Linked Life Data

15579466

Source:http://linkedlifedata.com/resource/pubmed/id/15579466

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
7
pubmed:dateCreated
2005-2-14
pubmed:abstractText
P-selectin glycoprotein ligand-1 (PSGL-1) interactions with selectins regulate leukocyte migration in inflammatory lesions. In mice, selectin ligand activity regulating leukocyte recruitment and lymphocyte homing into lymph nodes results from the sum of unequal contributions of fucosyltransferase (FucT)-IV and FucT-VII, with FucT-VII playing a predominant role. Here we have examined the role of human FucT-IV and -VII in conferring L-selectin, P-selectin, and E-selectin binding activities to PSGL-1. Lewis x (Le(x)) carbohydrate was generated at the CHO(dhfr)(-) cell surface by FucT-IV expression, whereas sialyl Le(x) (sLe(x)) was synthesized by FucT-VII. Both human FucT-IV and -VII had the ability to generate carbohydrate ligands that support L-selectin-, P-selectin-, and E-selectin-dependent rolling on PSGL-1, with FucT-VII playing a major role. Cooperation was observed between FucT-IV and -VII in recruiting L-, P-, or E-selectin-expressing cells on PSGL-1 and in regulating cell rolling velocity and stability. Additional rolling adhesion assays were performed to assess the role of Thr-57-linked core-2 O-glycans in supporting L-selectin-, P-selectin-, and E-selectin-dependent rolling on PSGL-1. These studies confirmed that core-2 O-glycans attached to Thr-57 play a critical role in supporting L- and P-selectin-dependent rolling and revealed that additional binding sites support >75% of E-selectin-mediated rolling. The observations presented here indicate that human FucT-IV and -VII both contribute and cooperate in regulating L-selectin-, P-selectin-, and E-selectin-dependent rolling on PSGL-1, with FucT-VII playing a predominant role in conferring selectin binding activity to PSGL-1.
pubmed:commentsCorrections
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
18
pubmed:volume
280
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
5378-90
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:15579466-Animals, pubmed-meshheading:15579466-Antigens, CD15, pubmed-meshheading:15579466-CHO Cells, pubmed-meshheading:15579466-Cell Adhesion, pubmed-meshheading:15579466-Cells, Cultured, pubmed-meshheading:15579466-Cricetinae, pubmed-meshheading:15579466-Epitopes, pubmed-meshheading:15579466-Flow Cytometry, pubmed-meshheading:15579466-Fucosyltransferases, pubmed-meshheading:15579466-Glycosylation, pubmed-meshheading:15579466-Humans, pubmed-meshheading:15579466-Leukocyte Rolling, pubmed-meshheading:15579466-Membrane Glycoproteins, pubmed-meshheading:15579466-Mice, pubmed-meshheading:15579466-Neutrophils, pubmed-meshheading:15579466-Oligosaccharides, pubmed-meshheading:15579466-Protein Binding, pubmed-meshheading:15579466-Selectins, pubmed-meshheading:15579466-Transfection
pubmed:year
2005
pubmed:articleTitle
Regulation of PSGL-1 interactions with L-selectin, P-selectin, and E-selectin: role of human fucosyltransferase-IV and -VII.
pubmed:affiliation
Service and Central Laboratory of Hematology, Centre Hospitalier Universitaire Vaudois, Bugnon 46, 1011 Lausanne, Switzerland.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't