Office: MLSC 225
Office Phone: 562-985-5594
- BIOL 342L
Comparative Muscle Physiology: I am generally interested in the physiology of vertebrate skeletal and cardiac muscle, and in particular, the myosin heavy-chain contractile protein. Myosin is the major force producing component of muscle, and has many functionally different isoforms; each protein is a distinct gene product and is differentially expressed in individual muscles. The control of myosin protein expression is complex, and is very sensitive to activity, temperature, and hormone influences. Skeletal muscle and the heart are both affected by exercise, resistance training, and other factors, which may dramatically change the muscle size and myosin heavy chain composition. I am most interested in shifts or transitions in myosin protein expression with increased activity, or conversely, with disuse.
As a proponent of the comparative approach, my laboratory investigates a wide variety of vertebrates, each of whom demonstrates some remarkable aspect of muscle physiology. The techniques involved are elementary to muscle physiology and molecular biology, but are somewhat novel in their application to these diverse organisms. Protein gel electrophoresis is useful for measuring the expression of myosin isoforms in individual muscles, or even individual muscle fibers. Reverse-transcriptase polymerase chain reaction (RT-PCR) allows estimation of the mRNA expression of each myosin gene, and in general, myosin genes from new species are sequenced where possible.