2-D Fluorescence Difference Gel Electrophoresis (DIGE) in Neuroproteomics

Review
In: Neuroproteomics. Boca Raton (FL): CRC Press/Taylor & Francis; 2010. Chapter 4.

Excerpt

The brain is of highest interest in biomedical research and in the pharmaceutical industry due to the appearance of widespread neurological diseases such as Alzheimer’s disease, Parkinson’s disease, Huntington’s disease, multiple sclerosis, and stroke. Research into protein function in the brain and its role in health and disease is advancing swiftly. In the past, research technology allowed the examination of only a few proteins at a time; however, it is rapidly becoming more common to examine simultaneously the expression of hundreds or even thousands of proteins (1). This enables a more holistic view for the comprehension of cellular processes. The importance of harnessing quantitative methodologies for the assessment of differences in protein expression is paramount. Thus, a growing body of work in neuroproteomics using two-dimensional fluorescence difference gel electrophoresis (2D-DIGE) is rapidly emerging, and a timely review of these data is warranted.

Why is it important for neuroscience research to examine thousands of proteins simultaneously? Although certain RNA molecules can act as effector molecules, proteins perform the majority of biological actions in the cell. Identifying the thousands of different proteins in a cell, the modifications to these proteins, along with their expressional level changes under different conditions, and all the protein-protein interactions is revolutionizing biology and medicine. There are many potential applications for proteomics in neuroscience (2). Comparative protein expression profiling and post-translational protein modification profiling are tasks that are best performed with DIGE.

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