JAM3 explained

Junctional adhesion molecule C is a protein that in humans is encoded by the JAM3 gene.^[1]

Gene

This gene is located on the long arm of chromosome 11 (11q25) on the Watson strand. It is 83,077 bases in length. The encoded protein is 310 amino acids long with a predicted molecular weight of 35.02 kilodaltons.

Function

Tight junctions represent one mode of cell-to-cell adhesion in epithelial or endothelial cell sheets, forming continuous seals around cells and serving as a physical barrier to prevent solutes and water from passing freely through the paracellular space. The protein encoded by this immunoglobulin superfamily gene member is localized in the tight junctions between high endothelial cells. Unlike other proteins in this family, this protein is unable to adhere to leukocyte cell lines and only forms weak homotypic interactions. The encoded protein is a member of the junctional adhesion molecule protein family and acts as a receptor for another member of this family.^[1]

Interactions

JAM3 has been shown to interact with PARD3.^[2]

Clinical significance

Loss-of-function mutations in this gene cause a rare syndrome - autosomal recessive hemorrhagic destruction of the brain, subependymal calcification and congenital cataracts.^[3]

Further reading

• Muller WA . Leukocyte-endothelial-cell interactions in leukocyte transmigration and the inflammatory response. . Trends Immunol. . 24 . 6 . 327–34 . 2003 . 12810109 . 10.1016/S1471-4906(03)00117-0 .
• Maruyama K, Sugano S . Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. . Gene . 138 . 1–2 . 171–4 . 1994 . 8125298 . 10.1016/0378-1119(94)90802-8 .
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, etal . Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. . Gene . 200 . 1–2 . 149–56 . 1997 . 9373149 . 10.1016/S0378-1119(97)00411-3 .
• Arrate MP, Rodriguez JM, Tran TM, etal . Cloning of human junctional adhesion molecule 3 (JAM3) and its identification as the JAM2 counter-receptor. . J. Biol. Chem. . 276 . 49 . 45826–32 . 2002 . 11590146 . 10.1074/jbc.M105972200 . free .
• Aurrand-Lions M, Johnson-Leger C, Wong C, etal . Heterogeneity of endothelial junctions is reflected by differential expression and specific subcellular localization of the three JAM family members. . Blood . 98 . 13 . 3699–707 . 2002 . 11739175 . 10.1182/blood.V98.13.3699 . 29405220 . free .
• Liang TW, Chiu HH, Gurney A, etal . Vascular endothelial-junctional adhesion molecule (VE-JAM)/JAM 2 interacts with T, NK, and dendritic cells through JAM 3. . J. Immunol. . 168 . 4 . 1618–26 . 2002 . 11823489 . 10.4049/jimmunol.168.4.1618. free .
• Phillips HM, Renforth GL, Spalluto C, etal . Narrowing the critical region within 11q24-qter for hypoplastic left heart and identification of a candidate gene, JAM3, expressed during cardiogenesis. . Genomics . 79 . 4 . 475–8 . 2002 . 11944976 . 10.1006/geno.2002.6742 .
• Cunningham SA, Rodriguez JM, Arrate MP, etal . JAM2 interacts with alpha4beta1. Facilitation by JAM3. . J. Biol. Chem. . 277 . 31 . 27589–92 . 2002 . 12070135 . 10.1074/jbc.C200331200 . free .
• Santoso S, Sachs UJ, Kroll H, etal . The junctional adhesion molecule 3 (JAM-3) on human platelets is a counterreceptor for the leukocyte integrin Mac-1. . J. Exp. Med. . 196 . 5 . 679–91 . 2002 . 12208882 . 10.1084/jem.20020267 . 2194005 .
• Strausberg RL, Feingold EA, Grouse LH, etal . Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. . Proc. Natl. Acad. Sci. U.S.A. . 99 . 26 . 16899–903 . 2003 . 12477932 . 10.1073/pnas.242603899 . 139241 . 2002PNAS...9916899M . free .
• Ebnet K, Aurrand-Lions M, Kuhn A, etal . The junctional adhesion molecule (JAM) family members JAM-2 and JAM-3 associate with the cell polarity protein PAR-3: a possible role for JAMs in endothelial cell polarity. . J. Cell Sci. . 116 . Pt 19 . 3879–91 . 2004 . 12953056 . 10.1242/jcs.00704 . free .
• Clark HF, Gurney AL, Abaya E, etal . The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. . Genome Res. . 13 . 10 . 2265–70 . 2003 . 12975309 . 10.1101/gr.1293003 . 403697 .
• Ota T, Suzuki Y, Nishikawa T, etal . Complete sequencing and characterization of 21,243 full-length human cDNAs. . Nat. Genet. . 36 . 1 . 40–5 . 2004 . 14702039 . 10.1038/ng1285 . free .
• Zen K, Babbin BA, Liu Y, etal . JAM-C is a component of desmosomes and a ligand for CD11b/CD18-mediated neutrophil transepithelial migration. . Mol. Biol. Cell . 15 . 8 . 3926–37 . 2005 . 15194813 . 10.1091/mbc.E04-04-0317 . 491847 .
• Zhang Z, Henzel WJ . Signal peptide prediction based on analysis of experimentally verified cleavage sites. . Protein Sci. . 13 . 10 . 2819–24 . 2005 . 15340161 . 10.1110/ps.04682504 . 2286551 .
• Chavakis T, Keiper T, Matz-Westphal R, etal . The junctional adhesion molecule-C promotes neutrophil transendothelial migration in vitro and in vivo. . J. Biol. Chem. . 279 . 53 . 55602–8 . 2005 . 15485832 . 10.1074/jbc.M404676200 . free .
• Gerhard DS, Wagner L, Feingold EA, etal . The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). . Genome Res. . 14 . 10B . 2121–7 . 2004 . 15489334 . 10.1101/gr.2596504 . 528928 .
• Aurrand-Lions M, Lamagna C, Dangerfield JP, etal . Junctional adhesion molecule-C regulates the early influx of leukocytes into tissues during inflammation. . J. Immunol. . 174 . 10 . 6406–15 . 2005 . 15879142 . 10.4049/jimmunol.174.10.6406. free .
• Santoso S, Orlova VV, Song K, etal . The homophilic binding of junctional adhesion molecule-C mediates tumor cell-endothelial cell interactions. . J. Biol. Chem. . 280 . 43 . 36326–33 . 2006 . 16118203 . 10.1074/jbc.M505059200 . free .

Notes and References

1. Web site: Entrez Gene: JAM3 junctional adhesion molecule 3.
2. Ebnet K, Aurrand-Lions M, Kuhn A, Kiefer F, Butz S, Zander K, Meyer zu Brickwedde MK, Suzuki A, Imhof BA, Vestweber D . The junctional adhesion molecule (JAM) family members JAM-2 and JAM-3 associate with the cell polarity protein PAR-3: a possible role for JAMs in endothelial cell polarity . J. Cell Sci. . 116 . Pt 19 . 3879–91 . October 2003 . 12953056 . 10.1242/jcs.00704 . free .
3. Akawi NA, Canpolat FE, White SM, Quilis-Esquerra J, Sanchez MM, Gamundi MJ, Mochida GH, Walsh CA, Ali BR, Al-Gazali L . Delineation of the Clinical, Molecular and Cellular Aspects of Novel JAM3 Mutations Underlying the Autosomal Recessive Hemorrhagic Destruction of the Brain, Subependymal Calcification and Congenital Cataracts . Hum. Mutat. . 34. 3. 498–505. December 2012 . 23255084 . 10.1002/humu.22263 . 3951164.