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MELBOURNE researchers may have found a way to block the progression of multiple sclerosis (MS).

Blocking a specific protein responsible for nerve damage acted as a hand brake to progression of the disease, researchers from RMIT and Monash Universities have discovered.

The findings, published this week in the international journal Brain, could provide hope to sufferers of MS, one of the world's most common neurological diseases.

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When the modified protein, or the communication between the two proteins, was blocked, disease progression was halted.
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"We define it as a 'hand brake'. It (the therapy) halts it, (and) then the body in its own right can actually repair."

Dr Petratos said the clinical method used to block the proteins had already been approved by the US Food and Drug Administration and Australia's Therapeutic Goods Administration to treat other conditions.

"This should mean that clinical trials - once they start - will be fast-tracked," he said.

He said if clinical trials on humans started within a few years, it was hoped a therapy could be available in a decade.

Scientists from the University of Toronto and Yale University in the United States were also involved in the research.

Collapsin response mediator protein2 (CRMP2) is a brain-specific protein involved in neuronal polarity and axonal guidance, and phosphorylation of CRMP2 regulates the function and the activity. CRMP2 has shown to be implicated in several neurodegenerative diseases (Alzheimer's disease, epilepsy and ischemia)

In another study, we have recently found that CRMP-2 interacts with Specifically Rac1-Associated protein (Sra-1/CYFIP1) (43a), which directly interacts with actin filaments (45). Thus, CRMP-2 may associate with actin filaments through Sra-1 in growth cones. In this study, Rho kinase-induced phosphorylation of CRMP-2 had no effect on the actin binding ability of CRMP-2. CRMP-2 is a highly conserved phosphoprotein, and its phosphorylation states alter upon NGF-induced neuronal differentiation or in the formation of degenerating neurites in the brains of patients with Alzheimer's disease (12, 33). These findings raise the possibility that other kinases up- or down-regulate CRMP-2 activity and mediate actin reorganization in the Rho family GTPase-mediated signal cascade. Further studies characterizing the protein kinases may shed some light on other functions of CRMP-2.

Since CRMP-2 is present in adult and aged brains, there is reason to speculate that it may have a role in neuritic and axonal growth and regeneration and thus contribute to a high level of plasticity in adult brains. In some disease states, CRMP-2 has been shown to be reduced, such as in Down syndrome fetal brain, epilepsy brain hippocampus and areas of traumatic brain injury. In Alzheimer’s disease, CRMP-2 has been shown to be associated with the paired helical filaments (PHF) in degenerating neurons. This PHF-associated CMPR-2 has been shown to be highly phosphorylated. This hyperphosphorylated form of CMPR-2 may lead to its inactivation and may accelerate the neuritic degeneration in Alzheimer’s disease.