Linked Life Data

8647865

Source:http://linkedlifedata.com/resource/pubmed/id/8647865

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
21
pubmed:dateCreated
1996-7-22
pubmed:abstractText
We have examined the post-translational modification of high molecular weight microtubule-associated proteins (MAPs) have shown that MAP1, MAP2, and MAP4 are glycosylated. The presence of carbohydrate residues on these proteins was indicated by labeling with biotin hydrazide following periodate oxidation, a specific and well established method for detecting saccharide moieties on proteins. Both MAP2 and MAP4 were also labeled in vitro by UDP-[3H]galactose in the presence of galactosyltransferase. Labeling by galactosyltransferase indicated that MAP2 and MAP4 contained terminal nonreducing GlcNAc residues, and they appeared to be O-linked to the proteins as shown by their sensitivity to beta-elimination. Chromatographic analysis showed that the GlcNAc residues were directly linked to the proteins as monosaccharides. Thus, we have added MAP2 and MAP4 to the list of intracellular O-GlcNAc-modified proteins, which includes other cytoskeletal proteins such as cytokeratins 8, 13, and 18 and neurofilament proteins NF-L and NF-M. We further characterized the O-GlcNAc modification of MAP2, and stoichiometric analysis indicated that nearly 10% of the MAP2 isolated from rat brain is modified by O-GlcNAc. However, this estimate is thought to reflect the minimal level of O-GlcNAc modification present on MAP2. We have also shown that both the O-GlcNAc and biotin hydrazide-reactive carbohydrate moieties are located on the projection domain of MAP2. Three O-GlcNAc-containing peaks were observed following fast protein liquid chromatography of a tryptic digest of MAP2, suggesting that multiple modification sites exist. The specific modification sites and functional significance of the O-GlcNAc glycosylation on the high Mr MAPs remain to be determined.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
24
pubmed:volume
271
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
12555-61
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1996
pubmed:articleTitle
High molecular weight microtubule-associated proteins contain O-linked-N-acetylglucosamine.
pubmed:affiliation
Department of Cell Biology, Neurobiology, and Anatomy, Ohio State University, Columbus 43210-1239, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.