Effect of Arachidonic Acid on Myosin II Function

Presenter Information

Trishala Karmacharya, Minnesota State University, Mankato

Location

CSU Ballroom

Start Date

2-4-2019 10:00 AM

End Date

2-4-2019 11:30 AM

Student's Major

Chemistry and Geology

Student's College

Science, Engineering and Technology

Mentor's Name

Rebecca Moen

Mentor's Department

Chemistry and Geology

Mentor's College

Science, Engineering and Technology

Description

The main contractile proteins in muscle are actin and myosin, the interaction between them is what generates movement and muscle contraction. Muscle myosin, myosin II, is the motor protein that drive muscle contraction through chemo-mechanical coupling; binding adenosine triphosphate (ATP) and hydrolyzing into adenosine diphosphate (ADP) and inorganic phosphate (Pi) as it produces force. This conversion of ATP into ADP and Pi is myosin's ATPase activity. Arachidonic acid is a bioactive lipid and is produced in all eukaryotic cells. It has been shown to stimulate the ATPase activity in smooth muscle myosin II (1). It is postulated to bind to myosin motor domain near the actin-binding site and increase the rate of Pi release, which also increases the ATPase activity of myosin (1). This study will test the effect of arachidonic acid on myosin II from Dictyostelium discoideum, which will specifically test ATPase activity in myosin and myosin's ability to interact with actin. The functional changes in myosin and actin will be tested using the myosin ATPase assay, which measures the rate at which myosin hydrolyses ATP, and actomyosin co-sedimentation assay, to measure the binding interaction and affinity of myosin for actin.