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PMID: 8310065 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.

Effect of brefeldin A on the structure of the Golgi apparatus and on the synthesis and secretion of proteins and polysaccharides in sycamore maple (Acer pseudoplatanus) suspension-cultured cells.

Plant physiology ·Vol. 101 ·No. 4 ·1993-04-00 ·Pages 1363-73

Driouich A, Zhang GF, Staehelin LA

Abstract

Brefeldin A (BFA), a specific inhibitor of Golgi-mediated secretion in animal cells, has been used to study the organization of the secretory pathway and the function of the Golgi apparatus in plant cells. To this end, we have employed a combination of electron microscopical, immunocytochemical, and biochemical techniques to investigate the effects of this drug on the architecture of the Golgi apparatus as well as on the secretion of proteins and complex cell wall polysaccharides in sycamore maple (Acer pseudoplatanus) suspension-cultured cells. We have used 2.5 and 7.5 micrograms/mL of BFA, which is comparable to the 1 to 10 micrograms/mL used in experiments with animal cells. Electron micrographs of high-pressure frozen and freeze-substituted cells show that although BFA causes swelling of the endoplasmic reticulum cisternae, unlike in animal cells, it does not induce the disassembly of sycamore maple Golgi stacks. Instead, BFA induces the formation of large clusters of Golgi stacks, an increase in the number of trans-like Golgi cisternae, and the accumulation in the cytoplasm of very dense vesicles that appear to be derived from trans Golgi cisternae. These vesicles contain large amounts of xyloglucan (XG), the major hemicellulosic cell wall polysaccharide, as shown by immunocytochemical labeling with anti-XG antibodies. All of these structural changes disappear within 120 min after removal of the drug. In vivo labeling experiments using [3H]leucine demonstrate that protein secretion into the culture medium, but not protein synthesis, is inhibited by approximately 80% in the presence of BFA. In contrast, the incorporation of [3H]fucose into N-linked glycoproteins, which occurs in trans-Golgi cisternae, appears to be affected to a greater extent than the incorporation of [3H]xylose, which has been localized to medial Golgi cisternae. BFA also affects secretion of complex polysaccharides as evidenced by the approximate 50% drop in incorporation of [3H]xylose and [3H]fucose into cell wall hemicelluloses. Taken together, these findings suggest that at concentrations of 2.5 to 7.5 mu g/mL BFA causes the following major changes in the secretory pathway of sycamore maple cells: (a) it inhibits the transport of secretory proteins to the cell surface by about 80% and of hemicelluloses by about 50%; (b) it changes the patterns of glycosylation of N-linked glycoproteins and hemicelluloses; (c) it reduces traffic between trans Golgi cisternae and secretory vesicles; (d) it produces a major block in the transport of XG-containing, dense secretory vesicles to the cell surface; and (e) it induces the formation of large aggregates of Golgi apparatus of plant and animal cels share many functional and structural characteristics, the plant Golgi apparatus possesses properties that make its response to BFA unique.

