We are developing an affinity column to isolate insulin C-peptide binding proteins from cell lysates.  Isolated proteins will be separated by SDS-PAGE and identified by mass spectrometry through peptide mapping.

We are working on several proteomics projects involving cancer cells.  We are particularly interested in the structural analysis of the protein prohibitin in melanoma cells.

  The post-translational phosphorylation of proteins is important in regulating cellular signalling, and it is estimated that 1/3 of all proteins are phosphorylated.  We have been working on the development of a novel PhosphoTip that will allow for the isolation/enrichment of phosphorylated peptides and proteins.  In this way, we will be able to map cellular protein phosphorylation events. 

The aim of this study is to determine whether leptin has a direct effect on the post-translational modification of the β-subunit of the insulin receptor.  Insulin simultaneously stimulates the phosphorylation of some cellular proteins and the dephosphorylation of others.  This contradictory effect could be mediated through separate signaling transduction pathways.  Therefore, it may be possible to alter one effect without interfering with the other pathway(s) by phosphorylating key residues in the β-subunit.  It is my hypothesis that leptin binding to its receptor may activate a kinase that can phosphorylate the insulin receptor thus altering the effects of insulin.

 

 

We are working on the biological analysis of a molecule that may play a critical role in cholesterol metabolism. 

Identification of insulin C-peptide binding proteins

Analysis of Insulin Receptor Structure

Development of a Novel PhosphoTip

Cancer Projects

Cholesterol Metabolism

Project List

Structure of cholesterol

Christina injects a sample of

the insulin C-peptide into the LCQ mass spectrometer as part of her capstone project.