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{{Lead too short|date=November 2016}}
{{PBB_Controls
{{Infobox gene}}
| update_page = yes
'''Integrin beta-2''' ('''CD18''') is a [[protein]] that in humans is encoded by the ''ITGB2'' [[gene]].
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}


<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
It is the beta subunit of four different structures:  
{{GNF_Protein_box
| image = PBB_Protein_ITGB2_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1l3y.
| PDB = {{PDB2|1l3y}}, {{PDB2|1yuk}}
| Name = Integrin, beta 2 (complement component 3 receptor 3 and 4 subunit)
| HGNCid = 6155
| Symbol = ITGB2
| AltSymbols =; LAD; LFA-1; MAC-1; CD18; LCAMB; MF17; MFI7
| OMIM = 600065
| ECnumber = 
| Homologene = 20092
| MGIid = 96611
| GeneAtlas_image1 = PBB_GE_ITGB2_202803_s_at_tn.png
| Function = {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0019901 |text = protein kinase binding}}
| Component = {{GNF_GO|id=GO:0008305 |text = integrin complex}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0006915 |text = apoptosis}} {{GNF_GO|id=GO:0006954 |text = inflammatory response}} {{GNF_GO|id=GO:0007155 |text = cell adhesion}} {{GNF_GO|id=GO:0007159 |text = leukocyte adhesion}} {{GNF_GO|id=GO:0007160 |text = cell-matrix adhesion}} {{GNF_GO|id=GO:0007229 |text = integrin-mediated signaling pathway}} {{GNF_GO|id=GO:0007267 |text = cell-cell signaling}} {{GNF_GO|id=GO:0007275 |text = multicellular organismal development}} {{GNF_GO|id=GO:0008360 |text = regulation of cell shape}} {{GNF_GO|id=GO:0019735 |text = antimicrobial humoral response}} {{GNF_GO|id=GO:0030593 |text = neutrophil chemotaxis}} {{GNF_GO|id=GO:0050730 |text = regulation of peptidyl-tyrosine phosphorylation}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 3689
    | Hs_Ensembl = ENSG00000160255
    | Hs_RefseqProtein = NP_000202
    | Hs_RefseqmRNA = NM_000211
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 21
    | Hs_GenLoc_start = 45130334
    | Hs_GenLoc_end = 45173181
    | Hs_Uniprot = P05107
    | Mm_EntrezGene = 16414
    | Mm_Ensembl = ENSMUSG00000000290
    | Mm_RefseqmRNA = NM_008404
    | Mm_RefseqProtein = NP_032430
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 10
    | Mm_GenLoc_start = 76985685
    | Mm_GenLoc_end = 77009099
    | Mm_Uniprot = Q542I8
  }}
}}
'''Integrin, beta 2 (complement component 3 receptor 3 and 4 subunit)''', also known as '''CD18''' or '''ITGB2''', is a human [[gene]].
 
'''CD18''' is the beta subunit of three different structures:  
* [[LFA-1]] (paired with [[CD11a]])
* [[LFA-1]] (paired with [[CD11a]])
* [[Macrophage-1 antigen]] (paired with [[CD11b]])
* [[Macrophage-1 antigen]] (paired with [[CD11b]])
* [[Integrin alphaXbeta2]] (paired with [[CD11c]])
* [[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.<ref>{{cite web | title = Entrez Gene: ITGB2 integrin, beta 2 (complement component 3 receptor 3 and 4 subunit)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3689| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
== Clinical significance==
{{PBB_Summary
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.<ref>{{cite journal|last1=Gjelstrup|first1=L. C.|last2=Boesen|first2=T.|last3=Kragstrup|first3=T. W.|last4=Jorgensen|first4=A.|last5=Klein|first5=N. J.|last6=Thiel|first6=S.|last7=Deleuran|first7=B. W.|last8=Vorup-Jensen|first8=T.|title=Shedding of Large Functionally Active CD11/CD18 Integrin Complexes from Leukocyte Membranes during Synovial Inflammation Distinguishes Three Types of Arthritis through Differential Epitope Exposure|journal=The Journal of Immunology|date=8 September 2010|volume=185|issue=7|pages=4154–4168|doi=10.4049/jimmunol.1000952}}</ref> The soluble beta 2 integrins are ligand binding and plasma levels are inversely associated with disease activity in the autoimmune disease spondyloarthritis.<ref>{{cite journal|last1=Kragstrup|first1=Tue W|last2=Jalilian|first2=Babak|last3=Hvid|first3=Malene|last4=Kjærgaard|first4=Anders|last5=Østgård|first5=René|last6=Schiøttz-Christensen|first6=Berit|last7=Jurik|first7=Anne G|last8=Robinson|first8=William H|last9=Vorup-Jensen|first9=Thomas|last10=Deleuran|first10=Bent|title=Decreased plasma levels of soluble CD18 link leukocyte infiltration with disease activity in spondyloarthritis|journal=Arthritis Research & Therapy|date=2014|volume=16|issue=1|pages=R42|doi=10.1186/ar4471}}</ref>
| section_title =  
| summary_text = 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.<ref>{{cite web | title = Entrez Gene: ITGB2 integrin, beta 2 (complement component 3 receptor 3 and 4 subunit)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3689| accessdate = }}</ref>
}}


