Linked Life Data

8636088

Source:http://linkedlifedata.com/resource/pubmed/id/8636088

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
12
pubmed:dateCreated
1996-7-9
pubmed:abstractText
We report the isolation and structural characterization of an oligo/polysialic acid-containing glycopeptide fraction (designated ESP-Sia) prepared from the egg cell surface complex of the sea urchin, Hemicentrotus pulcherrimus, by exhaustive pronase treatment. The carbohydrate chains isolated from ESP-Sia were shown to consist of O-linked oligo/polysialic acid-containing glycan units and N-linked carbohydrate chains. The present studies have revealed that the O-linked oligo/polysialic acid-containing glycan chains derived from the ESP-Sia were similar to those present in egg jelly coat polysialylated glycoprotein in being composed of tandem repeats of N-glycolylneuraminic acid (Neu5Gc) glycosidically linked in a novel fashion through the glycolyl group, (-->5-OglycolylNeu5Gcalpha2-->)n. However, they differ from the egg jelly coat in two key respects. First, the average degree of polymerization of the oligo/polysialic acid chains of ESP-Sia is only 3; a value far lower than that found in the jelly coat glycoprotein (average degree of polymerization was about 20). Second, ESP-Sia is uniquely characterized by the presence of 9-O-sulfated N-glycolylneuraminic acid (Neu5Gc9HSO3) residues at the nonreducing termini of the (-->5-OglycolylNeu5Gcalpha 2-->)n chains. The terminal sialyl residues in the Neu5Gc9HSO3 alpha2-->(-->5-OglycolylNeu5Gcalpha2-->)n chains were totally resistant to exosialidases. The discovery of Neu5Gc9HSO3 as the nonreducing terminal residue of oligo/poly(-->5-OglycolylNeu5Gcalpha 2-->) group is especially noteworthy in that Neu5Gc9HSO3 appears to be of limited distribution among glycoconjugates. Following the earlier discovery of oligo/polysialic acid chains capped with KDN, i.e. KDN alpha2-->(-->8Neu5Gcalpha2-->)n, found in rainbow trout egg polysialoglycoproteins, it now appears that the sulfated Neu5Gc can serve a similar capping function.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
22
pubmed:volume
271
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
6694-701
pubmed:dateRevised
2009-9-29
pubmed:meshHeading
pubmed:year
1996
pubmed:articleTitle
The occurrence of novel 9-O-sulfated N-glycolylneuraminic acid-capped alpha2-->5-Oglycolyl-linked oligo/polyNeu5Gc chains in sea urchin egg cell surface glycoprotein. Identification of a new chain termination signal for polysialyltransferase.
pubmed:affiliation
Department of Biophysics and Biochemistry, Graduate School of Science, University of Tokyo, Hongo-7 Tokyo 113, Japan.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't