CD18

Integrin, beta 2 (complement component 3 receptor 3 and 4 subunit)

PDB rendering based on 1l3y.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols ITGB2 ; CD18; LAD; LCAMB; LFA-1; MAC-1; MF17; MFI7
External IDs OMIM: 600065 MGI: 96611 HomoloGene: 20092 ChEMBL: 3631 GeneCards: ITGB2 Gene
RNA expression pattern
More reference expression data
Orthologs
Species Human Mouse
Entrez 3689 16414
Ensembl ENSG00000160255 ENSMUSG00000000290
UniProt P05107 P11835
RefSeq (mRNA) NM_000211 NM_008404
RefSeq (protein) NP_000202 NP_032430
Location (UCSC) Chr 21:
44.89 – 44.93 Mb		 Chr 10:
77.53 – 77.57 Mb
PubMed search

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:

Function

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. The beta 2 integrins have also been found in a soluble form.[2] The soluble beta 2 integrins are ligand binding and plasma levels are inversely associated with disease activity in the autoimmune disease spondyloarthritis.[3]

Interactions

CD18 has been shown to interact with:

See also

References

  1. ↑ "Entrez Gene: ITGB2 integrin, beta 2 (complement component 3 receptor 3 and 4 subunit)".
  2. ↑ Gjelstrup, L. C.; Boesen, T.; Kragstrup, T. W.; Jorgensen, A.; Klein, N. J.; Thiel, S.; Deleuran, B. W.; Vorup-Jensen, T. (8 September 2010). "Shedding of Large Functionally Active CD11/CD18 Integrin Complexes from Leukocyte Membranes during Synovial Inflammation Distinguishes Three Types of Arthritis through Differential Epitope Exposure". The Journal of Immunology 185 (7): 4154–4168. doi:10.4049/jimmunol.1000952.
  3. ↑ Kragstrup, Tue W; Jalilian, Babak; Hvid, Malene; Kjærgaard, Anders; Østgård, René; Schiøttz-Christensen, Berit; Jurik, Anne G; Robinson, William H; Vorup-Jensen, Thomas; Deleuran, Bent (2014). "Decreased plasma levels of soluble CD18 link leukocyte infiltration with disease activity in spondyloarthritis". Arthritis Research & Therapy 16 (1): R42. doi:10.1186/ar4471.
  4. ↑ Wixler V, Geerts D, Laplantine E, Westhoff D, Smyth N, Aumailley M, Sonnenberg A, Paulsson M (Oct 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". The Journal of Biological Chemistry 275 (43): 33669–78. doi:10.1074/jbc.M002519200. PMID 10906324.
  5. ↑ Liliental J, Chang DD (Jan 1998). "Rack1, a receptor for activated protein kinase C, interacts with integrin beta subunit". The Journal of Biological Chemistry 273 (4): 2379–83. doi:10.1074/jbc.273.4.2379. PMID 9442085.
  6. ↑ Kotovuori A, Pessa-Morikawa T, Kotovuori P, Nortamo P, Gahmberg CG (Jun 1999). "ICAM-2 and a peptide from its binding domain are efficient activators of leukocyte adhesion and integrin affinity". Journal of Immunology 162 (11): 6613–20. PMID 10352278.
  7. ↑ Lu C, Takagi J, Springer TA (May 2001). "Association of the membrane proximal regions of the alpha and beta subunit cytoplasmic domains constrains an integrin in the inactive state". The Journal of Biological Chemistry 276 (18): 14642–8. doi:10.1074/jbc.M100600200. PMID 11279101.
  8. ↑ Huang C, Springer TA (Aug 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)". The Journal of Biological Chemistry 270 (32): 19008–16. doi:10.1074/jbc.270.32.19008. PMID 7642561.
  9. ↑ Rietzler M, Bittner M, Kolanus W, Schuster A, Holzmann B (Oct 1998). "The human WD repeat protein WAIT-1 specifically interacts with the cytoplasmic tails of beta7-integrins". The Journal of Biological Chemistry 273 (42): 27459–66. doi:10.1074/jbc.273.42.27459. PMID 9765275.
  10. ↑ Geiger C, Nagel W, Boehm T, van Kooyk Y, Figdor CG, Kremmer E, Hogg N, Zeitlmann L, Dierks H, Weber KS, Kolanus W (Jun 2000). "Cytohesin-1 regulates beta-2 integrin-mediated adhesion through both ARF-GEF function and interaction with LFA-1". The EMBO Journal 19 (11): 2525–36. doi:10.1093/emboj/19.11.2525. PMC 212768. PMID 10835351.

Further reading

  • Bunting M, Harris ES, McIntyre TM, Prescott SM, Zimmerman GA (Jan 2002). "Leukocyte adhesion deficiency syndromes: adhesion and tethering defects involving beta 2 integrins and selectin ligands". Current Opinion in Hematology 9 (1): 30–5. doi:10.1097/00062752-200201000-00006. PMID 11753075. 
  • Roos D, Law SK (2003). "Hematologically important mutations: leukocyte adhesion deficiency". Blood Cells, Molecules & Diseases 27 (6): 1000–4. doi:10.1006/bcmd.2001.0473. PMID 11831866. 
  • Gahmberg CG, Fagerholm S (Aug 2002). "Activation of leukocyte beta2-integrins". Vox Sanguinis. 83 Suppl 1: 355–8. doi:10.1111/j.1423-0410.2002.tb05333.x. PMID 12617168. 
  • Schymeinsky J, Mócsai A, Walzog B (Aug 2007). "Neutrophil activation via beta2 integrins (CD11/CD18): molecular mechanisms and clinical implications". Thrombosis and Haemostasis 98 (2): 262–73. doi:10.1160/th07-02-0156. PMID 17721605. 

External links

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