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Elisabeth Barton - University of Florida. Gainesville, FL, US

Elisabeth Barton Elisabeth Barton

Professor | University of Florida

Gainesville, FL, UNITED STATES

Elisabeth Barton is a molecular physiologist with a primary interest in skeletal muscle repair.

Biography

Elisabeth Barton is a molecular physiologist with a primary interest in skeletal muscle repair. Her work has broad applications including accelerating the resolution of muscle damage after acute injuries, altering the balance between damage and repair in chronic injury associated with neuromuscular disease, and enhancing the repair axis in aging muscle. She has spent the last 20 years studying insulin-like growth factor I, a key player in the muscle regeneration process. More recently, Barton has focused on how muscles sense load, and how these sensors become dysfunctional in muscle disease. Her research has been supported by grants from NIH, NASA, Muscular Dystrophy Association and the DOD.

Industry Expertise (2)

Education/Learning

Health and Wellness

Areas of Expertise (5)

Muscular Dystrophy

Skeletal Muscle Repair

Mechanical Signal Transduction

Optimization of IGF-I for Muscle Therapeutics

Viral Gene Therapy

Media Appearances (2)

Promising New Strategy to Help Broken Bones Heal Faster

Laboratory Equipment  online

2020-02-25

From earlier work focused on muscular dystrophy conducted with former Penn Dental Medicine faculty member Elizabeth Barton, now at the University of Florida, the researchers believed that a particular form of IGF, a precursor of the protein that includes a separate component known as an e-peptide, was likely to stimulate regeneration better than mature IGF-1 that lacked the peptide. Current IGF1 used in the clinic not only lacks the e-peptide but is also glycosylated, a less active form.

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In space, not all muscles are created equal

UF News  online

2015-10-14

Muscles waste away when they’re not used, right? Turns out, it’s not that simple. Elisabeth Barton, a physiology professor in the University of Florida College of Health and Human Performance, studies how muscles react to reduced load. Her latest discovery comes from an unlikely source: mice in space.

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Social

Articles (3)

Novel γ-sarcoglycan interactors in murine muscle membranes

Skeletal Muscle

Tara C. Smith, et al.

2022-01-22

The sarcoglycan complex (SC) is part of a network that links the striated muscle cytoskeleton to the basal lamina across the sarcolemma. The SC coordinates changes in phosphorylation and Ca++-flux during mechanical deformation, and these processes are disrupted with loss-of-function mutations in gamma-sarcoglycan (Sgcg) that cause Limb girdle muscular dystrophy 2C/R5.

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Pharmacologic approaches to prevent skeletal muscle atrophy after spinal cord injury

Current Opinion in Pharmacology

Dana M. Otzel, et al.

2021-08-28

Skeletal muscle atrophy is a hallmark of severe spinal cord injury (SCI) that is precipitated by the neural insult and paralysis. Additionally, other factors may influence muscle loss, including systemic inflammation, low testosterone, low insulin-like growth factor (IGF)-1, and high-dose glucocorticoid treatment. The signaling cascades that drive SCI-induced muscle loss are common among most forms of disuse atrophy and include ubiquitin-proteasome signaling and others.

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Deletion of muscle Igf1 exacerbates disuse atrophy weakness in mice

Journal of Applied Physiology

Ray A. Spradlin, et al.

2021-08-26

Muscle atrophy occurs as a result of prolonged periods of reduced mechanical stimulation associated with injury or disease. The growth hormone/insulin-like growth factor-1 (GH/IGF-1) axis and load sensing pathways can both aid in recovery from disuse through their shared downstream signaling, but their relative contributions to these processes are not fully understood. The goal of this study was to determine whether reduced muscle IGF-1 altered the response to disuse and reloading.

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Languages (1)

  • English

Affiliations (3)

  • American Society for Cell Biology : Member
  • American Physiological Society : Member
  • Biophysical Society : Member