|ZFIN ID: ZDB-PUB-080227-20|
Molecular evolution and expression of zebrafish St8SiaIII, an alpha-2,8-sialyltransferase involved in myotome development
Bentrop, J., Marx, M., Schattschneider, S., Rivera-Milla, E., and Bastmeyer, M.
|Source:||Developmental dynamics : an official publication of the American Association of Anatomists 237(3): 808-818 (Journal)|
|Registered Authors:||Bastmeyer, Martin, Bentrop, Joachim, Marx, Monika, Rivera-Milla, Eric|
|Keywords:||zebrafish, sialic acid, polysialic acid, sialyltransferase, myotome development, somitogenesis, morpholino, in situ hybridization, muscle development, evolution|
|PubMed:||18265011 Full text @ Dev. Dyn.|
Bentrop, J., Marx, M., Schattschneider, S., Rivera-Milla, E., and Bastmeyer, M. (2008) Molecular evolution and expression of zebrafish St8SiaIII, an alpha-2,8-sialyltransferase involved in myotome development. Developmental dynamics : an official publication of the American Association of Anatomists. 237(3):808-818.
ABSTRACTEnzymes of the St8Sia family, a subgroup of the glycosyltransferases, mediate the transfer of sialic acid to glycoproteins or glycolipids. Here, we describe the cloning of the zebrafish St8SiaIII gene and study its developmental activity. A conserved synteny relationship among vertebrate chromosome regions containing St8SiaIII loci underscores an ancient duplication of this gene in the teleost fish lineage and a specific secondary loss of one paralog in the zebrafish. The single zebrafish St8SiaIII enzyme, which is expected to function as an oligosialyltransferase, lacks maternal activity, is weakly expressed during nervous system development, and shows a highly dynamic expression pattern in somites and somite-derived structures. Morpholino knock-down of St8SiaIII leads to anomalous somite morphologies, including defects in segment boundary formation and myotendious-junction integrity. These phenotypes hint for a basic activity of zebrafish St8SiaIII during segmentation and somite formation, providing novel evidence for a non-neuronal function of sialyltransferases during vertebrate development.