title: Structural integrity of the Golgi stack is essential for normal secretory functions of rat parotid acinar cells: effects of brefeldin A and okadaic acid.
abstract: We examined the effects of specific inhibitors, brefeldin A (BFA) and okadaic acid (OA), on the ultrastructural organization of the Golgi apparatus and distributions of amylase, Golgi-associated proteins, and cathepsin D in the rat parotid acinar cells. BFA induced a rapid regression of the Golgi stack into rudimentary Golgi clusters composed of tubulovesicules, in parallel with a redistribution of the Golgi-resident proteins and a coat protein (beta-COP) into the region of the rough endoplasmic reticulum (rER) or cytosol. The rapid disruption of the Golgi stack could also be induced by the effect of OA. However, redistribution of the Golgi proteins in rER or cytosol could not be observed and beta-COP was not dispersed but was retained on the rudimentary Golgi apparatus. These findings suggested that the mechanism of OA in inducing degeneration of the Golgi stack was markedly different from that of BFA. In addition, missorting of amylase, a Golgi protein, and cathepsin D into incorrect transport pathways is apparent in the course of the disruption of the Golgi stack by OA. These Golgi-disrupting effects are reversible and the reconstruction of the stacked structure of the Golgi apparatus started immediately after the removal of inhibitors. In the recovery processes, missorting was also observed until the integrated structure of the Golgi apparatus was completely reconstructed. This suggested that the integrated structure of the Golgi apparatus was quite necessary for the occurrence of normal secretory events, including proper sorting of molecules.
authors.affiliation: Department of Anatomy, Kitasato University School of Medicine, Sagamihara, Kanagawa, Japan. tamaki@kitasato-u.ac.jp
authors.forename: Hideaki
authors.initials: H
authors.lastname: Tamaki
authors.forename: Shohei
authors.initials: S
authors.lastname: Yamashina
mesh_terms: D000681:Amylases / Q000378:metabolism; D000818:Animals; D020126:Brefeldin A / Q000494:pharmacology*; D002402:Cathepsin D / Q000378:metabolism*; D020756:Coatomer Protein / Q000378:metabolism; D004268:DNA-Binding Proteins / Q000378:metabolism; D050981:Erythroid-Specific DNA-Binding Factors; D005629:Frozen Sections; D006056:Golgi Apparatus / Q000187:drug effects* / Q000378:metabolism / Q000648:ultrastructure; D007150:Immunohistochemistry; D066298:In Vitro Techniques; D008297:Male; D008361:Mannosidases / Q000378:metabolism; D018613:Microscopy, Confocal; D008854:Microscopy, Electron; D019319:Okadaic Acid / Q000494:pharmacology*; D010306:Parotid Gland / Q000166:cytology* / Q000378:metabolism / Q000648:ultrastructure; D051381:Rats; D017208:Rats, Wistar; D014157:Transcription Factors / Q000378:metabolism
chemical_list: D020756:Coatomer Protein; D004268:DNA-Binding Proteins; D050981:Erythroid-Specific DNA-Binding Factors; D014157:Transcription Factors; D019319:Okadaic Acid; D020126:Brefeldin A; D000681:Amylases; D008361:Mannosidases; C038829:mannosyl-oligosaccharide 1,3 - 1,6-alpha-mannosidase; D002402:Cathepsin D