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Glycobiology Advance Access published online on October 26, 2005
Glycobiology, doi:10.1093/glycob/cwj051
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© The Author 2005. Published by Oxford University Press. All rights reserved. For permissions, please e-mail: journals.permissions@oxfordjournals.org.
Received April 8, 2005
Revised September 30, 2005
Accepted October 18, 2005

Article

Expression of the UDP-GalNAc:Polypeptide N-Acetylgalactosaminyltransferase Family is Spatially and Temporally Regulated During Drosophila Development

E Tian 1 and Kelly G. Ten Hagen 1*

1 Developmental Glycobiology Unit, NIDCR, National Institutes of Health Building 30, Room 426 30 Convent Drive, MSC 4370 Bethesda, MD 20892-4370

* To whom correspondence should be addressed.
Kelly G. Ten Hagen, E-mail: Kelly.Tenhagen{at}nih.gov


  Abstract

The UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase enzyme family is responsible for the first committed step in the synthesis of mucin-type O-glycans on protein substrates. Previous work from our group has demonstrated both sequence and functional conservation between members of this family in mammals and the fruit fly, Drosophila melanogaster. One member of this family in Drosophila has been shown to be essential for viability and development. In an effort to understand the developmental stages and processes in which O-glycosylation is involved, we have determined the expression pattern of each functional family member as well as putative isoforms during Drosophila development. Our studies indicate that isoforms are expressed in discrete spatial and temporal fashions during development, with some isoforms being found uniquely in restricted areas of the developing embryo (brain, trachea, pharynx, esophagus, proventriculus, amnioserosa) while others are found in multiple regions and overlap with the expression of other isoforms (salivary glands, posterior midgut, anterior midgut and the fore-/hindgut) during embryogenesis. Additionally, we examined expression patterns in imaginal discs from third instar larvae, which will become the adult structures. Most isoforms are also expressed in the imaginal discs, with some showing unique transcript localization and spatial regulatory control. Thus, this report provides insight into the specific regions during Drosophila development that may require O-linked glycosylation in vivo as well as which isoforms may act cooperatively in certain tissues and which may be uniquely responsible for glycosylation in others.

Keywords: O-glycosylation/pgant/Drosophila embryogenesis/in situ hybridization/development.
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