Science Topics – 148
Hydrostatic pressure equivalent to 4,000 to 8,000 meters in the deep sea (40 to 80 MPa. 1 MPa is about 10 atm) reversibly changes the hydration state of the protein surface and weakens the binding between proteins. As a result, hydrostatic pressure of 40-80 MPa promotes structural changes in protein aggregates. Unlike the solution exchange operation that changes the solution composition, the feature of the hydrostatic pressure operation is that it acts on the protein aggregate reversibly and uniformly. We have clarified how this hydrostatic pressure manipulation can change the structure and function of myofibrils. In the experiment, myofibrils taken from the iliopsoas muscle of Japanese white rabbits were used. We clarified the structural changes of myofibrils during pressurization by using a high-pressure microscopy method in which observation is performed using an optical microscope under a hydrostatic pressure of 40 to 80 MPa. We also clarified the nature of self-excited contraction sarcomeric oscilaltions of myofibrils during and after pressurization. The pressure used in this experiment corresponds to the level inside the high-pressure hydrogen cylinder (35 MPa or 70 MPa) mounted on the fuel cell vehicle. Although the research fields are different, it can be said that it is a new result showing that ultra-high pressure changes the properties of living things.
We observed structural changes in myofibrils during pressurization using a high-pressure microscopy method, in which observation was performed using an optical microscope under hydrostatic pressure of 40 to 80 MPa. The structural changes evoked change depending on the presence or absence of adenosine triphosphate in the solution and the strength and time of the applied pressure.
1. Department of Biomedical Sciences, College of Life and Health Sciences, Chubu University