CD18
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)
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.
Interactions
CD18 has been shown to interact with ICAM-1,[2][3][4] FHL2,[5] PSCD1[6][7] and GNB2L1.[8]
References
- ^ "Entrez Gene: ITGB2 integrin, beta 2 (complement component 3 receptor 3 and 4 subunit)". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3689.
- ^ Kotovuori, A; Pessa-Morikawa T, Kotovuori P, Nortamo P, Gahmberg C G (Jun. 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.
- ^ 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. doi:10.1074/jbc.M100600200. ISSN 0021-9258. PMID 11279101.
- ^ Huang, C; Springer T A (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)". J. Biol. Chem. (UNITED STATES) 270 (32): 19008–16. doi:10.1074/jbc.270.32.19008. ISSN 0021-9258. PMID 7642561.
- ^ 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". J. Biol. Chem. (UNITED STATES) 275 (43): 33669–78. doi:10.1074/jbc.M002519200. ISSN 0021-9258. PMID 10906324.
- ^ 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". J. Biol. Chem. (UNITED STATES) 273 (42): 27459–66. doi:10.1074/jbc.273.42.27459. ISSN 0021-9258. PMID 9765275.
- ^ 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 (Jun. 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. doi:10.1093/emboj/19.11.2525. ISSN 0261-4189. PMC 212768. PMID 10835351. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=212768.
- ^ Liliental, J; Chang D D (Jan. 1998). "Rack1, a receptor for activated protein kinase C, interacts with integrin beta subunit". J. Biol. Chem. (UNITED STATES) 273 (4): 2379–83. doi:10.1074/jbc.273.4.2379. ISSN 0021-9258. PMID 9442085.
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. doi:10.1097/00062752-200201000-00006. PMID 11753075.
- Roos D, Law SK (2003). "Hematologically important mutations: leukocyte adhesion deficiency.". Blood Cells Mol. Dis. 27 (6): 1000–4. doi:10.1006/bcmd.2001.0473. PMID 11831866.
- Gahmberg CG, Fagerholm S (2003). "Activation of leukocyte beta2-integrins.". Vox Sang. 83 Suppl 1: 355–8. PMID 12617168.
- 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.
| v · d · ePDB gallery | ||||
|---|---|---|---|---|
|
See also
External links
- MeSH CD18+antigen
- ITGB2 Info with links in the Cell Migration Gateway
| v · Proteins: clusters of differentiation (see also list of human clusters of differentiation) | |
|---|---|
| 1-50 |
CD1 (a-c, 1A, 1D, 1E) · CD2 · CD3 (γ, δ, ε) · CD4 · CD5 · CD6 · CD7 · CD8 (a) · CD9 · CD10 · CD11 (a, b, c) · CD13 · CD14 · CD15 · CD16 (A, B) · CD18 · CD19 · CD20 · CD21 · CD22 · CD23 · CD24 · CD25 · CD26 · CD27 · CD28 · CD29 · CD30 · CD31 · CD32 (A, B) · CD33 · CD34 · CD35 · CD36 · CD37 · CD38 · CD39 · CD40 · CD41 · CD42 (a, b, c, d) · CD43 · CD44 · CD45 · CD46 · CD47 · CD48 · CD49 (a, b, c, d, e, f) · CD50 |
| 51-100 |
CD51 · CD52 · CD53 · CD54 · CD55 · CD56 · CD57 · CD58 · CD59 · CD61 · CD62 (E, L, P) · CD63 · CD64 (A, B, C) · CD66 (a, b, c, d, e, f) · CD68 · CD69 · CD70 · CD71 · CD72 · CD73 · CD74 · CD78 · CD79 (a, b) · CD80 · CD81 · CD82 · CD83 · CD84 · CD85 (a, d, e, h, j, k) · CD86 · CD87 · CD88 · CD89 · CD90 · CD91- CD92 · CD93 · CD94 · CD95 · CD96 · CD97 · CD98 · CD99 · CD100 |
