World Library  
Flag as Inappropriate
Email this Article

L-selectin

Article Id: WHEBN0005533369
Reproduction Date:

Title: L-selectin  
Author: World Heritage Encyclopedia
Language: English
Subject: Sulfatide, P-selectin, List of MeSH codes (D23), Selectin, Cell adhesion molecule
Collection: Cell Adhesion Proteins, Selectins
Publisher: World Heritage Encyclopedia
Publication
Date:
 

L-selectin

Selectin L
Rendering based on PDB .
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols  ; CD62L; LAM1; LECAM1; LEU8; LNHR; LSEL; LYAM1; PLNHR; TQ1
External IDs ChEMBL: GeneCards:
RNA expression pattern
Orthologs
Species Human Mouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)
RefSeq (protein)
Location (UCSC)
PubMed search

L-selectin, also known as CD62L, is a cell adhesion molecule found on lymphocytes and the preimplantation embryo. 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

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

Ligands

Function

L-selectin acts as a "homing receptor" for lymphocytes to enter secondary lymphoid tissues via high endothelial venules.


This article incorporates text from the United States National Library of Medicine, which is in the public domain.

  • Ryan US, Worthington RE (1992). "Cell-cell contact mechanisms". Curr. Opin. Immunol. 4 (1): 33–7.  
  • Nicholson IC (2003). "CD62L (L-selectin)". J. Biol. Regul. Homeost. Agents 16 (2): 144–6.  
  • Ivetic A, Ridley AJ (2005). "The telling tail of L-selectin". Biochem. Soc. Trans. 32 (Pt 6): 1118–21.  
  • 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.  
  • 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.  
  • Bevilacqua M, Butcher E, Furie B, et al. (1991). "Selectins: a family of adhesion receptors". Cell 67 (2): 233.  
  • 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.  
  • 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.  
  • 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.  
  • 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.  
  • Bajorath J, Aruffo A (1995). "A template for generation and comparison of three-dimensional selectin models". Biochem. Biophys. Res. Commun. 216 (3): 1018–23.  
  • 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.  
  • 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.  
  • 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.  
  • 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.  
  • 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.  
  • 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.  
  • 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.  
  • 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.  
  • 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.  

Further reading

External links

  1. ^ "Entrez Gene: SELL selectin L (lymphocyte adhesion molecule 1)". 
  2. ^ Robbins SL, Cotran RS, Kumar V, Collins T (1998). Robbins Pathologic Basis of Disease. Philadelphia: W.B Saunders Company.  
  3. ^ Kohn LA, Hao QL, Sasidharan R, Parekh C, Ge S, Zhu Y, Mikkola HK, Crooks GM (October 2012). "Lymphoid priming in human bone marrow begins before expression of CD10 with upregulation of L-selectin". Nat. Immunol. 13 (10): 963–71.  
  4. ^ James JL, Carter AM, Chamley LW (May 2012). "Human placentation from nidation to 5 weeks of gestation. Part I: What do we know about formative placental development following implantation?". Placenta 33 (5): 327–34.  

References

L-selectin is also present on the surface of human embryo trophoblasts prior to implantation into the uterus. Similar to its function in lymphocytes, L-selectin acts as a receptor to facilitate adhesion of the embryo to the site of invasion on the surface epithelium of the uterine endometrium. The embryo secretes human chorionic gonadotropin (hCG), which downregulates anti-adhesion factor, MUC-1, located on the uterine epithelium at the site of invasion. Removal of MUC-1 exposes the oligosaccharide ligands of the uterine epithelium, thus allowing binding by the L-selectin receptor of the trophopblast cell, followed by embryo adhesion and invasion.[4]

High expression of L-selectin on human bone marrow progenitor cells is an early sign of cells becoming committed to lymphoid differentiation.[3]

. 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. T cells The receptor is commonly found on the cell surfaces of [2]

This article was sourced from Creative Commons Attribution-ShareAlike License; additional terms may apply. World Heritage Encyclopedia content is assembled from numerous content providers, Open Access Publishing, and in compliance with The Fair Access to Science and Technology Research Act (FASTR), Wikimedia Foundation, Inc., Public Library of Science, The Encyclopedia of Life, Open Book Publishers (OBP), PubMed, U.S. National Library of Medicine, National Center for Biotechnology Information, U.S. National Library of Medicine, National Institutes of Health (NIH), U.S. Department of Health & Human Services, and USA.gov, which sources content from all federal, state, local, tribal, and territorial government publication portals (.gov, .mil, .edu). Funding for USA.gov and content contributors is made possible from the U.S. Congress, E-Government Act of 2002.
 
Crowd sourced content that is contributed to World Heritage Encyclopedia is peer reviewed and edited by our editorial staff to ensure quality scholarly research articles.
 
By using this site, you agree to the Terms of Use and Privacy Policy. World Heritage Encyclopedia™ is a registered trademark of the World Public Library Association, a non-profit organization.
 


Copyright © World Library Foundation. All rights reserved. eBooks from Project Gutenberg are sponsored by the World Library Foundation,
a 501c(4) Member's Support Non-Profit Organization, and is NOT affiliated with any governmental agency or department.