of the protein patterns overall, rather than a single change in an amino acid. Western blots confirmed the results, according to the researchers, though the changes in proteins were not as obvious in their protocol. The main significance to these findings are that JNJ460 are NGF are distinct processes that both control the protein output of the cell. JNJ460 resulted in increased neuronal size and stability while NGF resulted in increased membrane proteins. When combined, they significantly increase a neuron’s chance of growth. While JNJ460 may “prime” some parts of the cell for NGF treatment, they do not work together. JNJ460 is thought to interact with Schwann cells in regenerating actin and myosin, which are key players in axonal growth. NGF helps the neuron grow as a whole. These two proteins do not play a part in communication with other neurons, however. They merely increase the size of the membrane down which a signal can be sent. Other neurotrophic factor proteomes are needed to guide neurons to each other to create synapses. Limitations The broad scope of the available raw neuronal proteins to map requires that initial studies be focused on small areas of the neurons. When taking samples, there are a few places that interest neurologists most. The most important place to start for neurologists is the plasma membrane. This is where most of the communication between neurons takes place. The proteins being mapped here include ion channels, neurotransmitter receptors, and molecule transporters. Along the plasma membrane, the proteins involved in creating cholesterol-rich lipid rafts are being studied because they have been shown to be crucial for glutamate uptake during the initial stages of neuron formation. As mentioned before, vesicle proteins are also being studied closely because they are involved in disease. Collecting samples to study, however, requires special consideration to ensure that the reproducibility of the samples is not compromised. When taking a global sample of one area of the brain for example, proteins that are ubiquitous and relatively unimportant show up very clear in the SDS PAGE. Other unexplored, more specific proteins barely show up and are therefore ignored. It is usually necessary to divide up the plasma membrane proteome, for example, into subproteomes characterized by specific function. This allows these more specific classes of peptides to show up more clearly. In a way, dividing into subproteomes is simply applying a magnifying lens to a specific section