PMID: 2493652Mar 1, 1989Paper

Brefeldin A inhibits oligosaccharide processing of glycoproteins in mouse hypothyroid pituitary tissue at several subcellular sites

Proceedings of the Society for Experimental Biology and Medicine
V S PerkelJ A Magner

Abstract

We have studied the effects of brefeldin A (BFA) and monensin on the processing of the oligosaccharides of thyrotropin (TSH), free alpha-subunits, and cellular glycoproteins of mouse pituitary tissue to clarify the subcellular sites of action of BFA. BFA was previously shown to inhibit the translocation of glycoproteins from the rough endoplasmic reticulum to the Golgi apparatus but action at other sites was possible. Pituitaries from hypothyroid mice were incubated with [35S]methionine, [3H]mannose, [3H]galactose, [3H]fucose, N-[3H]acetylmannosamine, or [35S]sulfate for 2 hr in the absence or presence of 5 micrograms of BFA/ml or 2 microM monensin. TSH and free alpha-subunits were immunoprecipitated from tissue lysates and analyzed by sodium dodecyl sulfate-gel electrophoresis. The tryptic glycopeptides of TSH were separated using high-performance liquid chromatography. Total glycoproteins in cell lysates were precipitated using trichloroacetic acid. Labeled oligosaccharides were released from the tryptic glycopeptides of TSH and cellular glycoproteins by endoglycosidase H and they were analyzed by paper chromatography. Compared with control incubations, BFA caused the intracellular accumulation of glycoproteins having less th...Continue Reading

Citations

Jul 1, 1995·Journal of Industrial Microbiology·T G McCloudW B Lebherz
Nov 26, 1990·FEBS Letters·R E KneuselK D Klöppel
Jan 1, 1992·Thyroid : Official Journal of the American Thyroid Association·J MagnerF Wezeman
Aug 5, 2003·FASEB Journal : Official Publication of the Federation of American Societies for Experimental Biology·Giuseppe ProcinoGiovanna Valenti
Jun 11, 2002·The Journal of Organic Chemistry·Young-Ger SuhHyun-Ju Park

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