLICENCE 700 1- Yamamoto Akitsugu Department of Physiology, Kansai Medical University Moriguchi, Osaka 570 aut NATIONALLICENCE 700 1- Tashiro Yutaka Department of Physiology, Kansai Medical University Moriguchi, Osaka 570 aut NATIONALLICENCE 700 1- Mizushima Shoji School of Life Science, Tokyo University of Pharmacy and Life Science 1432-1 Horinouchi, Hachioji, Tokyo 1920S aut NATIONALLICENCE 773 0- The Journal of Biochemistry Oxford University Press 119/5(1996-05), 863-869 0021-924X 119:5<863 1996 119 jbchem Metadata rights reserved CC BY-NC-4.0 http://creativecommons.org/licenses/by-nc/4.0 nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-oxford