| First Author | Contente S | Year | 2009 |
| Journal | Biochim Biophys Acta | Volume | 1793 |
| Issue | 7 | Pages | 1272-8 |
| PubMed ID | 19410608 | Mgi Jnum | J:153482 |
| Mgi Id | MGI:4365521 | Doi | 10.1016/j.bbamcr.2009.04.013 |
| Citation | Contente S, et al. (2009) Tumor suppressive effect of lysyl oxidase proenzyme. Biochim Biophys Acta 1793(7):1272-8 |
| abstractText | Lysyl oxidase acts as both a matrix modifying enzyme and an oncogene suppressor. It is synthesized as a 50-kDa proenzyme, secreted, and processed into an approximately 30 kDa mature, active enzyme and an 18-kDa propeptide. The tumor suppressive effect of lysyl oxidase appears to be exerted within the cell, so the subcellular localization of protein forms was investigated. Propeptide-specific antibody detected 50-kDa proenzyme in cytoplasmic and nuclear extracts of non-transformed mouse fibroblasts, but free 18-kDa propeptide was not detected in any extract. Antibody to epitope near the N-terminus of mature lysyl oxidase detected the proenzyme product in non-transformed cells, and a 30-kDa cytoplasmic protein in both non-transformed and transformed cells. RNA interference reduced the expression of lysyl oxidase mRNA and 50-kDa proenzyme in non-transformed cells, but had no effect on 30-kDa protein, indicating that although this protein displays a lysyl oxidase epitope, it is not derived from lysyl oxidase message. The absence of both free 18-kDa propeptide and mature lysyl oxidase within non-transformed cells suggests that cellular reversion after restoration of lysyl oxidase gene expression is mediated by the 50-kDa proenzyme within cells. |