MeSH Terms
Brefeldin A Cell Wall/metabolism Cells, Cultured Cyclopentanes/pharmacology Fucose/metabolism Glycoproteins/metabolism Golgi Apparatus/drug effects,metabolism,ultrastructure Mannose/metabolism Plant Proteins/biosynthesis,metabolism Polysaccharides/biosynthesis,metabolism Trees/drug effects,metabolism,ultrastructure Xylose/metabolism
Chemicals
Cyclopentanes Glycoproteins Plant Proteins Polysaccharides Brefeldin A Fucose Xylose Mannose
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Driouich A
Department of Molecular, Cellular, and Developmental Biology, University of Colorado, Boulder 80309-0347.
Zhang G F
Staehelin L A
References (27)
27 references, click to expand
  1. Protein secretion in plant cells can occur via a default pathway.
    Plant Cell. 1990 Jan;2(1):51-9 PMID: 1967050
  2. Comparisons of Golgi structure and dynamics in plant and animal cells.
    J Electron Microsc Tech. 1991 Feb;17(2):179-99 PMID: 2013820
  3. Brefeldin A: insights into the control of membrane traffic and organelle structure.
    J Cell Biol. 1992 Mar;116(5):1071-80 PMID: 1740466
  4. Effects of brefeldin A on the synthesis and secretion of egg white proteins in primary cultured oviduct cells of laying Japanese quail (Coturnix coturnix japonica).
    Biochim Biophys Acta. 1989 Apr 25;991(1):36-43 PMID: 2713420
  5. Recruitment of coat proteins onto Golgi membranes in intact and permeabilized cells: effects of brefeldin A and G protein activators.
    Cell. 1992 Apr 3;69(1):129-38 PMID: 1555237
  6. Brefeldin A arrests the intracellular transport of a precursor of complement C3 before its conversion site in rat hepatocytes.
    FEBS Lett. 1987 Apr 6;214(1):135-8 PMID: 3569512
  7. Topography of glycosylation in the rough endoplasmic reticulum and Golgi apparatus.
    Annu Rev Biochem. 1987;56:63-87 PMID: 3304145
  8. Xylose-specific antibodies as markers of subcompartmentation of terminal glycosylation in the Golgi apparatus of sycamore cells.
    FEBS Lett. 1991 Dec 16;295(1-3):179-84 PMID: 1765151
  9. Kinetics of Golgi apparatus membrane flux following monensin treatment of embryogenic carrot cells.
    Eur J Cell Biol. 1983 Mar;30(1):25-32 PMID: 6852059
  10. Functional compartmentation of the Golgi apparatus of plant cells : immunocytochemical analysis of high-pressure frozen- and freeze-substituted sycamore maple suspension culture cells.
    Plant Physiol. 1992 Jul;99(3):1070-83 PMID: 16668973
  11. Brefeldin A causes a microtubule-mediated fusion of the trans-Golgi network and early endosomes.
    Cell. 1991 Nov 1;67(3):591-600 PMID: 1657400
  12. Biosynthetic protein transport and sorting by the endoplasmic reticulum and Golgi.
    Annu Rev Biochem. 1987;56:829-52 PMID: 3304148
  13. Assembly of asparagine-linked oligosaccharides.
    Annu Rev Biochem. 1985;54:631-64 PMID: 3896128
  14. Coated Vesicles Are Involved in the Transport of Storage Proteins during Seed Development in Pisum sativum L.
    Plant Physiol. 1989 Oct;91(2):674-8 PMID: 16667086
  15. Effects of Brefeldin A on the Golgi complex, endoplasmic reticulum and viral envelope glycoproteins in murine erythroleukemia cells.
    Eur J Cell Biol. 1991 Feb;54(1):38-54 PMID: 2032551
  16. Brefeldin A causes disassembly of the Golgi complex and accumulation of secretory proteins in the endoplasmic reticulum.
    J Biol Chem. 1988 Dec 5;263(34):18545-52 PMID: 3192548
  17. Role of microtubules in the organisation of the Golgi apparatus.
    Cell Motil Cytoskeleton. 1990;15(2):67-70 PMID: 2178782
  18. PtK1 cells contain a nondiffusible, dominant factor that makes the Golgi apparatus resistant to brefeldin A.
    J Cell Biol. 1991 Jun;113(5):1009-23 PMID: 1710224
  19. Macromolecular differentiation of Golgi stacks in root tips of Arabidopsis and Nicotiana seedlings as visualized in high pressure frozen and freeze-substituted samples.
    Protoplasma. 1990;157(1-3):75-91 PMID: 11537090
  20. A coat subunit of Golgi-derived non-clathrin-coated vesicles with homology to the clathrin-coated vesicle coat protein beta-adaptin.
    Nature. 1991 Jan 17;349(6306):215-20 PMID: 1898984
  21. Brefeldin A, a drug that blocks secretion, prevents the assembly of non-clathrin-coated buds on Golgi cisternae.
    Cell. 1991 Mar 22;64(6):1183-95 PMID: 2004424
  22. Rapid redistribution of Golgi proteins into the ER in cells treated with brefeldin A: evidence for membrane cycling from Golgi to ER.
    Cell. 1989 Mar 10;56(5):801-13 PMID: 2647301
  23. Brefeldin A redistributes resident and itinerant Golgi proteins to the endoplasmic reticulum.
    J Cell Biol. 1989 Jul;109(1):61-72 PMID: 2745557
  24. Brefeldin A's effects on endosomes, lysosomes, and the TGN suggest a general mechanism for regulating organelle structure and membrane traffic.
    Cell. 1991 Nov 1;67(3):601-16 PMID: 1682055
  25. Dissociation of a 110-kD peripheral membrane protein from the Golgi apparatus is an early event in brefeldin A action.
    J Cell Biol. 1990 Dec;111(6 Pt 1):2295-306 PMID: 2277061
  26. Microtubule-dependent retrograde transport of proteins into the ER in the presence of brefeldin A suggests an ER recycling pathway.
    Cell. 1990 Mar 9;60(5):821-36 PMID: 2178778
  27. The signal Peptide of a vacuolar protein is necessary and sufficient for the efficient secretion of a cytosolic protein.
    Plant Physiol. 1991 May;96(1):18-25 PMID: 16668149
Article Info
Journal
Plant physiology
Abbr.
Plant Physiol
ISSN
0032-0889
Published
1993-04-00
Pages
1363-73
Language
English
Region
United States
NLM ID
0401224
PMCID
PMC160661
Subset
IM
Grants
NIGMS NIH HHS · GM 18639 · United States
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