LEWISTON, Idaho – Leigh Latta, an assistant professor in the Natural Sciences & Mathematics Division at Lewis-Clark State College, has been awarded an IDeA Network of Biomedical Research Excellence (INBRE) Pilot Project grant for almost $100,000 over two years for his proposal “Mutation Accumulation and the Physiological Basis of Declines in Neural Function.”
Latta’s project was one of only two projects chosen from more than 25 applications to receive funding through the Idaho INBRE Program, which is administered by the University of Idaho. The Idaho INBRE Program’s purpose is to increase the state’s competitiveness for federal biomedical research funding and to improve the quality of biomedical education in Idaho. All 10 higher education institutions in the state, both public and private, are part of the Idaho INBRE network.
Latta has been studying the mutational process since his sophomore year at the University of Oregon. He admits his interest in the topic actually came from comic books, like the X-Men, which features mutants as superheroes.
“I was fascinated by it and so I wanted to become a mutant biologist,” he said. “I really enjoy what I do.”
Latta has studied mutation for more than 20 years and his latest project that received funding will take a look at the effects of mutation on the evolution of neural function. The research is motivated by recent studies that have shown average human intelligence has declined 3-5 percent over the last 50 years, and suggested that the cause is the accumulation of bad mutations in the human population.
Latta said in the animal world, good mutations normally keep populations healthy – the strongest survive while the weak die. With humans, however, Latta said both the strong and weak survive because of medicine and technology, so the bad mutations build up in the population.
Along with LCSC students involved in the project, Latta will examine how mutant genes impact the evolution of complex neural traits, like behavior. Additionally, Latta and students will investigate the underlying physiological changes caused by the mutations that might be responsible for changes in neural function. For example, proteins that are rendered non-functional by mutation can bind together and become toxic to neural cells, so it’s important to determine if mutation increases protein clumps in these cells. If so, the results may provide valuable information on possible physiological interventions for various human diseases, such as Huntington’s and Alzheimer’s disease that are caused by age-related increases in protein aggregation.
For more information on the project, contact Latta at either lclatta@lcsc.edu or at his office at 208-792-2892.