- 関
- L-セレクチン
- 関
- L-Selectin
Wikipedia preview
出典(authority):フリー百科事典『ウィキペディア(Wikipedia)』「2012/09/30 22:32:13」(JST)
[Wiki en表示]
Selectin L |
Rendering based on PDB 1KJB. |
Available structures |
PDB |
Ortholog search: PDBe, RCSB |
List of PDB id codes |
2LGF, 3CFW
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Identifiers |
Symbols |
SELL; CD62L; LAM1; LECAM1; LEU8; LNHR; LSEL; LYAM1; PLNHR; TQ1 |
External IDs |
OMIM: 153240 MGI: 98279 HomoloGene: 539 ChEMBL: 3161 GeneCards: SELL Gene |
Gene Ontology |
Molecular function |
• protease binding
• protein binding
• heparin binding
• carbohydrate binding
• glycosphingolipid binding
• cell adhesion molecule binding
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Cellular component |
• plasma membrane
• integral to plasma membrane
• external side of plasma membrane
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Biological process |
• cell adhesion
• blood coagulation
• response to ATP
• regulation of immune response
• leukocyte migration
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Sources: Amigo / QuickGO |
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RNA expression pattern |
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More reference expression data |
Orthologs |
Species |
Human |
Mouse |
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Entrez |
6402 |
20343 |
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Ensembl |
ENSG00000188404 |
ENSMUSG00000026581 |
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UniProt |
P14151 |
P18337 |
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RefSeq (mRNA) |
NM_000655.4 |
NM_001164059.1 |
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RefSeq (protein) |
NP_000646.2 |
NP_001157531.1 |
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Location (UCSC) |
Chr 1:
169.66 – 169.68 Mb |
Chr 1:
164.06 – 164.08 Mb |
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PubMed search |
[1] |
[2] |
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L-selectin, also known as CD62L, is a cell adhesion molecule found on lymphocytes. It belongs to the selectin family of proteins, which recognize 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 that play important roles in lymphocyte-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]
Contents
- 1 Ligands
- 2 Function
- 3 References
- 4 External links
- 5 Further reading
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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.
Function
L-selectin acts as a "homing receptor" for lymphocytes to enter secondary lymphoid tissues via high endothelial venules. Ligands present on endothelial cells will bind to lymphocytes expressing L-selectin, slowing lymphocyte 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, as they circulate in the periphery and have immediate effector functions upon encountering antigen.
References
- ^ "Entrez Gene: SELL selectin L (lymphocyte adhesion molecule 1)". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6402.
- ^ Cotran; Kumar, Collins (1998). Robbins Pathologic Basis of Disease. Philadelphia: W.B Saunders Company. ISBN 0-7216-7335-X.
External links
- L-Selectin at the US National Library of Medicine Medical Subject Headings (MeSH)
- Immunology at MCG 1/physresp
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. PMC 2189363. PMID 2473156. //www.ncbi.nlm.nih.gov/pmc/articles/PMC2189363/.
- 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. PMC 2115458. PMID 2663882. //www.ncbi.nlm.nih.gov/pmc/articles/PMC2115458/.
- 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. PMC 336895. PMID 2664786. //www.ncbi.nlm.nih.gov/pmc/articles/PMC336895/.
- 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. PMC 26412. PMID 8986819. //www.ncbi.nlm.nih.gov/pmc/articles/PMC26412/.
- 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. PMC 2134294. PMID 9024699. //www.ncbi.nlm.nih.gov/pmc/articles/PMC2134294/.
- 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. PMC 2212365. PMID 9625756. //www.ncbi.nlm.nih.gov/pmc/articles/PMC2212365/.
- Malhotra R, Ward M, Sim RB, Bird MI (1999). "Identification of human complement Factor H as a ligand for L-selectin". Biochem. J. 341 (1): 61–9. doi:10.1042/0264-6021:3410061. PMC 1220330. PMID 10377245. //www.ncbi.nlm.nih.gov/pmc/articles/PMC1220330/.
- 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. PMC 2118927. PMID 1678774. //www.ncbi.nlm.nih.gov/pmc/articles/PMC2118927/.
This article incorporates text from the United States National Library of Medicine, which is in the public domain.
