| CD15s | Sialyl Lewis X (sLex), sialylated Lewis X (Sle-x) |
| Molecule Type | Antigen Expression | Molecular Weight Min / Max |
| Non-lineage Restricted Molecule Carbohydrate | Neutrophil Basophil Monocyte Lymph Node Endothelium Lectin Granulocyte Eosinophil T Cell B Cell NK Cell Bone Marrow |
Expression | ||||||||||
| CD15s is expressed widely on neutrophils, basophils, mature granulocytes, monocytes, NK cells, memory helper T cells and T lymphocytes but expression on lymphocytes is variable depending on the antibodies used for detection. Expression is present on immature bone marrow cells and on endothelial cells of high endothelium (HEV) of peripheral lymph nodes. CD15s is expressed on myelomonocytic leukemia cells and on adenocarinomas. | ||||||||||
Structure | ||||||||||
| MOLECULAR FAMILY NAME: Belongs to the carbohydrate family. The CD15s antigen is the sialylated form of CD15 with the structure NeuAc a2 ->3Gal b1 ->4[Fuc a1 ->3]GlcNAc b. It is found at the non-reducing termini of N-linked or O-linked oligosaccharides on glycoproteins as well as on glycosphingolipids. CD15s is not synthesized by the direct sialylation of CD15 but is instead synthesized by fucosylation of NeuAc a2 ->3Gal b1 ->4GlcNAc b-R by the fucosyl transferase VII (FucT-VII). FucT-VII is distinct from FucT-IV which fucosylates Gal b1 ->4GlcNAc b-R to yield CD15s. MOLECULAR MASS
POST-TRANSCRIPTIONAL MODIFICATION: No information. POST-TRANSLATIONAL MODIFICATION: No information. | ||||||||||
Ligands | ||||||||||
| LIGANDS AND MOLECULES ASSOCIATED WITH CD15s The selectins CD62E and CD62P bind CD15s. However, although CD15s is carried by many glycoproteins, selectins appear to bind preferentially to a limited number of cell surface glycoproteins suggesting either that recognition depends on the protein backbone or that these glycoproteins carry rare carbohydrate structures related to CD15s which are better ligands than CD15s itself. | ||||||||||
Function | ||||||||||
| CD15s form is the strongest binding partner for E-selectin. CD15s is involved with different carbohydrate to carbohydrate cell adhesion. The importance of CD15s in health is illustrated by the disease leukocyte adhesion deficiency (LAD) type 2, in which a defect in fucosylation results in decreased levels of CD15s and CD15. Selectin-mediated cell adhesion is impaired in these patients. Mice deficient in the enzyme FucT-VII exhibit leukocytosis, impaired leukocyte extravasation into inflamed tissues, and defective lymphocyte homing. BIOCHEMICAL ACTIVITY: No information. DISEASE RELEVANCE AND FUNCTION OF CD15s IN INTACT ANIMAL: No information. | ||||||||||
Comments | ||||||||||
| MOLECULAR INTERACTIONS- PROTEINS AND DNA ELEMENTS WHICH REGULATE TRANSCRIPTION OF CD15s: No information. SUBSTRATES: No information. ENZYMES WHICH MODIFY CD15s: No information. | ||||||||||
Database accession numbers | ||||||||||
Revised June 25, 2008
|
||||||||||