L-selectin, also known as CD62L, is a cell adhesion molecule found on leukocytes. It belongs to the selectin family of proteins, which recognise sialylated carbohydrate groups. It is cleaved by ADAM17.
SELL is a cell surface component that is a member of a family of adhesion/homing receptors which play important roles in leukocyte-endothelial cell interactions. The molecule is composed of multiple domains: one homologous to lectins, one to epidermal growth factor, and two to the consensus repeat units found in C3/C4 binding proteins.[1]
Ligands
Function
L-selectin acts as a "homing receptor" for leukocytes to enter secondary lymphoid tissues via high endothelial venules. Ligands present on endothelial cells will bind to leukocyte expressing L-selectin, slowing leukocyte trafficking through the blood, and facilitating entry into a secondary lymphoid organ at that point[2]. The receptor is commonly found on the cell surfaces of T cells. Naive T-lymphocytes, which have not yet encountered their specific antigen, need to enter secondary lymph nodes to encounter their antigen. Central memory T-lymphocytes, which have encountered antigen, express L-selectin to localize in secondary lymphoid organs. Here they reside ready to proliferate upon re-encountering antigen. Effector memory T-lymphocytes do not express L-selectin. These cells circulate in the periphery, so they do not express L-selectin, and have immediate effector functions upon encountering antigen.
References
External links
Further reading
- Ryan US, Worthington RE (1992). "Cell-cell contact mechanisms.". Curr. Opin. Immunol. 4 (1): 33–7. doi:10.1016/0952-7915(92)90120-4. PMID 1375831.
- Nicholson IC (2003). "CD62L (L-selectin).". J. Biol. Regul. Homeost. Agents 16 (2): 144–6. PMID 12144128.
- Ivetic A, Ridley AJ (2005). "The telling tail of L-selectin.". Biochem. Soc. Trans. 32 (Pt 6): 1118–21. doi:10.1042/BST0321118. PMID 15506984.
- Lasky LA, Singer MS, Dowbenko D, et al. (1992). "An endothelial ligand for L-selectin is a novel mucin-like molecule.". Cell 69 (6): 927–38. doi:10.1016/0092-8674(92)90612-G. PMID 1376638.
- Ord DC, Ernst TJ, Zhou LJ, et al. (1990). "Structure of the gene encoding the human leukocyte adhesion molecule-1 (TQ1, Leu-8) of lymphocytes and neutrophils.". J. Biol. Chem. 265 (14): 7760–7. PMID 1692315.
- Bevilacqua M, Butcher E, Furie B, et al. (1991). "Selectins: a family of adhesion receptors.". Cell 67 (2): 233. doi:10.1016/0092-8674(91)90174-W. PMID 1717161.
- Tedder TF, Isaacs CM, Ernst TJ, et al. (1989). "Isolation and chromosomal localization of cDNAs encoding a novel human lymphocyte cell surface molecule, LAM-1. Homology with the mouse lymphocyte homing receptor and other human adhesion proteins.". J. Exp. Med. 170 (1): 123–33. doi:10.1084/jem.170.1.123. PMID 2473156.
- Camerini D, James SP, Stamenkovic I, Seed B (1989). "Leu-8/TQ1 is the human equivalent of the Mel-14 lymph node homing receptor.". Nature 342 (6245): 78–82. doi:10.1038/342078a0. PMID 2509939.
- Bowen BR, Nguyen T, Lasky LA (1989). "Characterization of a human homologue of the murine peripheral lymph node homing receptor.". J. Cell Biol. 109 (1): 421–7. doi:10.1083/jcb.109.1.421. PMID 2663882.
- Siegelman MH, Weissman IL (1989). "Human homologue of mouse lymph node homing receptor: evolutionary conservation at tandem cell interaction domains.". Proc. Natl. Acad. Sci. U.S.A. 86 (14): 5562–6. doi:10.1073/pnas.86.14.5562. PMID 2664786.
- Bajorath J, Aruffo A (1995). "A template for generation and comparison of three-dimensional selectin models.". Biochem. Biophys. Res. Commun. 216 (3): 1018–23. doi:10.1006/bbrc.1995.2722. PMID 7488174.
- Dianzani U, Bragardo M, Buonfiglio D, et al. (1995). "Modulation of CD4 lateral interaction with lymphocyte surface molecules induced by HIV-1 gp120.". Eur. J. Immunol. 25 (5): 1306–11. doi:10.1002/eji.1830250526. PMID 7539755.
- Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides.". Gene 138 (1-2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
- Brenner B, Gulbins E, Schlottmann K, et al. (1997). "L-selectin activates the Ras pathway via the tyrosine kinase p56lck.". Proc. Natl. Acad. Sci. U.S.A. 93 (26): 15376–81. doi:10.1073/pnas.93.26.15376. PMID 8986819.
