| First Author | Sol-Church K | Year | 2000 |
| Journal | Biochem Biophys Res Commun | Volume | 267 |
| Issue | 3 | Pages | 791-5 |
| PubMed ID | 10673370 | Mgi Jnum | J:60138 |
| Mgi Id | MGI:1352900 | Doi | 10.1006/bbrc.1999.2051 |
| Citation | Sol-Church K, et al. (2000) Cathepsin Q, a novel lysosomal cysteine protease highly expressed in placenta. Biochem Biophys Res Commun 267(3):791-5 |
| abstractText | The complete nucleotide sequence of a novel cathepsin cDNA derived from rat placenta was determined and is termed cathepsin Q. The predicted protein of 343 amino acid is a member of the family C1A protease related to cathepsin L. Rat cathepsin Q and its mouse counterpart were found highly expressed in placenta, whereas no detectable levels were found in lung, spleen, heart, brain, kidney, thymus, testicle, liver, or embryonic tissues. It is predicted that cathepsin Q will differ in catalytic specificity to another placental-specific protease, cathepsin P, indicating that these enzymes will have unique proteolytic functions in extra-embryonic tissues. Copyright 2000 Academic Press. |
