ICAM2
Intercellular adhesion molecule 2 | |||||||||||||
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PDB rendering based on 1zxq. | |||||||||||||
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Identifiers | |||||||||||||
Symbols | ICAM2 ; CD102 | ||||||||||||
External IDs | OMIM: 146630 MGI: 96394 HomoloGene: 675 GeneCards: ICAM2 Gene | ||||||||||||
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RNA expression pattern | |||||||||||||
More reference expression data | |||||||||||||
Orthologs | |||||||||||||
Species | Human | Mouse | |||||||||||
Entrez | 3384 | 15896 | |||||||||||
Ensembl | ENSG00000108622 | ENSMUSG00000001029 | |||||||||||
UniProt | P13598 | P35330 | |||||||||||
RefSeq (mRNA) | NM_000873 | NM_010494 | |||||||||||
RefSeq (protein) | NP_000864 | NP_034624 | |||||||||||
Location (UCSC) |
Chr 17: 64 – 64.02 Mb |
Chr 11: 106.38 – 106.39 Mb | |||||||||||
PubMed search | |||||||||||||
Intercellular adhesion molecule 2 (ICAM2), also known as CD102 (Cluster of Differentiation 102), is a human gene, and the protein resulting from it.
Protein structure
The protein encoded by this gene is a member of the intercellular adhesion molecule (ICAM) family. All ICAM proteins are type I transmembrane glycoproteins, contain 2–9 immunoglobulin-like C2-type domains, and bind to the leukocyte adhesion LFA-1 protein.
Protein functions
ICAM-2 molecules regulate spermatid adhesion on Sertori cell on the apical side of the blood-testis barrier (towards the lumen), thus playing a major role in spermatogenesis.[1]
This protein may also play a role in lymphocyte recirculation by blocking LFA-1-dependent cell adhesion. It mediates adhesive interactions important for antigen-specific immune response, NK-cell mediated clearance, lymphocyte recirculation, and other cellular interactions important for immune response and surveillance.[2]
Interactions
ICAM2 has been shown to interact with EZR.[3]
See also
References
- ↑ Xiao, X.; Mruk, D. D.; Cheng, C. Y. (2013). "Intercellular adhesion molecules (ICAMs) and spermatogenesis". Human Reproduction Update 19 (2): 167–186. doi:10.1093/humupd/dms049. PMC 3576004. PMID 23287428.
- ↑ "Entrez Gene: ICAM2 intercellular adhesion molecule 2".
- ↑ Heiska, L; Alfthan K; Grönholm M; Vilja P; Vaheri A; Carpén O (Aug 1998). "Association of ezrin with intercellular adhesion molecule-1 and −2 (ICAM-1 and ICAM-2). Regulation by phosphatidylinositol 4, 5-bisphosphate". J. Biol. Chem. (UNITED STATES) 273 (34): 21893–900. doi:10.1074/jbc.273.34.21893. ISSN 0021-9258. PMID 9705328.
Further reading
- Simmons DL (1995). "The role of ICAM expression in immunity and disease.". Cancer Surv. 24: 141–55. PMID 7553659.
- Hayflick JS, Kilgannon P, Gallatin WM (1998). "The intercellular adhesion molecule (ICAM) family of proteins. New members and novel functions.". Immunol. Res. 17 (3): 313–27. doi:10.1007/BF02786454. PMID 9638475.
- Lalor PF, Shields P, Grant A, Adams DH (2002). "Recruitment of lymphocytes to the human liver.". Immunol. Cell Biol. 80 (1): 52–64. doi:10.1046/j.1440-1711.2002.01062.x. PMID 11869363.
- Yonekawa K, Harlan JM (2005). "Targeting leukocyte integrins in human diseases.". J. Leukoc. Biol. 77 (2): 129–40. doi:10.1189/jlb.0804460. PMID 15548573.
