Neurological function is based on the interactions of many proteins of different origin, and so requires a systematic study of subsystems within its proteomic structure.
For this technique, proteins are run across an immobile gel with a pH gradient until they stop at the point where their net charge is neutral.
This fact reveals a fault with current technology; new techniques are needed to increase both the specificity and scope of proteome mapping.
Lack of sensory communication in neurons is often an outward sign of drug abuse, and so neuroproteomics is being applied to find out what proteins are being affected to prevent the transport of neurotransmitters.
After significant morphine application, tyrosine kinases received less phosphorylation and thus send fewer signals inside the cell.
These receptor proteins are unable to initiate the intracellular signaling processes that enable the neuron to live, and necrosis or apoptosis may be the result.
With more and more neurons affected along this chain of cell death, permanent loss of sensory or motor function may be the result.
By identifying the proteins that are changed with drug abuse, neuroproteomics may give clinicians even earlier biomarkers to test for to prevent permanent neurological damage.
These glutamate receptors acidify the surrounding intracranial fluid, causing further injury on the molecular level to nearby neurons.
Three different cysteine protease derivatives are involved in the apoptotic pathway induced by the acidic environment triggered by glutamate.
These three proteins are examples of detectable signs of traumatic brain injury that are much more specific than temperature, oxygen level, or intracranial pressure.
Proteomics thus also offers a tracking mechanism by which researchers can monitor the progression of traumatic brain injury, or a chronic disease such as Alzheimer’s or Parkinson’s.
Especially in Parkinson’s, in which neurotransmitters play a large role, recent proteomic research has involved the study of synaptotagmin.
By studying the intracellular mechanisms involved in neural apoptosis after traumatic brain injury, researchers can create a map that genetic changes can follow later on.
One group of researchers applied the field of neuroproteomics to examine how different proteins affect the initial growth of neuritis.
A peptide mixture was made by washing off unbound portions of the amino acid sequence in a reverse column.
JNJ460 is thought to interact with Schwann cells in regenerating actin and myosin, which are key players in axonal growth.
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.
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.
In a way, dividing into subproteomes is simply applying a magnifying lens to a specific section of a global proteome’s SDS PAGE map.