Expression of Cathepsin P mRNA, Protein and Activity in the Rat Choriocarcinoma Cell Line, Rcho-1, During Giant Cell Transformation

Abstract

Lysosomal proteases perform critical functions in protein turnover and are essential for normal growth and development. Cathepsin P is a member of a newly discovered family of lysosomal cysteine proteases uniquely expressed in rodent placenta (PECs), and is closely related to human cathepsin L. Using the rat choriocarcinoma cell line model, Rcho-1, mRNA for the PECs cathepsins P, M, Q, R, 1, 2 was found to increase in expression during differentiation into a trophoblast giant cell phenotype. By contrast, expression of cathepsin L was not regulated. A specific enzyme assay was developed to show that activity of cathepsin P mirrored mRNA expression during differentiation. Cathepsin P protein co-localizes with cathepsin B, indicating that the enzyme probably functions in the endosomal-lysosomal compartment. This study demonstrates that the PEC genes produce functional proteases that can perform specific placental roles that are probably performed by broader specificity proteases in human placenta.

Effects of dietary n-3-PUFA supplementation, post-insemination plane of nutrition and pregnancy status on the endometrial transcriptome of beef heifers

“…Expression of Cathepsin V was 1.5 fold lower in heifers on the control diet compared to n-3 PUFA supplemented heifers. Administration of leupeptin, an inhibitor of Cathepsin V , to rats on Day 4–5 embryos, completely blocked implantation of these embryos 31 . Cathepsin has also been demonstrated as having a potential role in the remodelling of endometrial cells in the porcine uterus and placenta 32 .…”

Brentuximab vedotin exerts profound antiproliferative and pro‐apoptotic efficacy in CD30‐positive as well as cocultured CD30‐negative germ cell tumour cell lines

“…Slight antiproliferative and pro-apoptotic effects at this concentration after 96 hrs occur most likely due to successive hydrolytic release of the tubulin-toxin MMAE. Of note, expression of different cathepsins known to mediate MMAE cleavage from the ADC is observed in a rodent choriocarcinoma cell line [17].…”