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Surface Glycosyltransferase Activities During Development of Neuronal Cell Cultures
Author(s) -
Matsui Yoshiki,
Lombard Dominique,
Massarelli Raphaël,
Mandel Paul,
Dreyfus Henri
Publication year - 1986
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1986.tb12937.x
Subject(s) - fucosylation , fucosyltransferase , synaptogenesis , glycoconjugate , fucose , glycolipid , glycoprotein , biochemistry , glycosyltransferase , microbiology and biotechnology , biology , chemistry , enzyme
Neurons in culture obtained from dissociated cerebral hemispheres of 8‐day‐old chick embryos showed measurable activities of galactosyl‐, fucosyl‐, and sialyl‐transferases at the external surface of their plasma membrane. Important changes in these activities were observed during cell proliferation and maturation, in particular the surface fucosyltransferase activity, and/or the amount of intraceilular fucosylated acceptors increased during synaptogenesis, between 3 and 5 days in culture (d.i.c.). A sodium dodecyl sulfate radioelectrophoretic analysis of the fucosylated neuronal acceptors labelled with [ 14 C]fucose showed, during synaptogenesis, the high labelling of two protein bands of 116 and 50 × 10 3 daltons. The fucosylation of glycoconjugates occurred preferentially, in neurons, upon glycoproteins whereas in glial cell cultures glycolipids were more fucosylated. The reasons for such a difference are not yet understood but the results suggest that the surface fucosyltransferase activity and fucosylated proteins in particular may play a role during the synaptogenesis of neurons in culture.