Identification of glycolipid binding sites for soybean agglutinin and differences in the surface glycolipids of cultured adrenergic and cholinergic sympathetic neurons

Zurn, A.D.

Developmental Biology 94(2): 483-498

1982


ISSN/ISBN: 0012-1606
PMID: 6185381
DOI: 10.1016/0012-1606(82)90365-7
Accession: 005613324

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Abstract
Cultured adrenergic neurons from newborn rat superior cervical ganglia bind the lectin soybean agglutinin (SBA) at a 5-fold higher density than the same neurons which were induced to become cholinergic (Schwab et Landis, 1981). In these experiments, the binding sites for this lectin on the surfaces of living neurons were identified by labeling the surfaces with the galactose oxidase-[3H]sodium borohydride reduction technique, with and without prior incubation with the lectin. SBA binds to and inhibits the labeling of 2 neutral glycolipids, a glycolipid comigrating with globoside on TLC and an unidentified glycolipid. When neuronal proteins are extracted and separated by polyacrylamide gel electrophoresis in sodium dodecyl sulfate, SBA shows only very faint labeling of this fraction. The SBA binding sites on these neurons appear to be 2 neutral glycolipids. The 2 neutral glycolipids detected by SBA are present in smaller amounts or are less accessible on the cholinergic than on the adrenergic neurons as measured by surface labeling. In addition to the difference in neutral glycolipids, external labeling revealed quantitative differences in the major gangliosides of the 2 types of cultured neurons. By using pure cultures of sympathetic neurons which can be induced to become either adrenergic or cholinergic, specific glycolipid profiles were correlated with the 2 neurotransmitter phenotypes.