Investigadores destapan detonador clave para potente producto marino contra el cáncerContributed by: Anonymous · Views: 1,179
Contributed by: Anonymous · January 04, 2008 @ 09:17 AM MST · Views: 1,179
Researchers Uncover Key Trigger
for Potent Cancer-Fighting Marine Product
Discovery could lead to new versions of drug being tested as a cancer treatment in humans
An unexpected discovery in marine biomedical laboratories at Scripps Institution of Oceanography at UC San Diego has led to new, key information about the fundamental biological processes inside a marine organism that creates a natural product currently being tested to treat cancer in humans. The finding could lead to new applications of the natural product in treating human diseases.
“This was a totally unexpected pathway,” said Moore. “There are well over 2,000 chlorinated natural products and this is the first example in which chlorine is assimilated by this kind of pathway,” said Moore.
Alessandra Eustáquio and her colleagues in Brad Moore's laboratory discoverd a new enzyme and biological pathway in Salinispora tropica, a promising marine organism that creates a natural product being tested to treat cancer.
Moore believes the discoveries provide a new “road map” for furthering S. tropica’s potential for drug development. Knowing the pathway of how the natural product is made biologically may give biotechnology and pharmaceutical scientists the ability to manipulate key molecules to engineer new versions of Salinispora-derived drugs. Genetic engineering may allow the development of second-generation compounds that can’t be found in nature.
“It’s possible that drug companies could manufacture this type of drug in greater quantities now that we know how nature makes it,” said Moore.
A high-resolution X-ray representation of the new enzyme's structure.
“The chlorine atom in salinosporamide A is key to the drug’s irreversible binding to its biological target and one of the reasons the drug is so effective against cancer,” said Moore.
According to Eustáquio, finding the enzyme and its new pathway also carries implications for understanding evolutionary developments, including clues for how and why related enzymes are activated in different ways.
Also joining Moore and Eustáquio in the research were coauthors Florence Pojer and Joseph Noel (of the Howard Hughes Medical Institute, Jack H. Skirball Center for Chemical Biology and Proteomics, The Salk Institute for Biological Studies), who developed high-resolution X-ray structures and other aspects of the research.
The work was supported by the National Oceanic and Atmospheric Administration, the National Institutes of Health and the National Science Foundation.
Media Contact: Mario Aguilera or Cindy Clark, 858-534-3624
Courtesy: University of California, San Diego