We use a variety of protein biochemical, molecular biology and multi-scale mechanical and structural analysis assays to study how contraction is regulated by the thin and thick filaments of cardiac and skeletal muscles. Studies are performed with human and animal tissue models and with stem cell derived cardiac and skeletal muscle cells. More recently we have also begun to look at how the contractile apparatus develops in early stage muscle as a means to understanding how this may be altered with mutations that initiate compensatory mechanisms and trigger of the disease process.

Related Publications

• Regnier M, Martin H, Barsotti RJ, Rivera AJ, Martyn DA, Clemmens E. Cross-bridge versus thin filament contributions to the level and rate of force development in cardiac muscle. Biophys J. 2004 Sep;87(3):1815-24. PubMed PMID: 15345560; PubMed Central PMCID: PMC1304586.
• Gillis TE, Martyn DA, Rivera AJ, Regnier M. Investigation of thin filament near-neighbour regulatory unit interactions during force development in skinned cardiac and skeletal muscle. J Physiol. 2007 Apr 15;580(Pt. 2):561-76. PubMed PMID: 17317743; PubMed Central PMCID: PMC2075566.
• Kreutziger KL, Piroddi N, McMichael JT, Tesi C, Poggesi C, Regnier M. Calcium binding kinetics of troponin C strongly modulate cooperative activation and tension kinetics in cardiac muscle. J Mol Cell Cardiol. 2011 Jan;50(1):165-74. PubMed PMID: 21035455; PubMed Central PMCID: PMC3018540.
• Korte FS, Feest ER, Razumova MV, Tu AY, Regnier M. Enhanced Ca²⁺ binding of cardiac troponin reduces sarcomere length dependence of contractile activation independently of strong crossbridges. Am J Physiol Heart Circ Physiol. 2012 Oct 1;303(7):H863-70. PubMed PMID: 22865385; PubMed Central PMCID: PMC3469702.