n-Butyrate reduces the expression of β-galactoside α2,6-sialyltransferase in Hep G2 cells

Siddhartha Shah, Michael P Lance, Terry J. Smith, Charles S. Berenson, Stefan A. Cohen, Peter J. Horvath, Joseph T Y Lau, Heinz Baumann

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Abstract

n-Butyrate, a short chain fatty acid that is produced by colonic bacterial fermentation, is detectable in portal blood and induces differentiation in various human neoplastic cell lines. Earlier reports indicated ∼20-fold induction in vitro by n-butyrate of the sialyltransferase that catalyzes terminal glycosylation of GMS ganglioside in HeLa and colon cancer cells. We previously isolated a 1.3-kilobase cDNA for a human β-galactoside α2,6-sialyltransferase, for which N-linked glycoproteins are the acceptors. We report here that treatment of Hep G2 cells with 5 mM n-butyrate for 24 h reduced β-galactoside α2,6-sialyltransferase mRNA levels by ∼90%. Reductions in mRNA level were followed by ∼75 and ∼90% reductions, respectively, in specific β-galactoside α2,6-sialyltransferase enzyme activity after treatment for 24 and 36 h with 5 mM n-butyrate. However, in contrast with earlier reports of enhanced ganglioside synthesis in response to n-butyrate treatment, incubation of Hep G2 cells with n-butyrate did not alter the ganglioside pattern as assessed by thin layer chromatography of lipids extracted from treated cells. Nuclear run-on reactions indicated that the rate of transcription of β-galactoside, α2,6-sialyltransferase was not altered by treatment with 5 mM n-butyrate for 24 h, but the effects of this treatment on cytoplasmic levels of β-galactoside α2,6-sialyltransferase mRNA were largely negated by co-treatment with actinomycin D or cycloheximide. Therefore, our results show that n-butyrate reduces expression of mature β-galactoside α2,6-sialyltransferase mRNA by post-transcriptional mechanisms.

Original languageEnglish (US)
Pages (from-to)10652-10658
Number of pages7
JournalJournal of Biological Chemistry
Volume267
Issue number15
StatePublished - May 25 1992
Externally publishedYes

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Sialyltransferases
Galactosides
Butyrates
Hep G2 Cells
Gangliosides
Messenger RNA
Cells
Glycosylation
Thin layer chromatography
Volatile Fatty Acids
Enzyme activity
Dactinomycin
Transcription
Cycloheximide
Thin Layer Chromatography
Colonic Neoplasms
Fermentation
Glycoproteins
Blood
Complementary DNA

ASJC Scopus subject areas

  • Biochemistry

Cite this

Shah, S., Lance, M. P., Smith, T. J., Berenson, C. S., Cohen, S. A., Horvath, P. J., ... Baumann, H. (1992). n-Butyrate reduces the expression of β-galactoside α2,6-sialyltransferase in Hep G2 cells. Journal of Biological Chemistry, 267(15), 10652-10658.

n-Butyrate reduces the expression of β-galactoside α2,6-sialyltransferase in Hep G2 cells. / Shah, Siddhartha; Lance, Michael P; Smith, Terry J.; Berenson, Charles S.; Cohen, Stefan A.; Horvath, Peter J.; Lau, Joseph T Y; Baumann, Heinz.

In: Journal of Biological Chemistry, Vol. 267, No. 15, 25.05.1992, p. 10652-10658.

Research output: Contribution to journalArticle

Shah, S, Lance, MP, Smith, TJ, Berenson, CS, Cohen, SA, Horvath, PJ, Lau, JTY & Baumann, H 1992, 'n-Butyrate reduces the expression of β-galactoside α2,6-sialyltransferase in Hep G2 cells', Journal of Biological Chemistry, vol. 267, no. 15, pp. 10652-10658.
Shah S, Lance MP, Smith TJ, Berenson CS, Cohen SA, Horvath PJ et al. n-Butyrate reduces the expression of β-galactoside α2,6-sialyltransferase in Hep G2 cells. Journal of Biological Chemistry. 1992 May 25;267(15):10652-10658.
Shah, Siddhartha ; Lance, Michael P ; Smith, Terry J. ; Berenson, Charles S. ; Cohen, Stefan A. ; Horvath, Peter J. ; Lau, Joseph T Y ; Baumann, Heinz. / n-Butyrate reduces the expression of β-galactoside α2,6-sialyltransferase in Hep G2 cells. In: Journal of Biological Chemistry. 1992 ; Vol. 267, No. 15. pp. 10652-10658.
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abstract = "n-Butyrate, a short chain fatty acid that is produced by colonic bacterial fermentation, is detectable in portal blood and induces differentiation in various human neoplastic cell lines. Earlier reports indicated ∼20-fold induction in vitro by n-butyrate of the sialyltransferase that catalyzes terminal glycosylation of GMS ganglioside in HeLa and colon cancer cells. We previously isolated a 1.3-kilobase cDNA for a human β-galactoside α2,6-sialyltransferase, for which N-linked glycoproteins are the acceptors. We report here that treatment of Hep G2 cells with 5 mM n-butyrate for 24 h reduced β-galactoside α2,6-sialyltransferase mRNA levels by ∼90{\%}. Reductions in mRNA level were followed by ∼75 and ∼90{\%} reductions, respectively, in specific β-galactoside α2,6-sialyltransferase enzyme activity after treatment for 24 and 36 h with 5 mM n-butyrate. However, in contrast with earlier reports of enhanced ganglioside synthesis in response to n-butyrate treatment, incubation of Hep G2 cells with n-butyrate did not alter the ganglioside pattern as assessed by thin layer chromatography of lipids extracted from treated cells. Nuclear run-on reactions indicated that the rate of transcription of β-galactoside, α2,6-sialyltransferase was not altered by treatment with 5 mM n-butyrate for 24 h, but the effects of this treatment on cytoplasmic levels of β-galactoside α2,6-sialyltransferase mRNA were largely negated by co-treatment with actinomycin D or cycloheximide. Therefore, our results show that n-butyrate reduces expression of mature β-galactoside α2,6-sialyltransferase mRNA by post-transcriptional mechanisms.",
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AU - Lau, Joseph T Y

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