Ripple reduction control of the undulation pump total artificial heart.

An undulation pump total artificial heart (UPTAH) in which the revolutions of the motor are converted to undulation motion of a disk has been developed. In an experiment, a goat using the UPTAH survived for 54 days. However, a large ripple was observed in the device's output pressure and flow waveform. In calculating the spectrum of the ripple, we found that the ripple mainly comprised 2 frequency sine waves: 1 having the same frequency as and 1 having double the frequency of the motor revolutions. To reduce the ripple, 2 sine waves, 1 having the same frequency as and 1 having double the frequency of the motor revolutions, were provided to the motor current to modulate the pulse width of the pulse width modulation controlling the motor revolutions. This ripple control method reduced the pressure ripple by 90% in a mock circulation and by 70% in animal experiments. These results revealed that the ripple generated in the UPTAH could be controlled through the use of motor control software.

Phosphorylation of Fanconi anemia protein, FANCA, is regulated by Akt kinase.

Phosphorylation of the Fanconi anemia complementation group A (FANCA) protein is thought to be important for the function of the FA pathway. However, the kinase for FANCA (so-called FANCA-PK) remains to be identified. FANCA has a consensus sequence for Akt kinase near serine 1149 (Ser1149), suggesting that Akt can phosphorylate FANCA. We performed in vitro kinase assays using as substrate either a GST-fusion wild-type (WT) FANCA fragment or a GST-fusion FANCA fragment containing a mutation from serine to alanine at 1149 (FANCA-S1149A). These experiments confirmed that FANCA is phosphorylated at Ser 1149, in vitro. However, (32)P-orthophosphate labeling experiments revealed that FANCA-S1149A was more efficiently phosphorylated than WT-FANCA. Furthermore, phosphorylation of wild-type FANCA was blocked by coexpression of a constitutively active (CA)-Akt and enhanced by a dominant-negative (DN) Akt. Our results suggest that Akt is a negative regulator of FANCA phosphorylation.