Effects of subperineurial injections of very-long-chain and medium-chain fatty acids into rat sciatic nerve

Sacktor, Ned; Griffin, John W.; Moser, Ann B.; Moser, Hugo W.

doi:10.1007/bf03028037

Cited by 2 publications

(1 citation statement)

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“…2-Hydroxy tetracosanoic acid, also known as cerebronic acid, is abundant in the brain [42]. It is worth mentioning that subperineurial injections of very long-chain fatty acids into rat sciatic nerves caused demyelination [43]. If this were the case, there is an intriguing possibility that free fatty acids released from the LOS of infectious agents could also have pathogenic effects.…”

Section: Discussionmentioning

confidence: 99%

Chemical validation of molecular mimicry: interaction of cholera toxin with Campylobacter lipooligosaccharides

et al. 2007

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It is generally believed that molecular mimicry between bacterial lipooligosaccharide (LOS) and nerve glycolipids may play an important pathogenic role in immune-mediated peripheral neuropathy. One of the putative infectious agents is Campylobacter jejuni (C. jejuni). To elucidate the structural basis for the molecular mimicry, we investigated the structure of the lipooligosaccharide (LOS) fraction of C. jejuni, strain HS19, and found that it includes at least two components, characterized as fast-and slow-moving bands (LF and LS) by thin-layer chromatography as revealed by cholera toxin B subunit (Ctxb) overlay. Structural analysis of the oligosaccharide portion of LS established that it had the following structure: Gal-GalNAc-(NeuAc)Gal-Hep-(Glc;PO 3 H)Hep-Kdo. The GM1-like epitope was validated by a terminal tetrasaccharide unit within this structure. On the other hand, analysis of LF revealed an entirely different structure: 1, 4′-bisphosphoryl glucosamine disaccharide N, N'-acylated by 3-(2-hydroxytetracosanoyloxy)octadecanoic acid at 2-and 2′-positions, which is consistent with that of lipid A. No GM1-like epitope was observed in LF. Both LS and LF interacted with Ctxb as demonstrated by TLC-overlay and sucrose density gradient centrifugation. Surprisingly, LF does not have the basic GM1 structure for interacting with Ctxb. Instead, the affinity of LF to Ctxb required that one or both of the phosphate groups be present in the glucosamine disaccharide residue because after alkaline phosphatase treatment the dephosphorylated LF was unable to bind to Ctxb. We conclude that LS is likely the component contributing to GM1-mimicry in autoimmune peripheral neuropathy and that the role of LF is not clear but may be associated with the initial activation of autoreactive T cells.

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Section: Discussionmentioning

confidence: 99%