A robotic arm samples the environment of the deep sea worm.
The 1812 Overture heightened the drama during David Shin's two and a half hour long descent in Alvin, the deep sea submersible operated by the Woods Hole Oceanographic Institute. Shin, a research associate in the Scripps Research Institute's Tainer lab, was crammed into Alvin's spherical space, six feet in diameter, with a pilot and one other scientist. He was there to find deep sea worms.
The worms, called Alvinella pompejana, live in hydrothermal vents off the coast of Costa Rica. The vents can reach temperatures of 84 degrees Celsius (176 degrees Fahrenheit), and the worms are considered the hottest animal on the planet.
Shin travelled nearly a week just to get to the descent site because the worms hold a great deal of promise to scientists studying amytrophic lateral sclerosis (ALS), commonly known as Lou Gehrig's disease. ALS is a progressive neurodegenerative disease that ravages neurons in the brain and spinal cord. The worms are eukaryotes — meaning that their cells have nuclei — whereas bacteria's cells do not. This makes their highly stable proteins more directly comparable to human proteins.
"While most of the microbes have similar proteins, eukaryotes lack important regulatory mechanisms," said John Tainer, a Professor at Scripps Research and its Skaggs Institute for Chemical Biology. "This organism is closer to us than to bacteria and can bridge the gap."
Tainer and Shin were specifically interested in the worm's superoxide dismutase (SOD) enzyme, which composes an important antioxidant defense system. Inhibiting the SOD enzyme has been proven to control cancer cell growth — cancer cells, which produce substantially more oxidants than regular cells, essentially overdose on oxidants.
And the enzyme's role in ALS may be even greater. The SOD enzyme is mutated in some 20 percent of inherited or familial ALS cases.
"With ALS, in a substantial number of cases, when you destabilize the protein [SOD], amyloid-like fiber aggregations are formed," said Shin. Amyloid aggregations are implicated in a number of neurodegenerative diseases.
This is where the worm protein becomes essential. In a study recently published by Tainer and Shin, they showed that the stability of the worm's SOD enzyme may be the result of a reduction in certain molecular movements that increase the destructive interactions associated with ALS.
"By using the worm protein we might be able to tease out what the mechanisms are behind some of these mutations that initiate this," Shin said. "It is a very good start toward deciphering the process."
Tainer and Shin's work resulted in an important test model to study destabilizing mutations that occur in ALS and how they play out. Furthermore, the work spurred the search for other stable worm proteins that are representative of human proteins that play key roles in disease.
Who would have thought that these charmingly ugly creatures could offer crucial insight to human health? But this is the strange and unpredictable path that science often takes.
And this is why the knowledge built through basic biomedical research is so important. Your gift can help ensure that Scripps Research will be able to continue seeking answers, wherever they might be found.