title: Inhibition of vesicle-mediated protein transport by nordihydroguaiaretic acid.
abstract: 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.
authors.affiliation: School of Life Science, Tokyo University of Pharmacy and Life Science.
authors.forename: M
authors.initials: M
authors.lastname: Tagaya
authors.forename: N
authors.initials: N
authors.lastname: Henomatsu
authors.forename: T
authors.initials: T
authors.lastname: Yoshimori
authors.forename: A
authors.initials: A
authors.lastname: Yamamoto
authors.forename: Y
authors.initials: Y
authors.lastname: Tashiro
authors.forename: S
authors.initials: S
authors.lastname: Mizushima
mesh_terms: D000818:Animals; D001692:Biological Transport / Q000187:drug effects; D020126:Brefeldin A; D002352:Carrier Proteins / Q000096:biosynthesis; D002460:Cell Line; D002462:Cell Membrane / Q000187:drug effects / Q000378:metabolism*; D006224:Cricetinae; D003517:Cyclopentanes / Q000494:pharmacology; D004721:Endoplasmic Reticulum / Q000187:drug effects / Q000378:metabolism* / Q000648:ultrastructure; D000091342:Endoplasmic Reticulum Chaperone BiP; D006023:Glycoproteins / Q000378:metabolism; D006056:Golgi Apparatus / Q000187:drug effects / Q000378:metabolism* / Q000648:ultrastructure; D006360:Heat-Shock Proteins; D008361:Mannosidases / Q000378:metabolism*; D009637:Masoprocol / Q000494:pharmacology*; D008562:Membrane Glycoproteins; D008870:Microtubules / Q000187:drug effects / Q000378:metabolism / Q000648:ultrastructure; D018832:Molecular Chaperones / Q000096:biosynthesis; D014721:Vesicular stomatitis Indiana virus / Q000502:physiology; D014759:Viral Envelope Proteins / Q000378:metabolism*
chemical_list: D002352:Carrier Proteins; D003517:Cyclopentanes; D000091342:Endoplasmic Reticulum Chaperone BiP; C028391:G protein, vesicular stomatitis virus; D006023:Glycoproteins; D006360:Heat-Shock Proteins; D008562:Membrane Glycoproteins; D018832:Molecular Chaperones; D014759:Viral Envelope Proteins; D020126:Brefeldin A; D009637:Masoprocol; D008361:Mannosidases; C038829:mannosyl-oligosaccharide 1,3 - 1,6-alpha-mannosidase