| First Author | Broder C | Year | 2013 |
| Journal | Proc Natl Acad Sci U S A | Volume | 110 |
| Issue | 35 | Pages | 14219-24 |
| PubMed ID | 23940311 | Mgi Jnum | J:200746 |
| Mgi Id | MGI:5509227 | Doi | 10.1073/pnas.1305464110 |
| Citation | Broder C, et al. (2013) Metalloproteases meprin alpha and meprin beta are C- and N-procollagen proteinases important for collagen assembly and tensile strength. Proc Natl Acad Sci U S A 110(35):14219-24 |
| abstractText | Type I fibrillar collagen is the most abundant protein in the human body, crucial for the formation and strength of bones, skin, and tendon. Proteolytic enzymes are essential for initiation of the assembly of collagen fibrils by cleaving off the propeptides. We report that Mep1a(-/-) and Mep1b(-/-) mice revealed lower amounts of mature collagen I compared with WT mice and exhibited significantly reduced collagen deposition in skin, along with markedly decreased tissue tensile strength. While exploring the mechanism of this phenotype, we found that cleavage of full-length human procollagen I heterotrimers by either meprin alpha or meprin beta led to the generation of mature collagen molecules that spontaneously assembled into collagen fibrils. Thus, meprin alpha and meprin beta are unique in their ability to process and release both C- and N-propeptides from type I procollagen in vitro and in vivo and contribute to the integrity of connective tissue in skin, with consequent implications for inherited connective tissue disorders. |
