Pathways to the perfect fit

Hannah Frye in the neurobiology lab could lead to a treatment for diseases like Alzheimer’s or Parkinson’s. Photo by B.A. Rupert.

Hannah Frye, pictured above warming media in the neurobiology lab, is doing work that could lead to a treatment for diseases like Alzheimer’s or Parkinson’s. Photo by B.A. Rupert.

At first glance, it is impossible to tell that Hannah Frye, a senior in chemistry with an emphasis in biochemistry, is helping Robert Aronstam perform groundbreaking research that could lead to treatments for diseases like Alzheimer’s or Parkinson’s. But stop her in the Havener Center at lunch and ask her about her work with the chair of biological sciences and she can explain anything from cell signaling to how she measures the calcium levels in a cell’s endoplasmic reticulum and cytoplasm.

Since starting in Aronstam’s lab two years ago, the Lee’s Summit, Mo., native has been studying how muscarinic acetylcholine receptors react to different pharmaceuticals. Acetylcholine is a neurotransmitter necessary for learning and concentration, as well as muscle movement. The receptor interaction with a transducer G protein determines the biological reaction pathway that the receptor will activate.

In degenerative diseases like Alzheimer’s and Parkinson’s, acetylcholine neurons disappear. Current treatments, which are only marginally effective, are designed to increase transmission in the acetylcholine cells that remain. Frye and Aronstam hope that by manipulating the pattern of acetylcholine signaling, they may be able to preserve that signaling for as long as possible.

“It’s still a new idea, but Alzheimer’s alters G proteins to make them go down different pathways too,” she says. “If you can understand how a G protein’s signaling changes, then you could possibly use gene therapy to correct the disease.

“It’s easy to measure the reactions with M1 and M3 muscarinic receptors because they emit calcium, but to measure the response of M2 and M4 receptors, you have to mutate a G protein so that the cell emits calcium,” Frye says. “It’s a wolf in sheep’s clothing.” By mutating the DNA coding for G proteins, Frye has altered the pattern of coupling between G proteins and their receptors in an way that may mimic changes that occur in diseases.

When she isn’t in the lab, Frye works as a resident assistant on campus. She’s also vice president of the International Genetically Engineered Machines (iGEM) Team and a member of Alpha Chi Sigma, a professional chemistry fraternity.

Frye says she has found the perfect fit in her research and in S&T, and she knows others can too.

“I enjoy the ability to expand my knowledge base with research that is outside of my normal coursework,” she says. “It is my goal to demonstrate that this school is truly a place where opportunities for personal, academic and professional growth are abundant.”

By Arielle Bodine

This story was originally published in Missouri S&T Magazine.

Read additional stories from the Spring 2014 issue.