Activities of Five Different Sialyltransferases in Fish and Rat Brains

Bettina Freischütz, Megumi Saito, Hinrich Rahmann, Robert K. Yu

Research output: Contribution to journalArticlepeer-review

33 Scopus citations

Abstract

Abstract: To investigate the role of Sialyltransferases in the metabolism of brain gangliosides, we examined activities of five different Sialyltransferases (GM3‐, GD3‐, GT3‐, GD1a‐, and GT1a‐synthase) using total membrane preparations from cichlid fish and Sprague‐Dawley rat brains, and analyzed the relationship between the enzyme activities and the ganglloside compositions. The patterns of sialyltransferase activities in fish and rat brains differed from each other. In fish brain, the GM3‐synthase activity was lower than GD3‐synthase activity, whereas the opposite relationship was observed in rat brain. The GT3‐synthase reaction with fish brain membranes produced radiolabeled GM3, GD3, and a ganglioside that was identified as GT3 based on mobility on TLC using two different solvent systems. No GT3‐synthase activity was detected in rat brain. The GD1a‐and GT1a‐synthase activities in fish brain were higher than those in rat brain. Although GT1a was a single radiolabeled ganglioside in fish GT1a‐synthase reaction, this ganglioside could not be detected in rat brain. The ratios of GM3‐, GD3‐, GT3‐, GD1a‐, and GT1a‐synthase activities in fish and rat brain were 23:31:4:28:14 and 61:21:0:18:0, respectively. Ganglioside analysis showed that fish brain was enriched with c‐series gangliosides including GT3 and polysialo‐species, whereas a‐and b‐se‐ries gangliosides were major components in rat brain. These results suggest that the species‐specific expression of gangliosides in brain tissues may be regulated, at least in part, at the level of sialyltransferase activities.

Original languageEnglish (US)
Pages (from-to)1965-1973
Number of pages9
JournalJournal of Neurochemistry
Volume62
Issue number5
DOIs
StatePublished - May 1994
Externally publishedYes

Keywords

  • Brain
  • Fish
  • GT3
  • Gangliosides
  • Sialyltransferases
  • Species‐specificity

ASJC Scopus subject areas

  • Biochemistry
  • Cellular and Molecular Neuroscience

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