Document Type

Honors Thesis

Major

Biology

Advisor(s)

Jared Talbot

Committee Members

Mark Haggerty, Clarissa Henry, Leonard Kass, Robert Wheeler

Graduation Year

May 2022

Publication Date

2025

Abstract

Mylpf protein stimulates muscle contraction by binding and stabilizing myosin proteins in fast-twitch muscle. This stabilization is important for the production of sarcomeres, which serve as the basic unit of muscle structure. During this study, mutant zebrafish were examined for the genes encoding myosin-binding proteins Mylpfa and/or Mylpfb to find how these proteins behave when sarcomere organization is disrupted in zebrafish. Last summer, a technician in the Talbot lab used DanioVision to find reduced peak velocities in mylpfa mutants, but that work needed another repeat, and it was unclear whether the mylpfa mutants fully lacked fast muscle function, which we knew to be absent in mylpfa;mylpfb double mutant fish. I have completed 21 Trials of DanioVision imaging in order to investigate what peak velocities each genotype group of zebrafish reached on their own volition. The primary goal of this study was to investigate how zebrafish behave when they swim on their own volition. By combining my data of 149 fish and analyzing 6,699,933 data points collected through DanioVision, I differentiated between the peak velocity ranges that correspond to slow-twitch muscle (0-65 mm/sec) and fast-twitch muscles (65- 250 mm/sec) in zebrafish. My DanioVision experiments can also tech us more about Mylpf. Surprisingly, I found that mylpfb mutants, despite having a proper sarcomere structure, were not able to reach high peak velocities with the same frequency as WT zebrafish. Mylpfa mutants, despite covering the same amount of distance as WT siblings, showed reduced peak velocity, suggesting that they swim moreat slower speeds. Consistent with initial prediction, mylpfa;mylpfb mutant zebrafish were the least likely group to to reach a velocity of >65 mm/sec.

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