Involvement of a highly polyvalent Glycan in the cell-binding of the aggregation factor from the marine sponge Microciona prolifera
✍ Scribed by Gradimir N. Misevic; Max M. Burger
- Publisher
- John Wiley and Sons
- Year
- 1990
- Tongue
- English
- Weight
- 606 KB
- Volume
- 43
- Category
- Article
- ISSN
- 0730-2312
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✦ Synopsis
A proteoglycan-like aggregation factor from the marine sponge Microciona prolqera (MAF) mediates cell-cell recognition via a cell-binding and a self-association domain. After repetitive and prolonged treatment of MAF with g1ycopeptide-Nglycosidase (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 M, = 6
x 1 O3 (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.