Linked Life Data

16105875

Source:http://linkedlifedata.com/resource/pubmed/id/16105875

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
Pt 17
pubmed:dateCreated
2005-8-30
pubmed:abstractText
Although the cell line K562 reportedly expresses a single species of beta1 integrin, alpha5beta1, surface staining with monoclonal antibodies JB1A, 12G10 and B3B11 to the beta1 chain clearly demonstrated differences in the expression levels of the epitopes detected by these antibodies. The present studies were initiated to determine the basis for this molecular heterogeneity in the integrins. Cross-linking of surface integrins with B3B11 caused their selective aggregation. This distribution was similar to that observed for the alpha5 chain. In contrast, cross-linking the beta1 chains with 12G10 did not cause codistribution of alpha5, suggesting that these two species were not associated on the cell surface. Immunoprecipitates of the surface integrins of K562 cells indicated the presence of 120 and 140 kDa forms of the beta1 chain which were detected by 12G10 and B3B11, respectively. Immunological, biochemical and mass spectrometric analysis of K562 surface integrins also failed to demonstrate the presence of any alpha chain in association with the 120 kDa species of beta1 of K562 cells. Treatment of the two forms of beta1 with PGNase reduced their masses to approximately 90 kDa, suggesting that N-glycosylation was responsible for the mass differences. Collectively, these results provide evidence for a novel species of beta1 on the cell surface, which does not appear to be associated with any alpha chain. The data also suggest that differences in glycosylation may be involved in defining the association between the integrin alpha and beta chains and the functional properties of these integrins.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0021-9533
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
118
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
4009-16
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2005
pubmed:articleTitle
Evidence for the presence of a low-mass beta1 integrin on the cell surface.
pubmed:affiliation
Manitoba Centre for Proteomics and Systems Biology, Department of Internal Medicine, University of Manitoba, 715 McDermot Avenue, Winnipeg, MB, Canada R3E 3P4.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't, Research Support, N.I.H., Extramural