- de Fougerolles AR, Stacker SA, Schwarting R, Springer TA (1991). "Characterization of ICAM-2 and evidence for a third counter-receptor for LFA-1.". J. Exp. Med. 174 (1): 253–67. doi:10.1084/jem.174.1.253. PMC 2118873. PMID 1676048.
- Sansom D, Borrow J, Solomon E, Trowsdale J (1992). "The human ICAM2 gene maps to 17q23-25.". Genomics 11 (2): 462–4. doi:10.1016/0888-7543(91)90157-A. PMID 1769660.
- Staunton DE, Dustin ML, Springer TA (1989). "Functional cloning of ICAM-2, a cell adhesion ligand for LFA-1 homologous to ICAM-1.". Nature 339 (6219): 61–4. doi:10.1038/339061a0. PMID 2497351.
- Bujía J, Holly A, Kim C, et al. (1994). "Expression of human intercellular adhesion molecules in middle ear cholesteatoma.". Am J Otolaryngol 15 (4): 271–5. doi:10.1016/0196-0709(94)90094-9. PMID 7526720.
- de Fougerolles AR, Qin X, Springer TA (1994). "Characterization of the function of intercellular adhesion molecule (ICAM)-3 and comparison with ICAM-1 and ICAM-2 in immune responses.". J. Exp. Med. 179 (2): 619–29. doi:10.1084/jem.179.2.619. PMC 2191386. PMID 7905020.
- Butini L, De Fougerolles AR, Vaccarezza M, et al. (1994). "Intercellular adhesion molecules (ICAM)-1 ICAM-2 and ICAM-3 function as counter-receptors for lymphocyte function-associated molecule 1 in human immunodeficiency virus-mediated syncytia formation.". Eur. J. Immunol. 24 (9): 2191–5. doi:10.1002/eji.1830240939. PMID 7916296.
- Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides.". Gene 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
- Hirao M, Sato N, Kondo T, et al. (1996). "Regulation mechanism of ERM (ezrin/radixin/moesin) protein/plasma membrane association: possible involvement of phosphatidylinositol turnover and Rho-dependent signaling pathway.". J. Cell Biol. 135 (1): 37–51. doi:10.1083/jcb.135.1.37. PMC 2121020. PMID 8858161.
- Bernstein CN, Sargent M, Gallatin WM, Wilkins J (1996). "Beta 2-integrin/intercellular adhesion molecule (ICAM) expression in the normal human intestine.". Clin. Exp. Immunol. 106 (1): 160–9. PMID 8870715.
- Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery.". Genome Res. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548.
- Casasnovas JM, Springer TA, Liu JH; et al. (1997). "Crystal structure of ICAM-2 reveals a distinctive integrin recognition surface.". Nature 387 (6630): 312–5. doi:10.1038/387312a0. PMID 9153399.
- Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library.". Gene 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
- Sainio M, Zhao F, Heiska L, et al. (1997). "Neurofibromatosis 2 tumor suppressor protein colocalizes with ezrin and CD44 and associates with actin-containing cytoskeleton.". J. Cell. Sci. 110. ( Pt 18): 2249–60. PMID 9378774.
- Yonemura S, Hirao M, Doi Y, et al. (1998). "Ezrin/radixin/moesin (ERM) proteins bind to a positively charged amino acid cluster in the juxta-membrane cytoplasmic domain of CD44, CD43, and ICAM-2.". J. Cell Biol. 140 (4): 885–95. doi:10.1083/jcb.140.4.885. PMC 2141743. PMID 9472040.
- Bernstein CN, Sargent M, Gallatin WM (1998). "Beta2 integrin/ICAM expression in Crohn's disease.". Clin. Immunol. Immunopathol. 86 (2): 147–60. doi:10.1006/clin.1997.4462. PMID 9473377.
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External links
- ICAM2 protein, human at the US National Library of Medicine Medical Subject Headings (MeSH)
This article incorporates text from the United States National Library of Medicine, which is in the public domain.
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