==References==
== Interactions ==
{{reflist|2}}
CD18 has been shown to [[Protein-protein interaction|interact]] with:
==Further reading==
{{div col|colwidth=20em}}
{{refbegin | 2}}
* [[FHL2]],<ref name = pmid10906324>{{cite journal | vauthors = Wixler V, Geerts D, Laplantine E, Westhoff D, Smyth N, Aumailley M, Sonnenberg A, Paulsson M | title = The LIM-only protein DRAL/FHL2 binds to the cytoplasmic domain of several alpha and beta integrin chains and is recruited to adhesion complexes | journal = The Journal of Biological Chemistry | volume = 275 | issue = 43 | pages = 33669–78 | date = October 2000 | pmid = 10906324 | doi = 10.1074/jbc.M002519200 }}</ref>
{{PBB_Further_reading
* [[GNB2L1]],<ref name = pmid9442085>{{cite journal | vauthors = Liliental J, Chang DD | title = Rack1, a receptor for activated protein kinase C, interacts with integrin beta subunit | journal = The Journal of Biological Chemistry | volume = 273 | issue = 4 | pages = 2379–83 | date = Jan 1998 | pmid = 9442085 | doi =  10.1074/jbc.273.4.2379}}</ref>
| citations =  
* [[ICAM-1]],<ref name = pmid10352278>{{cite journal | vauthors = Kotovuori A, Pessa-Morikawa T, Kotovuori P, Nortamo P, Gahmberg CG | title = ICAM-2 and a peptide from its binding domain are efficient activators of leukocyte adhesion and integrin affinity | journal = Journal of Immunology | volume = 162 | issue = 11 | pages = 6613–20 | date = June 1999 | pmid = 10352278 | doi =  }}</ref><ref name = pmid11279101>{{cite journal | vauthors = Lu C, Takagi J, Springer TA | title = Association of the membrane proximal regions of the alpha and beta subunit cytoplasmic domains constrains an integrin in the inactive state | journal = The Journal of Biological Chemistry | volume = 276 | issue = 18 | pages = 14642–8 | date = May 2001 | pmid = 11279101 | doi = 10.1074/jbc.M100600200 }}</ref><ref name = pmid7642561>{{cite journal | vauthors = Huang C, Springer TA | title = 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) | journal = The Journal of Biological Chemistry | volume = 270 | issue = 32 | pages = 19008–16 | date = August 1995 | pmid = 7642561 | doi =  10.1074/jbc.270.32.19008}}</ref>  and
*{{cite journal | author=Bunting M, Harris ES, McIntyre TM, ''et al.'' |title=Leukocyte adhesion deficiency syndromes: adhesion and tethering defects involving beta 2 integrins and selectin ligands. |journal=Curr. Opin. Hematol. |volume=9 |issue= 1 |pages= 30-5 |year= 2002 |pmid= 11753075 |doi=  }}
* [[PSCD1]].<ref name = pmid9765275>{{cite journal | vauthors = Rietzler M, Bittner M, Kolanus W, Schuster A, Holzmann B | title = The human WD repeat protein WAIT-1 specifically interacts with the cytoplasmic tails of beta7-integrins | journal = The Journal of Biological Chemistry | volume = 273 | issue = 42 | pages = 27459–66 | date = October 1998 | pmid = 9765275 | doi =  10.1074/jbc.273.42.27459}}</ref><ref name = pmid10835351>{{cite journal | vauthors = Geiger C, Nagel W, Boehm T, van Kooyk Y, Figdor CG, Kremmer E, Hogg N, Zeitlmann L, Dierks H, Weber KS, Kolanus W | title = Cytohesin-1 regulates beta-2 integrin-mediated adhesion through both ARF-GEF function and interaction with LFA-1 | journal = The EMBO Journal | volume = 19 | issue = 11 | pages = 2525–36 | date = June 2000 | pmid = 10835351 | pmc = 212768 | doi = 10.1093/emboj/19.11.2525 }}</ref>
*{{cite journal | author=Roos D, Law SK |title=Hematologically important mutations: leukocyte adhesion deficiency. |journal=Blood Cells Mol. Dis. |volume=27 |issue= 6 |pages= 1000-4 |year= 2003 |pmid= 11831866 |doi= 10.1006/bcmd.2001.0473 }}
{{Div col end}}
*{{cite journal | author=Gahmberg CG, Fagerholm S |title=Activation of leukocyte beta2-integrins. |journal=Vox Sang. |volume=83 Suppl 1 |issue= |pages= 355-8 |year= 2003 |pmid= 12617168 |doi=  }}
*{{cite journal | author=Schymeinsky J, Mócsai A, Walzog B |title=Neutrophil activation via beta2 integrins (CD11/CD18): molecular mechanisms and clinical implications. |journal=Thromb. Haemost. |volume=98 |issue= 2 |pages= 262-73 |year= 2007 |pmid= 17721605 |doi=  }}
}}
{{refend}}


