Open Access Articles- Top Results for CD18


SymbolsITGB2 ; CD18; LAD; LCAMB; LFA-1; MAC-1; MF17; MFI7
External IDsOMIM600065 MGI96611 HomoloGene20092 IUPHAR: 2456 ChEMBL: 3631 GeneCards: ITGB2 Gene
RNA expression pattern
File:PBB GE ITGB2 202803 s at tn.png
More reference expression data
RefSeq (mRNA)NM_000211NM_008404
RefSeq (protein)NP_000202NP_032430
Location (UCSC)Chr 21:
46.31 – 46.35 Mb
Chr 10:
77.53 – 77.57 Mb
PubMed search[1][2]

Integrin beta-2 (CD18) is a protein that in humans is encoded by the ITGB2 gene.

It is the beta subunit of four different structures:

The ITGB2 protein product is the integrin beta chain beta 2. Integrins are integral cell-surface proteins composed of an alpha chain and a beta chain. A given chain may combine with multiple partners resulting in different integrins. For example, beta 2 combines with the alpha L chain to form the integrin LFA-1, and combines with the alpha M chain to form the integrin Mac-1. Integrins are known to participate in cell adhesion as well as cell-surface mediated signalling.[1] In humans lack of CD18 causes Leukocyte Adhesion Deficiency, a disease defined by a lack of leukocyte extravasation from blood into tissues.


CD18 has been shown to interact with ICAM-1,[2][3][4] FHL2,[5] PSCD1[6][7] and GNB2L1.[8]

See also


  1. "Entrez Gene: ITGB2 integrin, beta 2 (complement component 3 receptor 3 and 4 subunit)". 
  2. Kotovuori, A; Pessa-Morikawa T; Kotovuori P; Nortamo P; Gahmberg C G (June 1999). "ICAM-2 and a peptide from its binding domain are efficient activators of leukocyte adhesion and integrin affinity". J. Immunol. (UNITED STATES) 162 (11): 6613–20. ISSN 0022-1767. PMID 10352278. 
  3. Lu, C; Takagi J; Springer T A (May 2001). "Association of the membrane proximal regions of the alpha and beta subunit cytoplasmic domains constrains an integrin in the inactive state". J. Biol. Chem. (United States) 276 (18): 14642–8. ISSN 0021-9258. PMID 11279101. doi:10.1074/jbc.M100600200. 
  4. Huang, C; Springer T A (August 1995). "A binding interface on the I domain of lymphocyte function-associated antigen-1 (LFA-1) required for specific interaction with intercellular adhesion molecule 1 (ICAM-1)". J. Biol. Chem. (UNITED STATES) 270 (32): 19008–16. ISSN 0021-9258. PMID 7642561. doi:10.1074/jbc.270.32.19008. 
  5. Wixler, V; Geerts D; Laplantine E; Westhoff D; Smyth N; Aumailley M; Sonnenberg A; Paulsson M (October 2000). "The LIM-only protein DRAL/FHL2 binds to the cytoplasmic domain of several alpha and beta integrin chains and is recruited to adhesion complexes". J. Biol. Chem. (UNITED STATES) 275 (43): 33669–78. ISSN 0021-9258. PMID 10906324. doi:10.1074/jbc.M002519200. 
  6. Rietzler, M; Bittner M; Kolanus W; Schuster A; Holzmann B (October 1998). "The human WD repeat protein WAIT-1 specifically interacts with the cytoplasmic tails of beta7-integrins". J. Biol. Chem. (UNITED STATES) 273 (42): 27459–66. ISSN 0021-9258. PMID 9765275. doi:10.1074/jbc.273.42.27459. 
  7. Geiger, C; Nagel W, Boehm T, van Kooyk Y, Figdor C G, Kremmer E, Hogg N, Zeitlmann L, Dierks H, Weber K S, Kolanus W (June 2000). "Cytohesin-1 regulates beta-2 integrin-mediated adhesion through both ARF-GEF function and interaction with LFA-1". EMBO J. (ENGLAND) 19 (11): 2525–36. ISSN 0261-4189. PMC 212768. PMID 10835351. doi:10.1093/emboj/19.11.2525. 
  8. Liliental, J; Chang D D (January 1998). "Rack1, a receptor for activated protein kinase C, interacts with integrin beta subunit". J. Biol. Chem. (UNITED STATES) 273 (4): 2379–83. ISSN 0021-9258. PMID 9442085. doi:10.1074/jbc.273.4.2379. 

Further reading

  • Bunting M, Harris ES, McIntyre TM et al. (2002). "Leukocyte adhesion deficiency syndromes: adhesion and tethering defects involving beta 2 integrins and selectin ligands.". Curr. Opin. Hematol. 9 (1): 30–5. PMID 11753075. doi:10.1097/00062752-200201000-00006. 
  • Roos D, Law SK (2003). "Hematologically important mutations: leukocyte adhesion deficiency.". Blood Cells Mol. Dis. 27 (6): 1000–4. PMID 11831866. doi:10.1006/bcmd.2001.0473. 
  • Gahmberg CG, Fagerholm S (2003). "Activation of leukocyte beta2-integrins.". Vox Sang. 83 Suppl 1: 355–8. PMID 12617168. doi:10.1111/j.1423-0410.2002.tb05333.x. 
  • Schymeinsky J, Mócsai A, Walzog B (2007). "Neutrophil activation via beta2 integrins (CD11/CD18): molecular mechanisms and clinical implications.". Thromb. Haemost. 98 (2): 262–73. PMID 17721605. doi:10.1160/th07-02-0156. 

External links

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