Cooney, David (2011) Possible Interacting Proteins for Retinol Binding Protein and Cellular Retinol Binding Protein. Masters thesis, National University of Ireland Maynooth.

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Abstract

Retinol or vitamin A is crucial for many biological processes in the body such as proliferation, differentiation and reproduction. It is mainly stored in the liver and can be broken down to retinoic acid inside the cell. It travels in the circulatory system attached to Retinol Binding Protein (RBP) and its transport into the cell is mediated by the RBP receptor STRA6. Inside the cell, retinol binds to cellular Retinol Binding Protein (CRBP) and can be converted to retinoic acid, which can then act as a regulator of transcription. High levels of RBP have been implicated in type 2 diabetes. Looking for possible interacting partners for proteins such as RBP, can further elucidate the function of the protein and its possible role in type 2 diabetes. The Membrane Yeast Two Hybrid (MYTH) system allows for the study of possible interacting partners for membrane proteins. Previous studies using (MYTH) looked at possible interacting partners for RBP and CRBP. Two hits for RBP were G-protein coupled receptors (GPCRs) RAIG2 and RAIG3. One hit for CRBP was the TRPC4 ion channel. Retinoic acid inducible gene (RAIG) is a recently discovered family C GPCR and the TRPC4 channel is a membrane ion channel responsible for calcium and sodium ion influxes into the cell. An RBP-RAIG interaction could implicate the RAIG receptor in type 2 diabetes. A CRBP-TRPC4 interaction could activate the ion channel causing a calcium influx and a possible mechanism of insulin resistance in the cell, the genesis of which is still very controversial. This thesis involves performing a series of pull down assays using a novel oil-based assay to determine if the proteins in the yeast two hybrid system are indeed interacting.

Item Type:	Thesis (Masters)
Keywords:	Interacting Proteins; Retinol Binding Protein; Cellular Retinol Binding Protein;
Academic Unit:	Faculty of Science and Engineering > Biology
Item ID:	4001
Depositing User:	IR eTheses
Date Deposited:	22 Nov 2012 14:51
URI:
Use Licence:	This item is available under a Creative Commons Attribution Non Commercial Share Alike Licence (CC BY-NC-SA). Details of this licence are available here

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