The role of serine proteases in gastrulation and early development in Xenopus laevis.

MGC116527, Xenopus laevis serine protease 27 (Prss27) and X. Laevis serine protease 8 (Prss8) belong to the superfamily of trypsin-like serine proteases. They have been shown to be involved in the development of the X. laevis. They cleave the epithelial sodium channel (ENaC), which is responsible fo...

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Bibliographic Details
Main Author: Ho Nurulain.
Other Authors: School of Biological Sciences
Format: Final Year Project
Language:English
Published: 2011
Subjects:
Online Access:http://hdl.handle.net/10356/45270
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Institution: Nanyang Technological University
Language: English
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Summary:MGC116527, Xenopus laevis serine protease 27 (Prss27) and X. Laevis serine protease 8 (Prss8) belong to the superfamily of trypsin-like serine proteases. They have been shown to be involved in the development of the X. laevis. They cleave the epithelial sodium channel (ENaC), which is responsible for maintaining the transmembrane potential across an embryo and overexpression of ion channels have been shown to interfere with development. In this thesis, we describe their spatio-temporal expression pattern and the effect of overexpressing or ablating their expression. MGC11527, Prss27 and Prss8 are expressed at all stages, mainly restricted to the ectoderm. Prss27 expression was also localised to the hatching gland, indicating a role in the hatching process.