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Dolphins are well known as excellent swimmers for being capable of efficient cruising and sharp acceleration. While studies of the thrust production and power consumption of dolphin swimming have been the main subject for decades, time-varying acceleration process during successive fluke beats still remains poorly understood. In this study, we quantified the time-varying kinematics of a dolphin (Lagenorhynchus obliquidens) by directly recording its burst-accelerating swimming before vertical jump in an aquarium with two synchronized high-speed video cameras. We tracked the three-dimensional trajectories of its beak, body sides, and fluke. We found that dolphin could quickly accelerate from 5.0 m s-1 to 8.7 m s-1 merely by 5 strokes (i.e. 2.5 fluke beats) in 0.7 seconds. During the strokes, it was further found that the dolphin demonstrated a great acceleration in downstroke but less acceleration or even a slight deceleration in upstroke. Hydrodynamic forces and thrust power for each stroke were further estimated based on the equation of body motion and a static hydrodynamic model. The drag coefficient of the dolphin was estimated through computational fluid dynamics (CFD) modeling of the steady flows around a realistic geometric model based on 3-D scan data. The thrust and thrust power were then calculated by combining the body kinematics and the drag coefficient, resulting in a maximum stroke-averaged thrust and power-to-mass ratio of 1.3 × 103 N and 90 W kg-1 at downstroke, and 3.3 × 102 N and 19 W kg-1 at upstroke, respectively. Our results point out the importance of asymmetric kinematics in burst acceleration of dolphin, which may be a useful mechanism for biomimetic design of high-performance underwater robots.

Phosphorylation of hormone-sensitive lipase (HSL) and perilipin by protein kinase A (PKA) promotes the hydrolysis of lipids in adipocytes. Although activation of lipolysis by PKA has been well studied, inactivation via protein phosphatases is poorly understood. Here, we investigated whether phospholipase C-related catalytically inactive protein (PRIP), a binding partner for protein phosphatase 1 and protein phosphatase 2A (PP2A), is involved in lipolysis by regulating phosphatase activity. PRIP knockout (PRIP-KO) mice displayed reduced body-fat mass as compared with wild-type mice fed with standard chow ad libitum. Most other organs appeared normal, suggesting that mutant mice had aberrant fat metabolism in adipocytes. HSL in PRIP-KO adipose tissue was highly phosphorylated compared to that in wild-type mice. Starvation of wild-type mice or stimulation of adipose tissue explants with the catabolic hormone, adrenaline, translocated both PRIP and PP2A from the cytosol to lipid droplets, but the translocation of PP2A was significantly reduced in PRIP-KO adipocytes. Consistently, the phosphatase activity associated with lipid droplet fraction in PRIP-KO adipocytes was significantly reduced and was independent of adrenaline stimulation. Lipolysis activity, as assessed by measurement of non-esterified fatty acids and glycerol, was higher in PRIP-KO adipocytes. When wild-type adipocytes were treated with a phosphatase inhibitor, they showed a high lipolysis activity at the similar level to PRIP-KO adipocytes. Collectively, these results suggest that PRIP promotes the translocation of phosphatases to lipid droplets to trigger the dephosphorylation of HSL and perilipin A, thus reducing PKA-mediated lipolysis.

Class V myosin (myosin-V) is a cargo transporter that moves along an actin filament with large (approximately 36-nm) successive steps. It consists of two heads that each includes a motor domain and a long (23 nm) neck domain. One of the more popular models describing these steps, the hand-over-hand model, assumes the two-headed structure is imperative. However, we previously succeeded in observing successive large steps by one-headed myosin-V upon optimizing the angle of the acto-myosin interaction. In addition, it was reported that wild type myosin-VI and myosin-IX, both one-headed myosins, can also generate successive large steps. Here, we describe the mechanical properties (stepsize and stepping kinetics) of successive large steps by one-headed and two-headed myosin-Vs. This study shows that the stepsize and stepping kinetics of one-headed myosin-V are very similar to those of the two-headed one. However, there was a difference with regards to stability against load and the number of multisteps. One-headed myosin-V also showed unidirectional movement that like two-headed myosin-V required 3.5 k(B)T from ATP hydrolysis. This value is also similar to that of smooth muscle myosin-II, a non-processive motor, suggesting the myosin family uses a common mechanism for stepping regardless of the steps being processive or non-processive. In this present paper, we conclude that one-headed myosin-V can produce successive large steps without following the hand-over-hand mechanism.