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Glycans of Myelin Proteins
KTH, School of Chemical Science and Engineering (CHE), Chemical Engineering and Technology.
2015 (English)In: Journal of Neuroscience Research, ISSN 0360-4012, E-ISSN 1097-4547, Vol. 93, no 1, 1-18 p.Article, review/survey (Refereed) Published
Abstract [en]

Human P0 is the main myelin glycoprotein of the peripheral nervous system. It can bind six different glycans, all linked to Asn(93), the unique glycosylation site. Other myelin glycoproteins, also with a single glycosylation site (PMP22 at Asn(36), MOG at Asn(31)), bind only one glycan. The MAG has 10 glycosylation sites; the glycoprotein OMgp has 11 glycosylation sites. Aside from P0, no comprehensive data are available on other myelin glycoproteins. Here we review and analyze all published data on the physicochemical structure of the glycans linked to P0, PMP22, MOG, and MAG. Most data concern bovine P0, whose glycan moieties have an MW ranging from 1,294.56 Da (GP3) to 2,279.94 Da (GP5). The pI of glycosylated P0 protein varies from pH 9.32 to 9.46. The most charged glycan is MS2 containing three sulfate groups and one glucuronic acid; whereas the least charged one is the BA2 residue. All glycans contain one fucose and one galactose. The most mannose rich are the glycans MS2 and GP4, each of them has four mannoses; OPPE1 contains five N-acetylglucosamines and one sulfated glucuronic acid; GP4 contains one sialic acid. Furthermore, human P0 variants causing both gain and loss of glycosylation have been described and cause peripheral neuropathies with variable clinical severity. In particular, the substitution (TM)-M-95 is a very common in Europe and is associated with a late-onset axonal neuropathy. Although peripheral myelin is made up largely of glycoproteins, mutations altering glycosylation have been described only in P0. This attractive avenue of research requires further study.

Place, publisher, year, edition, pages
2015. Vol. 93, no 1, 1-18 p.
Keyword [en]
P0, PMP22, MAG, MOG, glycans, CNS, PNS, CMT, glycosylation
National Category
URN: urn:nbn:se:kth:diva-158799DOI: 10.1002/jnr.23462ISI: 000345307200001ScopusID: 2-s2.0-84923699562OAI: diva2:785980

QC 20150204

Available from: 2015-02-04 Created: 2015-01-12 Last updated: 2015-02-04Bibliographically approved

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