Calmodulin’s Interaction with α- Synuclein, a Protein Implicated in Parkinson’s Disease

Authors

Joeli Reim, Chapman UniversityFollow
Jerry LaRue, Chapman UniversityFollow
Cedric P. Owens, Chapman UniversityFollow
Zeynep A. Ataman, Chapman UniversityFollow

Publication Date

Spring 5-2018

Faculty Advisor(s)

Jerry LaRue, Cedric Owens, Zeynep Ataman

Abstract

60,000 people in one year diagnosed, 1 million in the United States, and over 10 million worldwide have Parkinson’s disease (PD), which is the 2^nd most common neurodegenerative disease. PD is prevalent in males and is typically seen in patients in their 60s. The most notable symptom of PD is the degeneration of neuronal control, especially in the hands. Over $156 million is spent on researching this disease and about $25 billion is spent for diagnosed patients each year. Aside from managing the financial burdens of PD, patients also have physical burdens. Most patients develop tremors and have difficulties writing, eating, and can degenerate quickly. The PD has previously been attributed to the lack of the neurotransmitter, dopamine, in the patient’s brain; however recent biochemical studies have surfaced other biomolecular mechanisms that attribute to PD, such as the interaction between Calmodulin and α-Synuclein. Calmodulin (CaM) is a protein found in the brain of healthy patients and is an intermediate calcium (Ca²⁺) binding messenger with over 100 different targets in eukaryotic cells. α- Synuclein (α-Syn) is a protein found at the ends of neurons in the presynaptic terminals in healthy patients, suggesting involvement with neurotransmitter signaling, however the exact function of α- Syn is still under investigation. Recent studies show that α- Syn and CaM interact resulting in protein aggregation. The α- Syn aggregation is the main structural component of Lewy bodies which is enhanced in the presence of Ca²⁺. Lewy bodies are known to develop in cranial nerve cells of PD patients and interrupts neuronal function. Little is known about how Lewy bodies attribute to abnormalities in PD patients, but there are connections to low levels of acetylcholine and dopamine, in addition to an interruption of signals between nerve cells. By using fluorescence spectroscopy, we studied the interaction between α- Syn and CaM and explore Ca²⁺’s role in the interaction that promotes the degenerateness of PD patients.

Comments

Presented at the Spring 2018 Student Research Day at Chapman University.

Recommended Citation

Reim, Joeli; LaRue, Jerry; Owens, Cedric P.; and Ataman, Zeynep A., "Calmodulin’s Interaction with α- Synuclein, a Protein Implicated in Parkinson’s Disease" (2018). Student Scholar Symposium Abstracts and Posters. 275.
https://digitalcommons.chapman.edu/cusrd_abstracts/275