L-selectin

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Selectin L (lymphocyte adhesion molecule 1)

Identifiers

Symbols

SELL; CD62L; LAM-1; LAM1; LECAM1; LNHR; LSEL; LYAM1; Leu-8; Lyam-1; PLNHR; TQ1; hLHRc

External IDs

OMIM: 153240 MGI: 98279 HomoloGene: 539

Gene ontology
Molecular function:	• protein binding • sugar binding
Cellular component:	• plasma membrane • integral to plasma membrane • external side of plasma membrane
Biological process:	• cell motility • cell adhesion

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_000655 (mRNA)
NP_000646 (protein)

NM_011346 (mRNA)
NP_035476 (protein)

Location

Chr 1: 167.93 - 167.95 Mb

Chr 1: 165.9 - 165.91 Mb

Pubmed search

[1]

[2]

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]

1 Ligands
2 Function
3 External links
4 References
5 Further reading

[edit] Ligands

GlyCAM-1, found in the high endothelial venules of the lymph nodes.
CD34, found on endothelial cells.
MadCAM-1, found on endothelial cells of gut associated lymphoid tissue.
PSGL-1, binds with low affinity.

[edit] Function

L-selectin acts as a "homing receptor" for leukocytes to enter secondary lymphoid tissues via the high endothelial venules. Ligands present on endothelial cells will bind to leukocytes expressing L-selectin, which causes the leukocytes to become localised at that point^[2]. The receptor is also found on the cell surfaces of "naive" T cells, which have not yet encountered their specific antigen. This surface expression is lost after the cells are activated.

[edit] External links

MeSH L-Selectin
Immunology at MCG 1/physresp

[edit] References

^ "Entrez Gene: SELL selectin L (lymphocyte adhesion molecule 1)".
^ Cotran; Kumar, Collins. Robbins Pathologic Basis of Disease. Philadelphia: W.B Saunders Company. 0-7216-7335-X.

[edit] Further reading

Ryan US, Worthington RE (1992). "Cell-cell contact mechanisms.". Curr. Opin. Immunol. 4 (1): 33–7. 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. 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. 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. 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. 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. 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. 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. 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. 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. 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. 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. 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. PMID 10377245.

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v • d • e

Transmembrane receptors: immune receptors

Cytokine receptor

Type I	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, CSF2RB)

Type II	Interleukins (10, 20, 22, 28) - interferon (-α/β, -γ)

Ig superfamily	CSF1, C-kit, IL-1, IL-18

TNF	CD27, CD30, CD40, CD120, Lymphotoxin β

Chemokines	IL-8 (α, β), CCR1,CXCR4

Other	IL-17, TGF-beta (1, 2)

Other endogenous


Fc receptor	ε (FcεRI, FcεRII) γ (FcγRI, FcγRII, FcγRIII, Neonatal) α/μ (FcαRI, Fcα/μR)

Lymphocyte homing receptor	CD44 - L-selectin - integrin (VLA-4, LFA-1)

Other	Complement - Immunophilins - Integrin - Killer-cell immunoglobulin-like - Scavenger

Exogenous

Pattern recognition/Toll-like	TLR 1 - TLR 2 - TLR 3 - TLR 4 - TLR 5 - TLR 6 - TLR 7 - TLR 8 - TLR 9 - TLR 10

Antigen receptor	B-cell - T cell

Other	Formyl peptide

v • d • e Membrane proteins: cell adhesion molecules

IgSF	N-CAM (Myelin protein zero) - ICAM (1, 4) - VCAM-1 - PE-CAM - L1-CAM

Cadherins	Desmoglein (DSG1, DSG2, DSG3, DSG4) - Desmocollin (DSC1, DSC2, DSC3) - T-cadherin - Protocadherin - CDH1 - CDH2 - CDH3 - CDH4 - CDH5 - CDH6 - CDH8 - CDH11 - CDH12 - CDH15 - CDH16 - CDH17

Selectins	E-selectin - L-selectin - P-selectin

Integrins	LFA-1 - Integrin alphaXbeta2 - Macrophage-1 antigen - VLA-4 - Glycoprotein IIb/IIIa (Note: integrins not always classified as CAMs)

Other	Carcinoembryonic antigen - CD22 - CD24 - CD44 - CD146 - CD164

v • d • e 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 - 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	CD101 - CD102 - CD103 - CD104 - CD105 - CD106 - CD107 (a, b) - CD108 - CD109 - CD110 - CD111 - CD112 - CD113 - CD114 - CD115 - CD116 - CD117 - CD118 - CD119 - CD120 (a, b) - CD121 (a, b) - CD122 - CD123 - CD124 - CD125 - CD126 - CD127 - CD129 - CD130 - CD131 - CD132 - CD133 - CD134 - CD135 - CD136 - CD137 - CD138 - CD140b - CD141 - CD142 - CD143 - CD144 - CD146 - CD147 - CD148 - CD150

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	CD201 - CD202b - CD204 - CD205 - CD206 - CD207 - CD208 - CD209 - CDw210 (a, b) - CD212 - CD213a (1, 2) - CD217 - CD218 (a, b) - CD220 - CD221 - CD222 - CD223 - CD224 - CD225 - CD226 - CD227 - CD228 - CD229 - CD230 - CD233 - CD234 - CD235 (a, b) - CD236 - CD238 - CD239 - CD240CE - CD241 - CD243 - CD244 - CD246 - CD247- CD248 - CD249

251-300	CD252 - CD253 - CD254 - CD256 - CD257 - CD258 - CD261 - CD262 - CD264 - CD265 - CD266 - CD267 - CD268 - CD269 - CD271 - CD272 - CD273 - CD274 - CD275 - CD276 - CD278 - CD279 - CD280 - CD281 - CD282 - CD283 - CD284 - CD286 - CD288 - CD289 - CD290 - CD292 - CDw293 - CD294 - CD295 - CD297 - CD298 - CD299

301-350	CD300A - CD304 - CD305 - CD307 - CD309 - CD312 - CD314 - CD315 - CD316 - CD317 - CD318 - CD320 - CD321 - CD322 - CD324 - CD325 - CD326 - CD328 - CD329 - CD331 - CD332 - CD333 - CD334 - CD335 - CD336 - CD337 - CD338 - CD339 - CD340 - CD344 - CD349 - CD350

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