| First Author | Westmuckett AD | Year | 2011 |
| Journal | PLoS One | Volume | 6 |
| Issue | 5 | Pages | e20406 |
| PubMed ID | 21633705 | Mgi Jnum | J:172569 |
| Mgi Id | MGI:5008317 | Doi | 10.1371/journal.pone.0020406 |
| Citation | Westmuckett AD, et al. (2011) Tyrosine sulfation of native mouse psgl-1 is required for optimal leukocyte rolling on p-selectin in vivo. PLoS One 6(5):e20406 |
| abstractText | BACKGROUND: We recently demonstrated that tyrosine sulfation is an important contributor to monocyte recruitment and retention in a mouse model of atherosclerosis. P-selectin glycoprotein ligand-1 (Psgl-1) is tyrosine-sulfated in mouse monocyte/macrophages and its interaction with P-selectin is important in monocyte recruitment in atherosclerosis. However, whether tyrosine sulfation is required for the P-selectin binding function of mouse Psgl-1 is unknown. Here we test the function of native Psgl-1 expressed in leukocytes lacking endogenous tyrosylprotein sulfotransferase (TPST) activity. METHODOLOGY/PRINCIPAL FINDINGS: Psgl-1 function was assessed by examining P-selectin dependent leukocyte rolling in post-capillary venules of C57BL6 mice transplanted with hematopoietic progenitors from wild type (WT-->B6) or Tpst1;Tpst2 double knockout mice (Tpst DKO-->B6) which lack TPST activity. We observed that rolling flux fractions were lower and leukocyte rolling velocities were higher in Tpst DKO-->B6 venules compared to WT-->B6 venules. Similar results were observed on immobilized P-selectin in vitro. Finally, Tpst DKO leukocytes bound less P-selectin than wild type leukocytes despite equivalent surface expression of Psgl-1. CONCLUSIONS/SIGNIFICANCE: These findings provide direct and convincing evidence that tyrosine sulfation is required for optimal function of mouse Psgl-1 in vivo and suggests that tyrosine sulfation of Psgl-1 contributes to the development of atherosclerosis. |
