Richard Lovering

Publications (2)5.19 Total impact

• Source

  Available from: Susan G Dorsey

  Article: Genetic deletion of trkB.T1 increases neuromuscular function.

  Susan G Dorsey, Richard M Lovering, Cynthia L Renn, Carmen C Leitch, Xinyue Liu, Luke J Tallon, Lisa DeShong Sadzewicz, Abhishek Pratap, Sandra Ott, Naomi Sengamalay, [......], Robert Talmadge, Brandon K Harvey, Ryan M Wyatt, Elizabeth Vernon-Pitts, Chao Zhang, Kevan Shokat, Claire Fraser-Liggett, Rita J Balice-Gordon, Lino Tessarollo, Christopher W Ward
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  ABSTRACT: Neurotrophin-dependent activation of the tyrosine kinase receptor trkB.FL modulates neuromuscular synapse maintenance and function; however, it is unclear what role the alternative splice variant, truncated trkB (trkB.T1), may have in the peripheral neuromuscular axis. We examined this question in trkB.T1 null mice and demonstrate that in vivo neuromuscular performance and nerve-evoked muscle tension are significantly increased. In vitro assays indicated that the gain-in-function in trkB.T1(-/-) animals resulted specifically from an increased muscle contractility, and increased electrically evoked calcium release. In the trkB.T1 null muscle, we identified an increase in Akt activation in resting muscle as well as a significant increase in trkB.FL and Akt activation in response to contractile activity. On the basis of these findings, we conclude that the trkB signaling pathway might represent a novel target for intervention across diseases characterized by deficits in neuromuscular function.
  AJP Cell Physiology 08/2011; 302(1):C141-53. · 3.54 Impact Factor
• Article: Impaired recovery of dysferlin-null skeletal muscle after contraction-induced injury in vivo.

  Joseph A Roche, Richard M Lovering, Robert J Bloch
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  ABSTRACT: The protein, dysferlin, mediates sarcolemmal repair in vitro, implicating defective membrane repair in dysferlinopathies. To study the role of dysferlin in vivo, we assessed contractile function, sarcolemmal integrity, and myogenesis before and after injury from large-strain lengthening contractions in dysferlin-null and control mice. We report that dysferlin-null muscles produce higher contractile torque, and are equally susceptible to initial injury but recover from injury more slowly. Two weeks after injury, control muscles retain fluorescein dextran and do not show myogenesis. Dysferlin-null muscles do not retain fluorescein dextran, and show necrosis followed by myogenesis. Our data indicate that recovery of control muscles from injury primarily involves sarcolemmal repair whereas recovery of dysferlin-null muscles primarily involves myogenesis without repair and long-term survival of myofibers.
  Neuroreport 10/2008; 19(16):1579-84. · 1.66 Impact Factor