| First Author | LeBleu V | Year | 2010 |
| Journal | J Biol Chem | Volume | 285 |
| Issue | 53 | Pages | 41874-85 |
| PubMed ID | 20847057 | Mgi Jnum | J:167404 |
| Mgi Id | MGI:4868174 | Doi | 10.1074/jbc.M110.149534 |
| Citation | LeBleu V, et al. (2010) Identification of the NC1 domain of {alpha}3 chain as critical for {alpha}3{alpha}4{alpha}5 type IV collagen network assembly. J Biol Chem 285(53):41874-85 |
| abstractText | The network organization of type IV collagen consisting of alpha3, alpha4, and alpha5 chains in the glomerular basement membrane (GBM) is speculated to involve interactions of the triple helical and NC1 domain of individual alpha-chains, but in vivo evidence is lacking. To specifically address the contribution of the NC1 domain in the GBM collagen network organization, we generated a mouse with specific loss of alpha3NC1 domain while keeping the triple helical alpha3 chain intact by connecting it to the human alpha5NC1 domain. The absence of alpha3NC1 domain leads to the complete loss of the alpha4 chain. The alpha3 collagenous domain is incapable of incorporating the alpha5 chain, resulting in the impaired organization of the alpha3alpha4alpha5 chain-containing network. Although the alpha5 chain can assemble with the alpha1, alpha2, and alpha6 chains, such assembly is incapable of functionally replacing the alpha3alpha4alpha5 protomer. This novel approach to explore the assembly type IV collagen in vivo offers novel insights in the specific role of the NC1 domain in the assembly and function of GBM during health and disease. |
