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Synthetic heparan sulfate dodecasaccharides reveal single sulfation site interconverts CXCL8 and CXCL12 chemokine biology.

ABSTRACT: The multigram-scale synthesis of a sulfation-site programmed heparin-like dodecasaccharide is described. Evaluation alongside dodecasaccharides lacking this single glucosamine O6-sulfation, or having per-O6-sulfation, shows that site-specific modification of the terminal glucosamine dramatically interconverts regulation of in vitro and in vivo biology mediated by the two important chemokines, CXCL12 (SDF1?) or CXCL8 (IL-8).

SUBMITTER: Jayson GC

PROVIDER: S-EPMC4608306 | biostudies-literature | 2015 Sep

REPOSITORIES: biostudies-literature

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Synthetic heparan sulfate dodecasaccharides reveal single sulfation site interconverts CXCL8 and CXCL12 chemokine biology.

Jayson Gordon C GC Hansen Steen U SU Miller Gavin J GJ Cole Claire L CL Rushton Graham G Avizienyte Egle E Gardiner John M JM

Chemical communications (Cambridge, England) 20150803 72

The multigram-scale synthesis of a sulfation-site programmed heparin-like dodecasaccharide is described. Evaluation alongside dodecasaccharides lacking this single glucosamine O6-sulfation, or having per-O6-sulfation, shows that site-specific modification of the terminal glucosamine dramatically interconverts regulation of in vitro and in vivo biology mediated by the two important chemokines, CXCL12 (SDF1α) or CXCL8 (IL-8). ...[more]

PMID: 26234943

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