Kyla Rakoczy

 

Mentor: Dr. Elisabeth Barton

College of Health and Human Performance

"Gain new skills and insights into an environment integral to the medical field and technological advancements."

Major

Applied Physiology and Kinesiology

Minor

N/A

Research Interests

  • Muscular Dystrophy
  • Bone Growth
  • Neuromuscular Connections

Academic Awards

  • Florida Bright Futures (2015)
  • Emerging Scholars Program (2015)
  • University Scholars Program (2017-2018)

Organizations

  • Inclusive Fitness United Sports
  • UF Health and Human Performance Ambassadors
  • Center for Undergraduate Research Board of Students (CURBS)

Volunteer

  • Lincoln Middle School Science Club
  • Shands Hospital
  • Sidney Lanier Center

Hobbies and Interests

  • Baking
  • Football
  • Intramural Sports
  • Traveling

Research Description

Archvillan and Gamma Sarcoglycan Interactions
Muscular dystrophies are caused by genetic defects in sarcolemmal structural proteins, signaling intermediates and or membrane repair pathways. Two major sarcolemmal complexes attach the extracellular matrix to the actin cytoskeleton of muscle fibers, stabilizing the membrane against mechanical stresses. Both Limb Girdle Muscular Dystrophy (LGMD) and Duchenne’s muscular dystrophy (DMD) are characterized by absence of the SG complex. Sarcoglycans are a family of transmembrane proteins that make up the dystrophin glycoprotein complex (DGC). Four different kinds of LGMD involves a single sarcoglycan mutation causing a loss of all SG functioning, resulting in decreased membrane stability. Specifically, we’ve isolated the muscle specific protein archvillan as a key interacting protein. Archvillan is upregulated in LGMD2 patients and mice without gamm sarcogylcan subunit suggesting its integral role in the dystrophin complex. During our study we will further investigate the importance of archvillan and gamma sarcoglycan interaction for normal mechanical signaling as well as determine if aberrant mechanical signaling contributes to dystrophic pathology in LGMD2c patients. By the conclusion of our study we will have identified key proteins in sarcoglycan dependent mechnosensory machinery and signaling mechanisms that contribute to muscular dystrophy. Enhancement in the knowledge of specific signaling proteins In mechnosensory pathways can result in improvement in therapeutic and medicinal treatment modalities to improve length and quality of life for muscular dystrophy patients.