Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
1997-4-1
pubmed:abstractText
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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Brefeldin A, http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Cyclopentanes, http://linkedlifedata.com/resource/pubmed/chemical/G protein, vesicular stomatitis..., http://linkedlifedata.com/resource/pubmed/chemical/Glycoproteins, http://linkedlifedata.com/resource/pubmed/chemical/Heat-Shock Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Mannosidases, http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins, http://linkedlifedata.com/resource/pubmed/chemical/Molecular Chaperones, http://linkedlifedata.com/resource/pubmed/chemical/Nordihydroguaiaretic Acid, http://linkedlifedata.com/resource/pubmed/chemical/Viral Envelope Proteins, http://linkedlifedata.com/resource/pubmed/chemical/mannosyl-oligosaccharide 1,3 -..., http://linkedlifedata.com/resource/pubmed/chemical/molecular chaperone GRP78
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0021-924X
pubmed:author
pubmed:issnType
Print
pubmed:volume
119
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
863-9
pubmed:dateRevised
2007-12-19
pubmed:meshHeading
pubmed-meshheading:8797085-Animals, pubmed-meshheading:8797085-Biological Transport, pubmed-meshheading:8797085-Brefeldin A, pubmed-meshheading:8797085-Carrier Proteins, pubmed-meshheading:8797085-Cell Line, pubmed-meshheading:8797085-Cell Membrane, pubmed-meshheading:8797085-Cricetinae, pubmed-meshheading:8797085-Cyclopentanes, pubmed-meshheading:8797085-Endoplasmic Reticulum, pubmed-meshheading:8797085-Glycoproteins, pubmed-meshheading:8797085-Golgi Apparatus, pubmed-meshheading:8797085-Heat-Shock Proteins, pubmed-meshheading:8797085-Mannosidases, pubmed-meshheading:8797085-Membrane Glycoproteins, pubmed-meshheading:8797085-Microtubules, pubmed-meshheading:8797085-Molecular Chaperones, pubmed-meshheading:8797085-Nordihydroguaiaretic Acid, pubmed-meshheading:8797085-Vesicular stomatitis Indiana virus, pubmed-meshheading:8797085-Viral Envelope Proteins
pubmed:year
1996
pubmed:articleTitle
Inhibition of vesicle-mediated protein transport by nordihydroguaiaretic acid.
pubmed:affiliation
School of Life Science, Tokyo University of Pharmacy and Life Science.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't