The University of Toledo

Faculty/Staff

Tom McLoughlin, PhD.

Associate Professor, Department of Kinesiology
College: Health Science and Human Service
Office: HH 2505F
Email: thomas.mcloughlin@utoledo.edu
Phone: 419-530-5982
Fax: 419-530-4759

Click here to view laboratory photos.

Dr. McLoughlin joined the Department of Kinesiology at The University of Toledo as an Assistant Professor of Exercise Physiology in January 2004.  

Research Scope:

Skeletal muscle is a highly adaptable tissue that responds to various mechanical, metabolic, and environmental demands through changes in morphology, plasticity, enzyme capacity, and/or cytosolic composition.    These adaptations are accomplished through modulation in various molecular signaling cascades, resulting in transcriptional and translational alterations, changes in gene expression patterns, and select protein modifications.    Skeletal muscle atrophy, a process characterized by increased protein degradation and a decrease in muscle size, is a manifestation of physical inactivity, aging, neuromuscular injury, and/or various disease processes.  Understanding the molecular regulation and processes associated with skeletal muscle atrophy is necessary for attenuating losses in skeletal muscle mass and function associated with aging, injury, and various disease processes, and, ultimately, improving the overall quality of life in a multitude of individuals.     

Current Research:

Our lab is involved in several projects investigating the molecular regulation of skeletal muscle growth and the maintenance of skeletal muscle mass associated with physical activity and inactivity.    Specifically, Forkhead (FoxO) proteins constitute a sub-family of winged-helix transcription factors (i.e. FoxO1, FoxO3, and FoxO4) responsible for maintaining cell survival, proliferation and metabolic regulation.   Currently, our lab is investigating the contribution of FoxO1 in regulating the interplay between skeletal muscle growth and metabolic flux. 

EDUCATION
Postdoctoral Research Associate , 10/01-12/03
The Muscle Biology Laboratory
The University of Illinois at Chicago, Chicago, Illinois   60608
Supervisor: Karyn A. Esser, Ph.D.

Doctor of Philosophy , Applied Physiology, 8/01
Minor: Research and Measurement
The University of Toledo, Toledo, Ohio   43606

Dissertation Title: Neutrophil-mediated skeletal myotube injury: the contribution of reactive oxygen and nitrogen intermediates

Master of Arts , Exercise Physiology, 8/96
Adelphi University, Garden City, New York   11530

Bachelor of Science , Athletic Training/Exercise Science, 5/95 
Ithaca College, Ithaca, New York   14850

RECENT PUBLICATIONS

 

McLoughlin TJ, Smith SM, Delong AD, Wang H, Unterman TG, and Esser KA. FoxO1 induces apoptosis in skeletal myotubes in a DNA binding-dependent manner. Am J Physiol Cell Physiol, 2009.  297: C548-C555, 2009.

 Novak ML, Billich W, Smith SM, Sukhija KB, McLoughlin TJ, Hornberger TA, and Koh TJ. COX-2 inhibitor reduces skeletal muscle hypertrophy in mice. Am J Physiol Regul Integr Comp Physiol 296: R1132-1139, 2009.

 Moylan JS, Smith JD, Chambers MA, McLoughlin TJ, and Reid MB. TNF induction of atrogin-1/MAFbx mRNA depends on Foxo4 expression but not AKT-Foxo1/3 signaling. Am J Physiol Cell Physiol 295: C986-993, 2008.

 Marino JS, Tausch BJ, Dearth CL, Manacci MV, McLoughlin TJ, Rakyta SJ, Linsenmayer MP, and Pizza FX. Beta2-integrins contribute to skeletal muscle hypertrophy in mice. Am J Physiol Cell Physiol 295: C1026-1036, 2008.

 Kuntz AR, Griffiths CM, Rankin JM, Armstrong CW, and McLoughlin TJ. Cortisol concentrations in human skeletal muscle tissue after phonophoresis with 10% hydrocortisone gel. J Athl Train 41: 321-324, 2006.

 Nader GA, McLoughlin TJ, and Esser KA. mTOR function in skeletal muscle hypertrophy: increased ribosomal RNA via cell cycle regulators. Am J Physiol Cell Physiol 289: C1457-1465, 2005.

 Bastie CC, Nahle Z, McLoughlin T, Esser K, Zhang W, Unterman T, and Abumrad NA. FoxO1 stimulates fatty acid uptake and oxidation in muscle cells through CD36-dependent and -independent mechanisms. J Biol Chem 280: 14222-14229, 2005.