| First Author | Kurkinen M | Year | 1985 |
| Journal | Nature | Volume | 317 |
| Issue | 6033 | Pages | 177-9 |
| PubMed ID | 3839908 | Mgi Jnum | J:20208 |
| Mgi Id | MGI:68317 | Doi | 10.1038/317177a0 |
| Citation | Kurkinen M, et al. (1985) Characterization of 64-, 123- and 182-base-pair exons in the mouse alpha 2(IV) collagen gene. Nature 317(6033):177-9 |
| abstractText | Genes encoding types I, II and III collagens (fibrillar collagens) contain many discrete-size exons, most of them 54 base pairs (bp) long, in addition to the 45-, 99-, 108- and 162-bp exons. It has been suggested that these collagen genes evolved from an ancestral coding unit of 54 bp. Type IV collagen is a specific component of basement membranes and contains two genetically distinct polypeptides, the alpha 1(IV) and alpha 2(IV) chains. It differs from the types I-III collagens in that it contains interruptions in the Gly-X-Y repeat sequence and does not form ordered fibrillar structures. We have isolated complementary DNA and genomic clones for the mouse alpha 2(IV) collagen chain and here characterize 64-, 123- and 182-bp exons in the Gly-X-Y coding domain of the gene. The data suggest that the alpha 2(IV) collagen gene may have evolved differently from those encoding the fibrillar collagens. |
