CD18

ITGB2
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1L3Y, 1YUK, 2JF1, 2P26, 2P28, 3K6S, 3K71, 3K72, 2V7D, 4NEH, 4NEN, 5E6X, 5E6V, 5E6S, 5E6R, 5E6W, 5ES4, 5E6U
Identifiers
Aliases	ITGB2, CD18, LAD, LCAMB, LFA-1, MAC-1, MF17, MFI7, integrin subunit beta 2
External IDs	OMIM: 600065 MGI: 96611 HomoloGene: 20092 GeneCards: ITGB2
Gene ontology Molecular function • receptor activity • protein complex binding • metal ion binding • glycoprotein binding • protein binding • protein heterodimerization activity • ICAM-3 receptor activity • protein kinase binding • cell adhesion molecule binding Cellular component • integral component of membrane • extracellular vesicle • integrin alphaL-beta2 complex • membrane • plasma membrane • receptor complex • secretory granule • cell surface • integrin complex • extracellular exosome Biological process • leukocyte cell-cell adhesion • single organismal cell-cell adhesion • endodermal cell differentiation • toll-like receptor 4 signaling pathway • positive regulation of nitric oxide biosynthetic process • heterotypic cell-cell adhesion • cell-cell signaling • aging • receptor internalization • leukocyte migration involved in inflammatory response • natural killer cell activation • cellular response to low-density lipoprotein particle stimulus • extracellular matrix organization • receptor clustering • positive regulation of angiogenesis • neutrophil chemotaxis • cell adhesion • positive regulation of NF-kappaB transcription factor activity • regulation of cell shape • regulation of immune response • cellular extravasation • integrin-mediated signaling pathway • cell-matrix adhesion • inflammatory response • endothelial cell migration • leukocyte migration • regulation of peptidyl-tyrosine phosphorylation • apoptotic process • phagocytosis Sources:Amigo / QuickGO
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_001127491 NM_001303238	NM_008404
RefSeq (protein)	NP_000202.3 NP_001120963.2 NP_001290167.1	NP_032430.2
Location (UCSC)	Chr 21: 44.89 – 44.93 Mb	Chr 10: 77.53 – 77.57 Mb
PubMed search	[1]	[2]
Wikidata

View/Edit Human

View/Edit Mouse

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:

• LFA-1 (paired with CD11a)
• Macrophage-1 antigen (paired with CD11b)
• Integrin alphaXbeta2 (paired with CD11c)
• Integrin alphaDbeta2 (paired with CD11d)

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.^[3]

Clinical significance

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.^[4] The soluble beta 2 integrins are ligand binding and plasma levels are inversely associated with disease activity in the autoimmune disease spondyloarthritis.^[5]

Interactions

CD18 has been shown to interact with:

• FHL2,^[6]
• GNB2L1,^[7]
• ICAM-1,^[8][9][10] and
• PSCD1.^[11][12]

See also

• leukocyte adhesion deficiency
• integrin

References

1. "Human PubMed Reference:".
2. "Mouse PubMed Reference:".
3. "Entrez Gene: ITGB2 integrin, beta 2 (complement component 3 receptor 3 and 4 subunit)".
4. 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.
5. 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.
6. 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.
7. 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.
8. 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.
9. 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.
10. 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.
11. 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.
12. 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

• CD18 antigen at the US National Library of Medicine Medical Subject Headings (MeSH)
• ITGB2 Info with links in the Cell Migration Gateway