| First Author | Sol-Church K | Year | 2000 |
| Journal | Biochim Biophys Acta | Volume | 1491 |
| Issue | 1-3 | Pages | 289-94 |
| PubMed ID | 10760593 | Mgi Jnum | J:65735 |
| Mgi Id | MGI:1927202 | Doi | 10.1016/s0167-4781(00)00030-0 |
| Citation | Sol-Church K, et al. (2000) Mouse cathepsin M, a placenta-specific lysosomal cysteine protease related to cathepsins L and P. Biochim Biophys Acta 1491(1-3):289-94 |
| abstractText | The complete nucleotide sequence of a novel cathepsin cDNA derived from mouse placenta was determined and is termed cathepsin M. The predicted protein of 333 amino acid is a member of the family C1A proteases and is related to mouse cathepsins L and P. Mouse cathepsin M is highly expressed in placenta, whereas no detectable levels were found in lung, spleen, heart, brain, kidney, thymus, testicle, liver, or embryo. Phylogenic analyses of the sequences of human and mouse cathepsins show that cathepsin M is most closely related to cathepsins P and L. However, the differences are sufficiently large to indicate that the enzymes will be found in other species. This is in contrast to human cathepsins L and V, which probably resulted from a gene duplication after divergence of mammalian species. |
