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pubmed:abstractText |
Plasma membrane glycoproteins from Dictyostelium discoideum amoebae at three stages of early development were digested with Pronase and endoglycosidase H and fractionated by gel filtration. This gave three classes of glycans (polysaccharides, endoglycosidase H-resistant glycopeptides, and endoglycosidase H-released oligosaccharides), which were tested for their ability to block agglutination of amoebae from vegetative, aggregation (8-hr), and late-aggregation (13-hr) stages of development. The endoglycosidase H-resistant glycopeptides from 8-hr cells inhibited agglutination of disaggregated 8-hr cells but not vegetative or 13-hr cells. The 8-hr polysaccharide and endo H-sensitive oligosaccharides did not inhibit. The glycopeptides from 8-hr cells were resolved into five species by electrophoresis in borate-containing buffer. Two of these had agglutination-inhibiting activity, and three did not. None of the glycan fractions from vegetative or 13-hr cells inhibited agglutination of vegetative, 8-, or 13-hr cells. These data implicate specific cell surface glycans in aggregation-stage intercellular cohesion and suggest that both these glycans and receptors for them are developmentally regulated.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.
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