Biology:ICAM2

Short description: Protein-coding gene in the species Homo sapiens

Generic protein structure example

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 Sertoli cell on the apical side of the blood-testis barrier (towards the lumen), thus playing a major role in spermatogenesis.

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.

Interactions

ICAM2 has been shown to interact with EZR. It has also been shown to bind to P9 (Uniprot: B2UM07), a secreted protein from Akkermansia muciniphila.

See also

• Cluster of differentiation

Further reading

• "The role of ICAM expression in immunity and disease". Cancer Surveys 24: 141–55. 1995. PMID 7553659. 
• "The intercellular adhesion molecule (ICAM) family of proteins. New members and novel functions". Immunologic Research 17 (3): 313–27. 1998. doi:10.1007/BF02786454. PMID 9638475. 
• "Recruitment of lymphocytes to the human liver". Immunology and Cell Biology 80 (1): 52–64. February 2002. doi:10.1046/j.1440-1711.2002.01062.x. PMID 11869363. 
• "Targeting leukocyte integrins in human diseases". Journal of Leukocyte Biology 77 (2): 129–40. February 2005. doi:10.1189/jlb.0804460. PMID 15548573. 
• "Characterization of ICAM-2 and evidence for a third counter-receptor for LFA-1". The Journal of Experimental Medicine 174 (1): 253–67. July 1991. doi:10.1084/jem.174.1.253. PMID 1676048. 
• "The human ICAM2 gene maps to 17q23-25". Genomics 11 (2): 462–4. October 1991. doi:10.1016/0888-7543(91)90157-A. PMID 1769660. 
• "Functional cloning of ICAM-2, a cell adhesion ligand for LFA-1 homologous to ICAM-1". Nature 339 (6219): 61–4. May 1989. doi:10.1038/339061a0. PMID 2497351. Bibcode: 1989Natur.339...61S. 
• "Expression of human intercellular adhesion molecules in middle ear cholesteatoma". American Journal of Otolaryngology 15 (4): 271–5. 1994. doi:10.1016/0196-0709(94)90094-9. PMID 7526720. 
• "Characterization of the function of intercellular adhesion molecule (ICAM)-3 and comparison with ICAM-1 and ICAM-2 in immune responses". The Journal of Experimental Medicine 179 (2): 619–29. February 1994. doi:10.1084/jem.179.2.619. PMID 7905020. 
• "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". European Journal of Immunology 24 (9): 2191–5. September 1994. doi:10.1002/eji.1830240939. PMID 7916296. 
• "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene 138 (1–2): 171–4. January 1994. doi:10.1016/0378-1119(94)90802-8. PMID 8125298. 
• "Regulation mechanism of ERM (ezrin/radixin/moesin) protein/plasma membrane association: possible involvement of phosphatidylinositol turnover and Rho-dependent signaling pathway". The Journal of Cell Biology 135 (1): 37–51. October 1996. doi:10.1083/jcb.135.1.37. PMID 8858161. 
• "Beta 2-integrin/intercellular adhesion molecule (ICAM) expression in the normal human intestine". Clinical and Experimental Immunology 106 (1): 160–9. October 1996. PMID 8870715. 
• "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Research 6 (9): 791–806. September 1996. doi:10.1101/gr.6.9.791. PMID 8889548. 
• "Crystal structure of ICAM-2 reveals a distinctive integrin recognition surface". Nature 387 (6630): 312–5. May 1997. doi:10.1038/387312a0. PMID 9153399. Bibcode: 1997Natur.387..312C. 
• "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene 200 (1–2): 149–56. October 1997. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149. 
• "Neurofibromatosis 2 tumor suppressor protein colocalizes with ezrin and CD44 and associates with actin-containing cytoskeleton". Journal of Cell Science. 110 110 (18): 2249–60. September 1997. doi:10.1242/jcs.110.18.2249. PMID 9378774. 
• "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". The Journal of Cell Biology 140 (4): 885–95. February 1998. doi:10.1083/jcb.140.4.885. PMID 9472040. 
• "Beta2 integrin/ICAM expression in Crohn's disease". Clinical Immunology and Immunopathology 86 (2): 147–60. February 1998. doi:10.1006/clin.1997.4462. PMID 9473377. 

External links

• ICAM2+protein,+human at the US National Library of Medicine Medical Subject Headings (MeSH)
• PDBe-KB provides an overview of all the structure information available in the PDB for Human Intercellular adhesion molecule 2 (ICAM2)

This article incorporates text from the United States National Library of Medicine, which is in the public domain.