Testing of aequorin has yielded promising results, said Mark Y. Underwood of Quincy Bioscience located in Madison. Researcher James Moyer, Jr., an assistant professor at UW-Milwaukee, subjected brain cells to the "lab" equivalent of a stroke, and more than half treated with aequorin survived without residual toxicity.
Why does it work? Diseases like Alzheimer's are associated with a loss of "calcium-binding" proteins that protect nerve cells, said Moyer. Calcium is necessary for communication between neurons in the brain, and learning and memory are not possible without it. But too much of it leads to neuron death, interfering with memory and contributing to neurodegenerative diseases.
"There are ways in which cells control the influx of calcium, such as sequestering it by binding it with certain proteins," said Moyer. "If it weren't for these proteins, the high level of calcium would overwhelm the neuron and trigger a cascade of events ultimately leading to cell death."
Calcium-binding proteins decline with age, however, limiting the brain's ability to control or handle the amount of calcium "allowed in."
Aequorin, the jellyfish protein, appears to be a viable substitute.
Moyer, like Underwood, is interested in the "calcium hypothesis of aging and dementia," which is just one of many theories that attempts to explain what is going on in neuron degeneration.
He became interested in aequorin as an undergraduate at UW-Milwaukee, after reading an article that linked the stings of jellyfish with the symptoms of multiple sclerosis, a disease of the central nervous system that his mother has.
Aequorin was discovered in the 1960s and has been used in research for a
Source:University of Wisconsin - Milwaukee