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

Muthu Periasamy, Ph.D. Muthu Periasamy, Ph.D.
Professor and Chair
The Ohio State University

Department of Physiology and Cell Biology
Davis Heart & Lung Research Institute
300 Hamilton Hall
1645 Neil Avenue
Columbus. OH 43210

Office Phone: (614) 292-2310
Fax: (614) 292-4888
Email: Periasamy.1@osu.edu
Web: http://biomed.osu.edu/physiology/3484.cfm

Education & Training:
PhD in Biochemistry. University of Montpellier France; Post doctoral research at Albert Einstein college of Medicine & Harvard Medical School.

Research Interest:
The overall goal of my laboratory is to demonstrate the roles of skeletal muscle beyond contraction, especially in thermogenesis and metabolism . Our research has identified a novel protein called Sarcolipin (SLN) in muscle that controls SERCA pump (Ca2+ ion transport ATP ase) activity. We found that this protein promotes uncoupling of SERCA pump, and prolongs Ca2+ cycling, as a result SLN increases ATP hydrolysis and heat production by SERCA, at the same time increasing energy cost for Ca2+ cycling. Using both loss and gain of function mouse models for SLN, We have recently demonstrated that SLN is essential for temperature regulation. Interestingly we found that SLN also regulates metabolism. Mice without SLN are susceptible to diet induced obesity, whereas SLN overexpression protects them from diet induced obesity. These studies collectively suggested that muscle also plays vital roles in thermogenesis and heat production. Current research in the lab is focused on 1) the molecular mechanism behind how SLN/SERCA interaction leads to uncoupling and heat production, and 2) studying the role of SLN in energy metabolism and obesity and testing if SLN based mechanism can be used as an effective therapy optimizing to treat obesity. Our research utilizes a number of approaches ranging from whole animal models and as well studies at the molecular level.

Selected Publications:

  • Babu GJ, Bhupathy P, Timofeyev V, Petrashevskaya NN, Reiser PJ, Chiamvimonvat N, Periasamy M. Ablation of sarcolipin enhances sarcoplasmic reticulum calcium transport and atrial contractility. Proc Natl Acad Sci U S A 2007; 104 (45):17867-72.
  • Chi M, Zhou Y, Vedamoorthyrao S, Babu GJ, Periasamy M. Ablation of smooth muscle myosin heavy chain SM2 increases smooth muscle contraction and results in postnatal death in mice. Proc Natl Acad Sci U S A 2008; 105 (47):18614-8.
  • Periasamy M, Bhupathy P, Babu GJ. Regulation of sarcoplasmic reticulum Ca2+ ATPase pump expression and its relevance to cardiac muscle physiology and pathology. Cardiovasc Res 2008; 77(2):265-73.
  • Stevens SC, Terentyev D, Kalyanasundaram A, Periasamy M, Györke S. Intra-sarcoplasmic reticulum Ca2+ oscillations are driven by dynamic regulation of ryanodine receptor function by luminal Ca2+ in cardiomyocytes. J Physiol 2009; 587 (Pt 20):4863-72.
  • Kalyanasundaram A, Bal NC, Franzini Armstrong C, Knollmann BC, Periasamy M. The calsequestrin mutation CASQ2D307H does not affect protein stability and targeting to the JSR but compromises its dynamic regulation of calcium buffering. J Biol Chem 2010; 285(5):3076-83
  • Bal NC, Maurya SK, Sopariwala DH, Sahoo SK, Gupta SC, Shaikh SA, Pant M, Rowland LA, Goonasekera SA, Molkentin JD, Periasamy M. Sarcolipin is a newly identified regulator of muscle-based thermogenesis in mammals. Nat Med 2012; 18(10):1575-9.