Transmembrane receptors: Immunoglobulin superfamily immune receptors
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Antibody receptor:
Fc receptor |
Epsilon (ε)
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FcεRI · (FcεRII is C-type lectin)
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Gamma (γ)
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FcγRI · FcγRII · FcγRIII · Neonatal
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Alpha (α)/mu (μ)
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FcαRI · Fcα/μR
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Secretory
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Polymeric immunoglobulin receptor
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Antigen receptor |
B cells
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Antigen receptor
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BCR
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Co-receptor
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stimulate: CD21/CD19/CD81
inhibit: CD22
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Accessory molecules
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Ig-α/Ig-β (CD79)
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T cells
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Ligands
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MHC (MHC class I and MHC class II)
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Antigen receptor
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TCR: TRA@ · TRB@ · TRD@ · TRG@
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Co-receptors
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CD8 (with two glycoprotein chains CD8α and CD8β) · CD4
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Accessory molecules
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CD3 · CD3γ · CD3δ · CD3ε · ζ-chain (also called CD3ζ and TCRζ)
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Cytokine receptor |
see cytokine receptors
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Killer-cell IG-like receptors |
KIR2DL1, KIR2DL2, KIR2DL3, KIR2DL4, KIR2DL5A, KIR2DL5B, KIR2DS1, KIR2DS2, KIR2DS3, KIR2DS4, KIR2DS5, KIR3DL1, KIR3DL2, KIR3DL3, KIR3DS1
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Leukocyte IG-like receptors |
LILRA1 · LILRA2 · LILRA3 · LILRA4 · LILRA5 · LILRA6 · LILRB1 · LILRB2 · LILRB3 · LILRB4 · LILRB5 · LILRA6 · LILRA5
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B trdu: iter (nrpl/grfl/cytl/horl), csrc (lgic, enzr, gprc, igsr, intg, nrpr/grfr/cytr), itra (adap, gbpr, mapk), calc, lipd; path (hedp, wntp, tgfp+mapp, notp, jakp, fsap, hipp, tlrp)
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cell/phys/auag/auab/comp, igrc
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Membrane proteins: cell adhesion molecules
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Calcium-independent |
IgSF CAM |
- N-CAM (Myelin protein zero)
- ICAM (1, 5)
- VCAM-1
- PE-CAM
- L1-CAM
- Nectin (PVRL1, PVRL2, PVRL3)
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Integrins |
- LFA-1 (CD11a+CD18)
- Integrin alphaXbeta2 (CD11c+CD18)
- Macrophage-1 antigen (CD11b+CD18)
- VLA-4 (CD49d+CD29)
- Glycoprotein IIb/IIIa (ITGA2B+ITGB3)
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Calcium-dependent |
Cadherins |
Classical |
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Desmosomal |
- Desmoglein (DSG1, DSG2, DSG3, DSG4)
- Desmocollin (DSC1, DSC2, DSC3)
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Protocadherin |
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Unconventional/ungrouped |
- T-cadherin
- CDH4
- CDH5
- CDH6
- CDH8
- CDH11
- CDH12
- CDH15
- CDH16
- CDH17
- CDH9
- CDH10
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Selectins |
- E-selectin
- L-selectin
- P-selectin
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Other |
- Lymphocyte homing receptor: CD44
- L-selectin
- integrin (VLA-4, LFA-1)
- Carcinoembryonic antigen
- CD22
- CD24
- CD44
- CD146
- CD164
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- See also
- cell membrane protein disorders
B memb: cead, trns (1A, 1C, 1F, 2A, 3A1, 3A2-3, 3D), othr
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UpToDate Contents
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English Journal
- Vitamin C treatment of mouse bone marrow-derived dendritic cells enhanced CD8(+) memory T cell production capacity of these cells in vivo.
- Jeong YJ1, Kim JH1, Hong JM1, Kang JS1, Kim HR1, Lee WJ1, Hwang YI2.
- Immunobiology.Immunobiology.2014 Jul;219(7):554-64. doi: 10.1016/j.imbio.2014.03.006. Epub 2014 Mar 20.
- Vitamin C has been found to stimulate dendritic cells (DCs) to secrete more IL-12 and thereby drive naïve CD4(+) T cells to differentiate into Th1 cells. In the present study, we evaluated the effect of these vitamin C-treated DCs on CD8(+) T cell differentiation both in vitro and in vivo. Mouse bo
- PMID 24698552
- Inhibition of human neutrophils NEP activity, CD11b/CD18 expression and elastase release by 3,4-dihydroxyphenylethanol-elenolic acid dialdehyde, oleacein.
- Czerwińska ME1, Kiss AK1, Naruszewicz M2.
- Food chemistry.Food Chem.2014 Jun 15;153:1-8. doi: 10.1016/j.foodchem.2013.12.019. Epub 2013 Dec 11.
- Polyphenols, such as oleacein (3,4-DHPEA-EDA; 3,4-dihydroxyphenylethanol-elenolic acid dialdehyde), are believed to play a role in the prevention of cardiovascular diseases. Due to an increase of neutrophil mediators in acute myocardial infarction the aim of this study was to establish the effect of
- PMID 24491692
- Trafficking phenotype and production of granzyme B by double negative B cells (IgG(+)IgD(-)CD27(-)) in the elderly.
