Matches in UGent Biblio for { <https://biblio.ugent.be/publication/625952#aggregation> ?p ?o. }
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- aggregation classification "A4".
- aggregation creator B329568.
- aggregation creator B329569.
- aggregation creator B329570.
- aggregation creator B329571.
- aggregation creator B329572.
- aggregation creator B329573.
- aggregation creator person.
- aggregation date "2008".
- aggregation format "application/pdf".
- aggregation hasFormat 625952.bibtex.
- aggregation hasFormat 625952.csv.
- aggregation hasFormat 625952.dc.
- aggregation hasFormat 625952.didl.
- aggregation hasFormat 625952.doc.
- aggregation hasFormat 625952.json.
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- aggregation hasFormat 625952.txt.
- aggregation hasFormat 625952.xls.
- aggregation hasFormat 625952.yaml.
- aggregation isPartOf urn:issn:1875-3981.
- aggregation language "eng".
- aggregation publisher "Bentham Science Publishers".
- aggregation rights "I have retained and own the full copyright for this publication".
- aggregation subject "Biology and Life Sciences".
- aggregation title "Consequences of soluble ICAM-1 N-glycan alterations on receptor binding and signaling kinetics in mouse astrocytes".
- aggregation abstract "Soluble intercellular adhesion molecule-1 (sICAM-1) is elevated in the cerebrospinal fluid of patients with severe brain trauma and mouse sICAM-1 induces the production of macrophage inflammatory protein-2 (MIP-2) in mouse astrocytes. The production of MIP-2 is greatly enhanced when sICAM-1 contains sialylated complex-type N-glycans (sICAM-1-CT) as produced by Chinese hamster ovary (CHO) cells. By contrast, sICAM-1 from the Lec1 mutant of CHO cells (sICAM-1-HM), containing only high mannose-type N-glycans, is relatively inactive. Here we show that the Nglycans of sICAM-1-CT are mostly 2,3-sialylated bi-, tri-, and tetraantennary complex-type structures with varying amounts of core fucosylation. Unexpectedly, sICAM-1-CT and sICAM-1-HM bound equivalently to mouse astrocytes. Enhanced MIP-2 induction by sICAM-1-CT was associated with a more rapid, higher level, and prolonged MIP-2 response as well as sICAM-1-CT accumulation at the plasma membranes of mouse astrocytes. These results show that glycosylation of sICAM-1 contributes to its signaling properties at the astrocyte cell surface, and suggest that altered glycosylation which might arise as a result of inflammation could regulate the bioactivity of sICAM-1.".
- aggregation authorList BK621665.
- aggregation endPage "51".
- aggregation startPage "40".
- aggregation volume "1".
- aggregation aggregates 2936522.
- aggregation isDescribedBy 625952.
- aggregation similarTo 1875398100801010040.
- aggregation similarTo LU-625952.