- Zöllner O, Lenter MC, Blanks JE, et al. (1997). "L-selectin from human, but not from mouse neutrophils binds directly to E-selectin.". J. Cell Biol. 136 (3): 707–16. doi:10.1083/jcb.136.3.707. PMID 9024699.
- Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library.". Gene 200 (1-2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
- Prakobphol A, Thomsson KA, Hansson GC, et al. (1998). "Human low-molecular-weight salivary mucin expresses the sialyl lewisx determinant and has L-selectin ligand activity.". Biochemistry 37 (14): 4916–27. doi:10.1021/bi972612a. PMID 9538010.
- Sassetti C, Tangemann K, Singer MS, et al. (1998). "Identification of podocalyxin-like protein as a high endothelial venule ligand for L-selectin: parallels to CD34.". J. Exp. Med. 187 (12): 1965–75. doi:10.1084/jem.187.12.1965. PMID 9625756.
- Malhotra R, Ward M, Sim RB, Bird MI (1999). "Identification of human complement Factor H as a ligand for L-selectin.". Biochem. J. 341 ( Pt 1): 61–9. doi:10.1042/0264-6021:3410061. PMID 10377245.
- Bradley LM, Duncan DD,Tonkonogy S, Swain SL (1999). "CD4+ effector T cells in vivo: immunization results in a transient population of MEL-14-, CD45RB- helper cells that secretes interleukin 2 (IL-2), IL-3, IL-4, and interferon gamma.". J. Exp. Med. 174 (3): 547-59. doi:10.1084/jem.174.3.547. PMID 1678774.
This article incorporates text from the United States National Library of Medicine, which is in the public domain.
|
Transmembrane receptors: immune receptors |
|
| Cytokine receptor |
|
|
Interleukins ( 2, 3, 4, 5, 6, 7, 9, 11, 12, 13, 15, 21, 23, 27)
CSF receptors (EPO, GM-CSF, G-CSF)
GH · prolactin · Oncostatin M · Leukemia inhibitory factor
common subunits ( Common gamma chain, common beta chain, gp130)
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Other
|
|
|
|
| Other endogenous |
|
|
| Exogenous |
|
|
|
Proteins: clusters of differentiation (see also list of human clusters of differentiation) |
|
| 1-50 |
CD1 ( a-c, 1A, 1D, 1E) · CD2 · CD3 ( γ, δ, ε) · CD4 · CD5 · CD6 · CD7 · CD8 ( a) · CD9 · CD10 · CD11 ( a, b, c) · CD13 · CD14 · CD15 · CD16 ( A, B) · CD18 · CD19 · CD20 · CD21 · CD22 · CD23 · CD24 · CD25 · CD26 · CD27 · CD28 · CD29 · CD30 · CD31 · CD32 ( A, B) · CD33 · CD34 · CD35 · CD36 · CD37 · CD38 · CD39 · CD40 · CD41 · CD42 ( a, b, c, d) · CD43 · CD44 · CD45 · CD46 · CD47 · CD48 · CD49 ( a, b, c, d, e, f) · CD50
|
|
| 51-100 |
CD51 · CD52 · CD53 · CD54 · CD55 · CD56 · CD57 · CD58 · CD59 · CD61 · CD62 ( E, L, P) · CD63 · CD64 ( A, B, C) · CD66 ( a, b, c, d, e, f) · CD68 · CD69 · CD70 · CD71 · CD72 · CD73 · CD74 · CD78 · CD79 ( a, b) · CD80 · CD81 · CD82 · CD83 · CD84 · CD85 ( a, d, e, h, j, k) · CD86 · CD87 · CD88 · CD89 · CD90 · CD91- CD92 · CD93 · CD94 · CD95 · CD97 · CD98 · CD99 · CD100
|
|
| 101-150 |
|
|
| 151-200 |
CD151 · CD152 · CD153 · CD154 · CD155 · CD156 ( a, b, c) · CD157 · CD158 ( a, d, e, i, k) · CD159 ( a, c) · CD160 · CD161 · CD162 · CD163 · CD164 · CD166 · CD167 ( a, b) · CD168 · CD169 · CD170 · CD171 · CD172 ( a, b, g) · CD174 · CD177 · CD178 · CD179 ( a, b) · CD181 · CD182 · CD183 · CD184 · CD185 · CD186 · CD191 · CD192 · CD193 · CD194 · CD195 · CD196 · CD197 · CDw198 · CDw199 · CD200
|
|
| 201-250 |
|
|
| 251-300 |
|
|
| 301-350 |
|
|
This entry is from Wikipedia, the leading user-contributed encyclopedia. It may not have been reviewed by professional editors (see full disclaimer)
