Artikel: Tyrosine replacement in P-selectin glycoprotein ligand-1 affects distinct kinetic and mechanical properties of bonds with P- and L-selectin.
Proceedings of the National Academy of Sciences of the United States of America
1999 Band 96, Heft 24, Seite(n) 13771–13776
Abstract: ... strength to resist premature dissociation by the forces applied in shear flow. P- and L-selectin bind ... to the N-terminal region of P-selectin glycoprotein ligand-1 (PSGL-1), a mucin on leukocytes. To define ... we compared rolling of transfected preB cells expressing P- or L-selectin on transfected cell monolayers ...
| Abstract | Selectins are adhesion molecules that initiate tethering and rolling of leukocytes on the vessel wall. Rolling requires rapid formation and breakage of selectin-ligand bonds that must have mechanical strength to resist premature dissociation by the forces applied in shear flow. P- and L-selectin bind to the N-terminal region of P-selectin glycoprotein ligand-1 (PSGL-1), a mucin on leukocytes. To define determinants on PSGL-1 that contribute to the kinetic and mechanical properties of bonds with selectins, we compared rolling of transfected preB cells expressing P- or L-selectin on transfected cell monolayers expressing wild-type PSGL-1 or PSGL-1 constructs with substitutions in targeted N-terminal residues. Rolling through P- or L-selectin required a Thr or Ser at a specific position on PSGL-1, the attachment site for an essential O-glycan, but required only one of three nearby Tyr residues, which are sites for Tyr-SO(3) formation. The adhesive strengths and numbers of cells rolling through P- or L-selectin were similar on wild-type PSGL-1 and on each of the three PSGL-1 constructs containing only a single Tyr. However, the cells rolled more irregularly on the single-Tyr forms of PSGL-1. Analysis of the lifetimes of transient tethers on limiting densities of PSGL-1 revealed that L-selectin dissociated faster from single-Tyr than wild-type PSGL-1 at all shears examined. In sharp contrast, P-selectin dissociated faster from single-Tyr than wild-type PSGL-1 at higher shear but not at lower shear. Thus, tyrosine replacements in PSGL-1 affect distinct kinetic and mechanical properties of bonds with P- and L-selectin. |
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| Mesh-Begriff(e) | Amino Acid Sequence ; Animals ; B-Lymphocytes/cytology ; B-Lymphocytes/metabolism ; CHO Cells ; Cricetinae ; Gene Expression ; Genetic Engineering ; Hematopoietic Stem Cells/cytology ; Hematopoietic Stem Cells/metabolism ; Humans ; Kinetics ; L-Selectin/genetics ; L-Selectin/metabolism ; Ligands ; Membrane Glycoproteins/genetics ; Membrane Glycoproteins/metabolism ; Molecular Sequence Data ; Mucins/genetics ; Mucins/metabolism ; Mutagenesis, Site-Directed ; P-Selectin/genetics ; P-Selectin/metabolism ; Sequence Homology, Amino Acid ; Tyrosine/genetics ; Tyrosine/metabolism |
| Chemische Substanzen | Ligands ; Membrane Glycoproteins ; Mucins ; P-Selectin ; P-selectin ligand protein ; L-Selectin (126880-86-2) ; Tyrosine (42HK56048U) |
| Sprache | Englisch |
| Erscheinungsdatum | 1999-11-23 |
| Erscheinungsland | United States |
| Dokumenttyp | Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, P.H.S. |
| ZDB-ID | 209104-5 |
| ISSN | 1091-6490 ; 0027-8424 |
| ISSN (online) | 1091-6490 |
| ISSN | 0027-8424 |
| DOI | 10.1073/pnas.96.24.13771 |
| Datenquelle | MEDical Literature Analysis and Retrieval System OnLINE |
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