Linked Life Data

8104555

Source:http://linkedlifedata.com/resource/pubmed/id/8104555

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1993-11-18
pubmed:abstractText
Protein structure and tissue type are known to influence glycosylation of proteins. We have previously investigated the N-glycans at each of the three glycosylation sites of the cell surface glycoprotein Thy-1 when isolated from rat brain and thymocytes. Here we report a comparative analysis of the site-specific N-glycosylation patterns from rat (Asn 23, 74, 98), mouse (Asn 23, 75, 99) and human (Asn 23, 60, 100) neural Thy-1. Despite considerable differences in amino acid sequence, the results show a remarkable conservation of the pattern of N-glycans at corresponding sites between the three species, as judged by chromatographic comparisons and glycosidase susceptibility. This is particularly marked for sites at Asn 74/75 in rat/mouse and the equivalent site at 60 in human Thy-1, as well as for sites at Asn 98/99 and 100, respectively. The sites at Asn 23 in rat/mouse also contained almost identical glycosylation patterns, but at this site human Thy-1 showed significantly different glycosylation patterns. These site glycosylation patterns are discussed in relation to the likely accessibility of the oligosaccharides for processing. It is known that within a species, the glycosylation of Thy-1 is tissue specific; therefore, this degree of conservation of glycosylation of Thy-1 expressed in the same tissue in different species is all the more striking, given the known variation between species in the amino acid sequence of Thy-1. It is therefore proposed that neural cells have a particular requirement for specific surface carbohydrates and that the Thy-1 polypeptide serves as an appropriate carrier for these structures.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0959-6658
pubmed:author
pubmed:issnType
Print
pubmed:volume
3
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
339-48
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:8104555-Amino Acid Sequence, pubmed-meshheading:8104555-Animals, pubmed-meshheading:8104555-Antigens, Surface, pubmed-meshheading:8104555-Antigens, Thy-1, pubmed-meshheading:8104555-Brain Chemistry, pubmed-meshheading:8104555-Glycopeptides, pubmed-meshheading:8104555-Glycosylation, pubmed-meshheading:8104555-Humans, pubmed-meshheading:8104555-Membrane Glycoproteins, pubmed-meshheading:8104555-Mice, pubmed-meshheading:8104555-Molecular Sequence Data, pubmed-meshheading:8104555-Multigene Family, pubmed-meshheading:8104555-N-Acetylneuraminic Acid, pubmed-meshheading:8104555-Nerve Tissue Proteins, pubmed-meshheading:8104555-Oligosaccharides, pubmed-meshheading:8104555-Peptide Fragments, pubmed-meshheading:8104555-Polysaccharides, pubmed-meshheading:8104555-Protein Conformation, pubmed-meshheading:8104555-Rats, pubmed-meshheading:8104555-Regulatory Sequences, Nucleic Acid, pubmed-meshheading:8104555-Sequence Homology, Amino Acid, pubmed-meshheading:8104555-Sialic Acids
pubmed:year
1993
pubmed:articleTitle
Comparative analysis of the N-glycans of rat, mouse and human Thy-1. Site-specific oligosaccharide patterns of neural Thy-1, a member of the immunoglobulin superfamily.
pubmed:affiliation
MRC Cellular Immunology Unit, Sir William Dunn School of Pathology, University of Oxford, UK.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't