| First Author | Colognato H | Year | 2000 |
| Journal | Dev Dyn | Volume | 218 |
| Issue | 2 | Pages | 213-34 |
| PubMed ID | 10842354 | Mgi Jnum | J:62705 |
| Mgi Id | MGI:1859475 | Doi | 10.1002/(SICI)1097-0177(200006)218:2<213::AID-DVDY1>3.0.CO;2-R |
| Citation | Colognato H, et al. (2000) Form and function: the laminin family of heterotrimers. Dev Dyn 218(2):213-34 |
| abstractText | The laminins are a family of glycoproteins that provide an integral part of the structural scaffolding of basement membranes in almost every animal tissue. Each laminin is a heterotrimer assembled from alpha, beta, and gamma chain subunits, secreted and incorporated into cell-associated extracellular matrices. The laminins can self-assemble, bind to other matrix macromolecules, and have unique and shared cell interactions mediated by integrins, dystroglycan, and other receptors. Through these interactions, laminins critically contribute to cell differentiation, cell shape and movement, maintenance of tissue phenotypes, and promotion of tissue survival. Recent advances in the characterization of genetic disruptions in humans, mice, nematodes and flies have revealed developmental roles for the different laminin subunits in diverse cell types, affecting differentiation from blastocyst formation to the post-natal period. These genetic defects have challenged some of the previous concepts about basement membranes and have shed new light on the diversity and complexity of laminin functions as well as established the molecular basis of several human diseases. Copyright 2000 Wiley-Liss, Inc. |
