| First Author | Miner JH | Year | 1999 |
| Journal | Int J Biochem Cell Biol | Volume | 31 |
| Issue | 8 | Pages | 811-6 |
| PubMed ID | 10481268 | Mgi Jnum | J:59494 |
| Mgi Id | MGI:1351729 | Doi | 10.1016/s1357-2725(99)00030-8 |
| Citation | Miner JH, et al. (1999) Laminin-11. Int J Biochem Cell Biol 31(8):811-6 |
| abstractText | Laminins are a family of glycoproteins which are ubiquitous components of basement membranes and play key structural and functional roles. Eleven isoforms have been identified to date; each is an alpha beta gamma heterotrimer assembled from a repertoire of five alpha, three beta and two gamma chains. Studies of laminin-11 (alpha 5 beta 2 gamma 1) illustrate the unique expression patterns and distinct functions that can be displayed by laminin isoforms. Laminin-11 is found in the glomerular basement membrane in kidney, in the neuromuscular synaptic cleft in skeletal muscle and in other tissues such as placenta and lung. Mice lacking laminin-11 exhibit defective glomerular filtration and developmental defects in neuromuscular synapse formation, with Schwann cells invading the synaptic cleft. Consistent with these observations, both motoneurons and Schwann cells distinguish laminin-11 from other isoforms in vitro. These results suggest that laminin-11 is a structural component of the basement membrane which influences cell behavior in physiologically relevant ways. A greater understanding of laminin-11 assembly and basement membrane incorporation could provide a logical basis for therapy in merosin-deficient congenital muscular dystrophy. |
