| First Author | Timpl R | Year | 1996 |
| Journal | Bioessays | Volume | 18 |
| Issue | 2 | Pages | 123-32 |
| PubMed ID | 8851045 | Mgi Jnum | J:31490 |
| Mgi Id | MGI:78998 | Doi | 10.1002/bies.950180208 |
| Citation | Timpl R, et al. (1996) Supramolecular assembly of basement membranes. Bioessays 18(2):123-32 |
| abstractText | Basement membranes are thin sheets of extracellular proteins situated in close contact with cells at various locations in the body. They have a great influence on tissue compartmentalization and cellular phenotypes from early embryonic development onwards. The major constituents of all basement membranes are collagen IV and laminin, which both exist as multiple isoforms and each form a huge irregular network by self assembly. These networks are connected by nidogen, which also binds to several other components (proteoglycans, fibulins). Basement membranes are connected to cells by several receptors of the integrin family, which bind preferentially to laminins and collagen IV, and via some lectin-type interactions. The formation of basement membranes requires cooperation between different cell types since nidogen, for example, is usually synthesized by cells other than those exposed to the basement membranes. Thus many molecular interactions, of variable affinities, determine the final shape of basement membranes and their preferred subanatomical localization. |
