|  Help  |  About  |  Contact Us

Publication : Expression of cathepsin proteinases by mouse trophoblast in vivo and in vitro.

First Author  Afonso S Year  1999
Journal  Dev Dyn Volume  216
Issue  4-5 Pages  374-84
PubMed ID  10633857 Mgi Jnum  J:58845
Mgi Id  MGI:1350499 Doi  10.1002/(SICI)1097-0177(199912)216:4/5<374::AID-DVDY6>3.0.CO;2-N
Citation  Afonso S, et al. (1999) Expression of cathepsin proteinases by mouse trophoblast in vivo and in vitro. Dev Dyn 216(4-5):374-84
abstractText  Implantation and placentation in the mouse requires successful invasion of the uterine wall by primary and secondary trophoblast giant cells. Their invasive nature depends in part on the upregulation of proteinases for the phagocytosis and extracellular digestion of maternal cells and matrix materials. The work reported here studies the expression of cathepsin proteinases during secondary trophoblast differentiation, and compares the expression patterns to fully differentiated day 8.5 primary trophoblast giant cells. Cathepsins B (CB), L (CL), and D (CD) were found to be upregulated during trophoblast differentiation in vivo at the message and protein level producing expression patterns equivalent to those of primary trophoblast. Invasive trophoblast cells expressed higher levels of the processed or active forms of the enzymes, coinciding with the period of trophoblast phagocytosis of maternal blood, decidual cells, and matrix materials. Trophoblast differentiation in vitro showed a similar upregulation of cathepsin enzymes. The enzymes were localized to heterogeneous vesicles that resembled both lysosomes and heterophagic vesicles. The presence of a large lysosomal population within the giant cells was confirmed by vital staining with acridine orange. Analysis of trophoblast-conditioned media also demonstrated secreted forms of CB and CL. The results suggest that cathepsin enzymes may contribute to trophoblast invasion not only through the intracellular breakdown of molecules phagocytosed by trophoblast cells, but also by the extracellular digestion of matrix molecules and activation of other pro-enzymes.
Quick Links:
 
Quick Links:
 

Expression

Publication --> Expression annotations

 

Other

4 Bio Entities

Trail: Publication

62 Expression

Trail: Publication