| First Author | Lasky LA | Year | 1992 |
| Journal | Cell | Volume | 69 |
| Issue | 6 | Pages | 927-38 |
| PubMed ID | 1376638 | Mgi Jnum | J:45480 |
| Mgi Id | MGI:1195510 | Doi | 10.1016/0092-8674(92)90612-g |
| Citation | Lasky LA, et al. (1992) An endothelial ligand for L-selectin is a novel mucin-like molecule. Cell 69(6):927-38 |
| abstractText | The adhesive interaction between circulating lymphocytes and the high endothelial venules (HEV) of lymph nodes (LN) is mediated by lymphocyte L-selectin, a member of the selectin family of cell adhesion proteins. Previous work has identified a sulfated 50 kd glycoprotein (Sgp50) as an HEV ligand for L-selectin. We now report the purification of this glycoprotein and the utilization of the derived N-terminal amino acid sequence to clone a cDNA. The predicted sequence reveals a novel, mucin-like molecule containing two serine/threonine-rich domains. The mRNA encoding this glycoprotein is preferentially expressed in LN. Antibodies against predicted peptides immunoprecipitate Sgp50 and stain the apical surface of LN HEV. These results thus define a tissue-specific mucin-like endothelial glycoprotein that appears to function as a scaffold that presents carbohydrates to the L-selectin lectin domain. |
