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| Subject | Predicate | Object |
|---|---|---|
| http://purl.uniprot.org/citations/11566773 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/11566773 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/11566773 | http://www.w3.org/2000/01/rdf-schema#comment | "P-selectin glycoprotein ligand-1 (PSGL-1) is a large (240 kDa) glycoprotein found on the surface of nearly all leukocytes. The mature molecule is decorated with multiple N- and O-linked glycans and displays copies of the tetrasaccharide sialyl-Lewis(x) (sLe(X)), as well as a cluster of three tyrosine sulfate (tyr-SO(3)) groups near the N-terminus of the processed protein. Previous studies have suggested that PSGL-1 needs to be tyrosine-sulfated, in addition to glycosylated with sLe(X), to successfully interact with P-selectin. To better understand how biochemical features of the PSGL-1 ligand are related to its adhesion phenotype, we have measured the dynamics of adhesion under flow of a series of well-defined PSGL-1 variants that differ in their biochemical modification, to both P- and E-selectin-coated substrates. These variants are distinct PSGL-1 peptides: one that possesses sLe(X) in conjunction with three N-terminal tyr-SO(3) groups (SGP3), one that possesses sLe(X) without tyrosine sulfation (GP1), and one that lacks sLe(X) but has three N-terminal tyr-SO(3) groups (SP3). Although all peptides expressing sLe(X), tyr-SO(3), or both supported some form of rolling adhesion on P-selectin, only peptides expressing sLe(X) groups showed rolling adhesion on E-selectin. On P-selectin, the PSGL-1 peptides demonstrated a decreasing strength of adhesion in the following order: SGP3 > GP1 > SP3. Robust, rolling adhesion on P-selectin was mediated by the GP1 peptide, despite its lack of tyrosine sulfation. However, the addition of tyrosine sulfation to glycosylated peptides (SGP3) creates a super ligand for P-selectin that supports slower rolling adhesion at all shear rates and supports rolling adhesion at much higher shear rates. Tyrosine sulfation has no similar effect on PSGL-1 rolling on E-selectin. Such functional distinctions in rolling dynamics are uniquely realized with a cell-free system, which permits precise, unambiguous identification of the functional activity of adhesive ligands. These findings are consistent with structural and functional characterizations of the interactions between these peptides and E- and P-selectin published recently."xsd:string |
| http://purl.uniprot.org/citations/11566773 | http://purl.org/dc/terms/identifier | "doi:10.1016/s0006-3495(01)75850-x"xsd:string |
| http://purl.uniprot.org/citations/11566773 | http://purl.org/dc/terms/identifier | "doi:10.1016/s0006-3495(01)75850-x"xsd:string |
| http://purl.uniprot.org/citations/11566773 | http://purl.uniprot.org/core/author | "Camphausen R.T."xsd:string |
| http://purl.uniprot.org/citations/11566773 | http://purl.uniprot.org/core/author | "Camphausen R.T."xsd:string |
| http://purl.uniprot.org/citations/11566773 | http://purl.uniprot.org/core/author | "Hammer D.A."xsd:string |
| http://purl.uniprot.org/citations/11566773 | http://purl.uniprot.org/core/author | "Hammer D.A."xsd:string |
| http://purl.uniprot.org/citations/11566773 | http://purl.uniprot.org/core/author | "Rodgers S.D."xsd:string |
| http://purl.uniprot.org/citations/11566773 | http://purl.uniprot.org/core/author | "Rodgers S.D."xsd:string |
| http://purl.uniprot.org/citations/11566773 | http://purl.uniprot.org/core/date | "2001"xsd:gYear |
| http://purl.uniprot.org/citations/11566773 | http://purl.uniprot.org/core/date | "2001"xsd:gYear |
| http://purl.uniprot.org/citations/11566773 | http://purl.uniprot.org/core/name | "Biophys. J."xsd:string |
| http://purl.uniprot.org/citations/11566773 | http://purl.uniprot.org/core/name | "Biophys. J."xsd:string |
| http://purl.uniprot.org/citations/11566773 | http://purl.uniprot.org/core/pages | "2001-2009"xsd:string |
| http://purl.uniprot.org/citations/11566773 | http://purl.uniprot.org/core/pages | "2001-2009"xsd:string |
| http://purl.uniprot.org/citations/11566773 | http://purl.uniprot.org/core/title | "Tyrosine sulfation enhances but is not required for PSGL-1 rolling adhesion on P-selectin."xsd:string |
| http://purl.uniprot.org/citations/11566773 | http://purl.uniprot.org/core/title | "Tyrosine sulfation enhances but is not required for PSGL-1 rolling adhesion on P-selectin."xsd:string |
| http://purl.uniprot.org/citations/11566773 | http://purl.uniprot.org/core/volume | "81"xsd:string |
| http://purl.uniprot.org/citations/11566773 | http://purl.uniprot.org/core/volume | "81"xsd:string |
| http://purl.uniprot.org/citations/11566773 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/11566773 |
| http://purl.uniprot.org/citations/11566773 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/11566773 |
| http://purl.uniprot.org/citations/11566773 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/11566773 |
| http://purl.uniprot.org/citations/11566773 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/11566773 |