| 101-150 |
CD101 · CD102 · CD103 · CD104 · CD105 · CD106 · CD107 (a, b) · CD108 · CD109 · CD110 · CD111 · CD112 · CD113 · CD114 · CD115 · CD116 · CD117 · CD118 · CD119 · CD120 (a, b) · CD121 (a, b) · CD122 · CD123 · CD124 · CD125 · CD126 · CD127 · CD129 · CD130 · CD131 · CD132 · CD133 · CD134 · CD135 · CD136 · CD137 · CD138 · CD140b · CD141 · CD142 · CD143 · CD144 · CD146 · CD147 · CD148 · CD150 |
| 151-200 |
CD151 · CD152 · CD153 · CD154 · CD155 · CD156 (a, b, c) · CD157 · CD158 (a, d, e, i, k) · CD159 (a, c) · CD160 · CD161 · CD162 · CD163 · CD164 · CD166 · CD167 (a, b) · CD168 · CD169 · CD170 · CD171 · CD172 (a, b, g) · CD174 · CD177 · CD178 · CD179 (a, b) · CD181 · CD182 · CD183 · CD184 · CD185 · CD186 · CD191 · CD192 · CD193 · CD194 · CD195 · CD196 · CD197 · CDw198 · CDw199 · CD200 |
| 201-250 |
CD201 · CD202b · CD204 · CD205 · CD206 · CD207 · CD208 · CD209 · CDw210 (a, b) · CD212 · CD213a (1, 2) · CD217 · CD218 (a, b) · CD220 · CD221 · CD222 · CD223 · CD224 · CD225 · CD226 · CD227 · CD228 · CD229 · CD230 · CD233 · CD234 · CD235 (a, b) · CD236 · CD238 · CD239 · CD240CE · CD240D · CD241 · CD243 · CD244 · CD246 · CD247- CD248 · CD249 |
| 251-300 |
CD252 · CD253 · CD254 · CD256 · CD257 · CD258 · CD261 · CD262 · CD264 · CD265 · CD266 · CD267 · CD268 · CD269 · CD271 · CD272 · CD273 · CD274 · CD275 · CD276 · CD278 · CD279 · CD280 · CD281 · CD282 · CD283 · CD284 · CD286 · CD288 · CD289 · CD290 · CD292 · CDw293 · CD294 · CD295 · CD297 · CD298 · CD299 |
| 301-350 |
| v · Cluster of differentiation by lineage | |||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lymphoid |
|
||||||||||||||||
| Myeloid |
|
||||||||||||||||
| Stem cell | |||||||||||||||||
| v · d · eProteins: complement system (C, L, A) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Activators/enzymes |
|
||||||||
| Inhibitors | |||||||||
| Complement receptors | |||||||||
| v · Membrane proteins: cell adhesion molecules | |||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Calcium-independent |
|
||||||||||||||||
| Calcium-dependent |
|
||||||||||||||||
| Other |
Lymphocyte homing receptor: CD44 · L-selectin · integrin (VLA-4, LFA-1) Carcinoembryonic antigen · CD22 · CD24 · CD44 · CD146 · CD164 |
||||||||||||||||
|
see also cell membrane protein disorders |
| v · Integrins | |
|---|---|
| Alpha | |
| Beta | |
| Dimers |
Cytoadhesin receptor: Integrin alpha6beta4 · Glycoprotein IIb/IIIa (ITGA2B+ITGB3) Fibrinogen receptor: Macrophage-1 antigen (CD11b+CD18) Fibronectin receptor: Integrin alpha2beta1 · Integrin alpha4beta1 · Integrin alpha5beta1 Leukocyte-adhesion receptor: LFA-1 (CD11a+CD18) · Macrophage-1 antigen (CD11b+CD18) · Integrin alphaXbeta2 (CD11c+CD18) Very late antigen receptor: Integrin alpha1beta1 · Integrin alpha2beta1 · Integrin alpha3beta1 · VLA-4 (CD49d+CD29) · Alpha-5 beta-1 · Integrin alpha6beta1 Vitronectin receptor: Alpha-v beta-3 · Alpha-v beta-5 |
|
see also cell surface receptor deficiencies |