==See also==
== See also ==
* [[leukocyte adhesion deficiency]]
* [[leukocyte adhesion deficiency]]
* [[integrin]]
* [[integrin]]


==External links==
== References ==
{{reflist}}
 
== Further reading ==
{{refbegin | 2}}
* {{cite journal | vauthors = Bunting M, Harris ES, McIntyre TM, Prescott SM, Zimmerman GA | title = Leukocyte adhesion deficiency syndromes: adhesion and tethering defects involving beta 2 integrins and selectin ligands | journal = Current Opinion in Hematology | volume = 9 | issue = 1 | pages = 30–5 | date = Jan 2002 | pmid = 11753075 | doi = 10.1097/00062752-200201000-00006 }}
* {{cite journal | vauthors = Roos D, Law SK | title = Hematologically important mutations: leukocyte adhesion deficiency | journal = Blood Cells, Molecules & Diseases | volume = 27 | issue = 6 | pages = 1000–4 | year = 2003 | pmid = 11831866 | doi = 10.1006/bcmd.2001.0473 }}
* {{cite journal | vauthors = Gahmberg CG, Fagerholm S | title = Activation of leukocyte beta2-integrins | journal = Vox Sanguinis | volume = 83 Suppl 1 | issue =  | pages = 355–8 | date = August 2002 | pmid = 12617168 | doi = 10.1111/j.1423-0410.2002.tb05333.x }}
* {{cite journal | vauthors = Schymeinsky J, Mócsai A, Walzog B | title = Neutrophil activation via beta2 integrins (CD11/CD18): molecular mechanisms and clinical implications | journal = Thrombosis and Haemostasis | volume = 98 | issue = 2 | pages = 262–73 | date = August 2007 | pmid = 17721605 | doi = 10.1160/th07-02-0156 }}
{{refend}}
{{PDB Gallery|geneid=3689}}
 
== External links ==
* {{MeshName|CD18+antigen}}
* {{MeshName|CD18+antigen}}
*[http://cmkb.cellmigration.org/report.cgi?report=orth_overview&orth_acc=co00001789 ITGB2] Info with links in the [http://www.cellmigration.org/index.shtml Cell Migration Gateway]
* {{UCSC gene info|ITGB2}}


{{immunology-stub}}
{{Clusters of differentiation}}
{{Clusters of differentiation}}
{{Clusters of differentiation by lineage}}
{{Complement system}}
{{Complement system}}
{{Cell adhesion molecules}}
{{Integrins}}
{{Use dmy dates|date=April 2017}}
[[Category:Integrins]]
[[Category:Clusters of differentiation]]


[[ca:CD18]]
 
[[es:CD18]]
{{immunology-stub}}
{{WikiDoc Sources}}

Latest revision as of 21:32, 29 November 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

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]

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.[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 (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". 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 (June 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 (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)". 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 (October 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 (June 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 (August 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 (August 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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