ICAM2
From Wikipedia, the free encyclopedia
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Intercellular adhesion molecule 2
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| PDB rendering based on 1zxq. | ||||||||||||||
| Available structures: 1zxq | ||||||||||||||
| Identifiers | ||||||||||||||
| Symbol(s) | ICAM2; CD102 | |||||||||||||
| External IDs | OMIM: 146630 MGI: 96394 HomoloGene: 675 | |||||||||||||
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| RNA expression pattern | ||||||||||||||
| Orthologs | ||||||||||||||
| Human | Mouse | |||||||||||||
| Entrez | 3384 | 15896 | ||||||||||||
| Ensembl | ENSG00000108622 | ENSMUSG00000001029 | ||||||||||||
| Uniprot | P13598 | P35330 | ||||||||||||
| Refseq | NM_000873 (mRNA) NP_000864 (protein) |
NM_010494 (mRNA) NP_034624 (protein) |
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| Location | Chr 17: 59.43 - 59.45 Mb | Chr 11: 106.19 - 106.2 Mb | ||||||||||||
| Pubmed search | [1] | [2] | ||||||||||||
Intercellular adhesion molecule 2 (ICAM2), also known as CD102 (Cluster of Differentiation 102), is a human gene.
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. This protein may 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.[1]
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[edit] See also
[edit] References
[edit] 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. 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. PMID 11869363.
- Yonekawa K, Harlan JM (2005). "Targeting leukocyte integrins in human diseases.". J. Leukoc. Biol. 77 (2): 129–40. doi:. 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. PMID 1676048.
- Sansom D, Borrow J, Solomon E, Trowsdale J (1992). "The human ICAM2 gene maps to 17q23-25.". Genomics 11 (2): 462–4. 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:. 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. 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. 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. 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. 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. 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. 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:. 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. 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. PMID 9472040.
- Bernstein CN, Sargent M, Gallatin WM (1998). "Beta2 integrin/ICAM expression in Crohn's disease.". Clin. Immunol. Immunopathol. 86 (2): 147–60. PMID 9473377.
[edit] External links
This article incorporates text from the United States National Library of Medicine, which is in the public domain.

