Ohio State - Nationwide Children's Hospital - Research For Muscle Biology and Disease
 

Brandon Biesiadecki, Ph.D.Tom Best, M.D., Ph.D., FACSM
Associate Professor
The Ohio State University

Physiology and Cell Biology
404 Hamilton Hall
1645 Neil Ave.
Columbus, OH 43210

Office Phone: (614) 247-4091
Email: biesiadecki.1@osu.edu
Web: http://biomed.osu.edu/physiology/13796.cfm

Education & Training:
Alma College, Alma, MI 1996, B.S. Biology
Medical College of Ohio, Toledo, OH, 1998, M.S. Biomedical Science
Case Western Reserve University, Cleveland, OH, 2003, Ph.D. Physiology
Case Western Reserve University, Cleveland, OH, 2003-2004 Postdoctoral Fellow
University of Illinois at Chicago, Chicago, OH, 2004-2009 Postdoctoral Fellow

Research Interest:
Research in my laboratory is focused on understanding the molecular mechanisms of how muscle protein post-translational modifications (phosphorylation, radical modification, degradation, ect.) alter heart function. Key to this focus is employing an integrated and multi-level experimental approach of molecular biology, biochemistry and physiology to provide a comprehensive understanding towards the development of novel treatments for heart dysfunction.

The function of the heart as an organ is determined by its ability to pump oxygen rich blood to the organs of the body. How well the heart functions (i.e. pumps blood) is largely determined by the ability of the heart cells to produce force by shortening and generate the necessary pressures required to circulate blood. Cellular shortening is mediated by an interaction of the molecular motor myosin with actin and is regulated through the signaling molecule calcium. Muscle cell contraction can be modulated by: 1) Altering the intracellular calcium concentration. 2) Altering the response of the muscle to calcium. 3) Altering the activity of the myosin motor. My laboratory is interested in understanding the role of protein modifications to alter the muscle’s response to calcium and affect heart function. Specifically, I am interested in understanding the physiological and pathological effects of regulated or stress induced phosphorylation and radical mediated post-translational modification of the muscle proteins that regulate the interaction of myosin with actin and their effect on cardiac contractility.

Selected Publications:

  • Nixon, B.R., Liu, B., Scellini, B., Tesi, C., Piroddi, N., Ogut, O., Solaro, R.J., Ziolo, M.T., Janssen, P.M., Davis, J.P., Poggesi, C., Biesiadecki, B.J. (in press) Tropomyosin Ser-283 pseudo-phosphorylation slows myofibril relaxation. Arch Biochem Biophys http://doi.org/10.1016/j.abb.2012.11.010. PMID: 23232082.
  • Roof, S.R., Biesiadecki, B.J., Davis, J.P., Janssen, P.M. and Ziolo, M.T. (2012) Effects of increased systolic Ca(2+) and β-adrenergic stimulation on Ca(2+) transient decline in NOS1 knockout cardiac myocytes. Nitric Oxide 27(4):242-247. PMID: 22960389.
  • Kranstuber, A.L., Del Rio, C., Biesiadecki, B.J., Hamlin, R.L., Ottobre, J., Gyorke, S., Lacombe and V.A. (2012) Advanced glycation end products cross-link breaker attenuates diabetes-induced cardiac dysfunction by improving sarcoplasmic reticulum calcium handling. Front Physiology 3:293. PMID 22934044.
  • Haizlip, K., Hiranandani, N., Biesiadecki, B.J. and Janssen, P.M. (2012) Impact of hydroxyl radical-induced injury on calcium handling and myofilament sensitivity in isolated myocardium. J Appl Physiol 113(5):766-774. PMID: 22773772.
  • Liu, B., Lee, R.S., Biesiadecki, B.J., Tikunova, S.B. and Davis, J.P. (2012) Engineered troponin C corrects disease-related cardiac myofilament calcium sensitivity. J Biol Chem 287(24):20027-20036. PMID: 22511780.
  • Nixon, B.R., Thawornkaiwong, A., Jin, J., Brundage, E.A., Little, S., Davis, J.P., Solaro, R.J. and Biesiadecki, B.J. (2012) AMP activated protein kinase phosphorylates cardiac troponin I at Ser-150 to increase myofilament calcium sensitivity and blunt PKA dependent function. J Biol Chem 287(23):19136-19147. PMID: 22493448.
  • Biesiadecki, B.J., and Jin, J.-P. (2011) A high throughput solid phase microplate binding assay to investigate interactions between myofilament proteins. Journal of Biomedicine and Biotechnology 2011:Acticle ID 421701, 8 pages, doi:10.1155/2011/421701. PMID: 22190850.
  • Biesiadecki, B.J., Tachampa, K., Yuan, C., de Tombe, P.P. and Solaro, R.J. (2010) Removal of the cardiac troponin I N-terminal extension improves cardiac function in aged mice. J Biol Chem 285(25):19688-19698.
  • Biesiadecki, B.J., Kobayashi, T., Walker, J.S., Solaro, R.J., de Tombe, P.P. (2007) Troponin C G159D mutation blunts myofilament desensitization induced by troponin I Ser-23/24 phosphorylation. Circulation Research 100(10):1486-1493.
  • Biesiadecki, B.J., Chong, S.M., Nosek, T.M. and Jin, J.-P. (2007) Troponin T core structure and the regulatory NH2-variable region. Biochemistry 46(5):1368-1379. PMID: 17260966.
  • Biesiadecki B.J. and Jin J.-P. (2002) Exon skipping in cardiac troponin T of turkeys with inherited dilated cardiomyopathy. J Biol Chem. 277(21):18459-18468.