Glycoconjugate Journal

, Volume 20, Issue 7, pp 493–500

Identification of seven new α2,3-sialyltransferase III, ST3Gal III, transcripts from human foetal brain


DOI: 10.1023/B:GLYC.0000038295.87747.0b

Cite this article as:
Grahn, A., Barkhordar, G.S. & Larson, G. Glycoconj J (2003) 20: 493. doi:10.1023/B:GLYC.0000038295.87747.0b


We have recently cloned and sequenced 19 human ST3Gal III gene isotranscripts from peripheral blood leukocytes and identified very complex patterns of isotranscripts of this gene in neuronal tissues. We have now cloned and sequenced additionally seven new isotranscripts from foetal brain. These novel isotranscripts showed losses of complete exons along the whole length of the coding sequence. None of the new isotranscripts coded for proteins with the two (L- and S-) sialylmotifs intact. One of the isotranscripts belonged to the isoform ST3Gal III-B, five to the ST3Gal III-C isoform and one to ST3Gal III-D isoform of isotranscripts, which lacks exon 3, exons 3 and 4 and exon 4 respectively. Two of the C series isotranscripts, ST3Gal III C4 and C11 had both lost exons 12 and 13 containing the S-motif but had otherwise the L- and the VS-motifs intact. Three isotranscripts, ST3Gal III C5, C12 and D5, were similar in the 3′-end coding for an identical amino acid sequence unrelated to the original enzyme. Isotranscripts ST3Gal III C9 and B10 were distinctly different from all other forms identified so far. The splice variants reported here are unlikely to express enzymatic activities but may other biological functions. Published in 2004.

sialyltransferase ST3Gal III transcripts alternative splicing capillary electrophoresis 

Copyright information

© Kluwer Academic Publishers 2004

Authors and Affiliations

  • Ammi Grahn
    • 1
  • Giti Shah Barkhordar
    • 1
  • Göran Larson
    • 1
  1. 1.Institute of Laboratory Medicine, Department of Clinical Chemistry and Transfusion MedicineSahlgrenska University HospitalGöteborgSweden

Personalised recommendations