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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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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spelling sg-ntu-dr.10356-452702023-02-28T18:00:00Z The role of serine proteases in gastrulation and early development in Xenopus laevis. Ho Nurulain. School of Biological Sciences A*STAR Institute of Medical Biology Thomas R. Keeble C.Michael Jones DRNTU::Science::Biological sciences::Zoology::Embryology 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. Bachelor of Science in Biological Sciences 2011-06-10T06:32:04Z 2011-06-10T06:32:04Z 2011 2011 Final Year Project (FYP) http://hdl.handle.net/10356/45270 en Nanyang Technological University 53 p. application/pdf
institution Nanyang Technological University
building NTU Library
continent Asia
country Singapore
Singapore
content_provider NTU Library
collection DR-NTU
language English
topic DRNTU::Science::Biological sciences::Zoology::Embryology
spellingShingle DRNTU::Science::Biological sciences::Zoology::Embryology
Ho Nurulain.
The role of serine proteases in gastrulation and early development in Xenopus laevis.
description 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.
author2 School of Biological Sciences
author_facet School of Biological Sciences
Ho Nurulain.
format Final Year Project
author Ho Nurulain.
author_sort Ho Nurulain.
title The role of serine proteases in gastrulation and early development in Xenopus laevis.
title_short The role of serine proteases in gastrulation and early development in Xenopus laevis.
title_full The role of serine proteases in gastrulation and early development in Xenopus laevis.
title_fullStr The role of serine proteases in gastrulation and early development in Xenopus laevis.
title_full_unstemmed The role of serine proteases in gastrulation and early development in Xenopus laevis.
title_sort role of serine proteases in gastrulation and early development in xenopus laevis.
publishDate 2011
url http://hdl.handle.net/10356/45270
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