- Bulati M1, Buffa S1, Martorana A1, Candore G1, Lio D1, Caruso C1, Colonna-Romano G2.
- Experimental gerontology.Exp Gerontol.2014 Jun;54:123-9. doi: 10.1016/j.exger.2013.12.011. Epub 2014 Jan 2.
- The impairment of humoral immune response in elderly humans has been extensively demonstrated. We have reported the increase of memory B cells (IgG(+)IgD(-)CD27(-), double negative, DN) population in the elderly, in which there is also a typical inflammatory micro-environment. In order to evaluate w
- PMID 24389059
Japanese Journal
- P1-013 NK細胞はIL-7と協調し腸炎惹起性T細胞の分化増殖を制御する
- 永石 宇司,山地 統,鬼沢 道夫,鈴木 雅博,谷口 未樹,金井 隆典,荒瀬 尚,渡辺 守
- 日本臨床免疫学会会誌 35(4), 333a-333a, 2012
- … 対する細胞傷害活性はIL-7の有無によって影響されなかった.抗asialo GM1抗体の投与でRAG−/−のNK細胞を除去し,naive T細胞の移入後早期の腸間膜リンパ節を解析した結果,移入5日後よりCD44+ CD62L−およびCD44− CD62L−のT細胞分画が増加した.RAG−/−およびIL-7−/−RAG−/−へnaive T細胞を移入して大腸炎を誘発しつつ,抗asialo GM1抗体を第1-4週,第5-12週,第1-12週に投与した各群と12週間の溶媒コントロー …
- NAID 130003364050
- P1-009 Abatacept治療によるリウマチ患者末梢血Treg phenotypeおよびTreg/Th17バランスの変化
- 前田 伸治,前田 智代,難波 大夫,速水 芳仁
- 日本臨床免疫学会会誌 35(4), 331a-331a, 2012
- … 【方法】今回我々はAbatacept使用前後(0, 4 wks)のヒトリウマチ患者末梢血(n=16) CD4+ Foxp3+T cell (Treg)のPhenotype (CD25, CD45RA, CD69, CD62L, CD31, CD39, CD127, CD161),機能マーカー(CTLA-4 (intra), GITR, GARP, LAG-3, HLA-DR)ケモカイン受容体(CCR4, CCR6, CXCR3)および,内在性(Helios)および増殖マーカー(Ki67)と全部で18のマーカーを染色,多色フローサイトメトリー法にて網羅的に比較解析した. …
- NAID 130003364046
- W6-6 関節リウマチにおけるCTLA4-Ig共刺激シグナル阻害剤のCD8+ T細胞への影響
- 松谷 隆治,李 穎,村上 美帆,關口 昌弘,松井 聖,北野 将康,大村 浩一郎,井村 嘉孝,藤井 隆夫,黒岩 孝則,中原 英子,前田 恵治,船内 正憲,村上 孝作,入交 重雄,森田 智視,川人 豊,三森 経世,佐野 統,西本 憲弘
- 日本臨床免疫学会会誌 35(4), 313b-313b, 2012
- … 【方法】生物学的製剤未使用RA患者に対するABTの有効性と安全性の検討試験(ABROAD試験)に登録した31例の患者から治療前および治療後6ヵ月に末梢血単核球を分離し,T細胞活性化に関わるCD25, CD69, CD62L等の細胞表面マーカーをFACSで解析し,CD4+ T細胞とCD8+ T細胞の間で比較した. …
- NAID 130003364018
Related Links
- クローン 145/15は、細胞表面抗原のセレクチンファミリーに属する 74 kDa の糖タンパク質であるヒトCD62Lを認識します。CD62L抗原は、L-セレクチン, LECAM-1, LAM-1 とも呼ばれます。CD62L は、CD34, GlyCAM-1, MAdCAM-1などの糖 ...
- CD62L抗原は、LECAM-1またはL-セレクチンとも呼ばれる分子量75kDaの分子で、末梢リンパ節へのホーミングレセプタとして機能します。リンパ球の高内皮小静脈(HEV)への結合と活性化した内皮細胞上でのローリングにも関与します。
Related Pictures
★リンクテーブル★
[★]
- 同
- MY10, SGP90
発現細胞
- hematopoietic precursors, capillary endothelium (IMM.785)
- GIST
機能
[★]
- 関
- T細胞、late double-positive thymocyte<-->memory CD4 T cell
- TCRを備え、胸腺から出てた抗原刺激をまだ受けていないT細胞。
細胞表面マーカー=
[★]
- 英
- L-selectin
- 同
- MEL-14抗原 MEL-14 antigen、LAM-1、LECAM-1、LEC-CAM-1、Leu8、CD62L
- 関
- セレクチンファミリー,細胞接着分子
[★]
- 同
- CD62L
- 同
- CD62L