Involvement of a highly polyvalent glycan in the cell-binding of the aggregation factor from the marine sponge Microciona prolifera.
A proteoglycan-like aggregation factor from the marine sponge Microciona prolifera (MAF) mediates cell-cell recognition via a cell-binding and a self-association domain. After repetitive and prolonged treatment of MAF with glycopeptide-N-glycosidase (PNGase) the specific binding of MAF to homotypic cells was decreased by 72%. Polyacrylamide gel electrophoresis and gel filtration analysis of such PNGase digests showed that: 1) the enzyme released a single glycan type of Mr = 6 X 10(3) (G-6) from MAF, 2) 1 mole of MAF contains at least 830 moles of N-linked chains of G-6 glycan. The correlation between the loss of the binding activity of MAF and the extent of the release of the repetitive G-6 polysaccharide strongly suggests its involvement in MAF-cell association via highly polyvalent interactions.
Misevic
G N
GN
Friedrich Miescher-Institut, Basel, Switzerland.
Burger
M M
MM
D000581:Amidohydrolases / Q000378:metabolism; D000818:Animals; D015815:Cell Adhesion Molecules; D002449:Cell Aggregation / Q000187:drug effects; D002450:Cell Communication; D004492:Edetic Acid; D043524:Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase; D011134:Polysaccharides / Q000032:analysis / Q000378:metabolism*; D011161:Porifera / Q000378:metabolism*; D011506:Proteins / Q000032:analysis / Q000378:metabolism*
D015815:Cell Adhesion Molecules; D011134:Polysaccharides; D011506:Proteins; C013065:cell aggregation factors; D004492:Edetic Acid; D000581:Amidohydrolases; D043524:Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase