| First Author | Kang LI | Year | 2007 |
| Journal | Int J Biochem Cell Biol | Volume | 39 |
| Issue | 3 | Pages | 576-85 |
| PubMed ID | 17118692 | Mgi Jnum | J:129577 |
| Mgi Id | MGI:3769812 | Doi | 10.1016/j.biocel.2006.10.016 |
| Citation | Kang LI, et al. (2007) Deletion of JAM-A causes morphological defects in the corneal epithelium. Int J Biochem Cell Biol 39(3):576-85 |
| abstractText | Junctional adhesion molecule-A (JAM-A, JAM-1, F11R) is an Ig domain containing transmembrane protein that has been proposed to function in diverse processes including platelet activation and adhesion, leukocyte transmigration, angiogenesis, epithelial cell shape and endothelial cell migration although its function in vivo is less well established. In the mouse eye, JAM-A protein expression is first detected at 12.5 dpc in the blood vessels of the tunica vasculosa, while it is first detected in both the corneal epithelium and lens between 13.5 and 14.5 dpc. In the corneal epithelium, JAM-A levels remain appreciable throughout life, while JAM-A immunostaining becomes stronger in the lens as the animals age. Both the cornea and lens of mice lacking an intact JAM-A gene are transparent until at least a year of age, although the cells of the JAM-A null corneal epithelium are irregularly shaped. In wild-type mice, JAM-A protein is found at the leading edge of repairing corneal epithelial wounds, however, corneal epithelial wound repair was qualitatively normal in JAM-A null animals. In summary, JAM-A is expressed in the corneal epithelium where it appears to regulate cell shape. |
