Visual Biofeedback of Force Information for Eccentric Training of Hemiplegic Patients.

Motor learning issues for hemiplegics not only include motor impairments such as spastic paralysis, but reportedly also an inability to appropriately recognize somatic sensations. In this regard, biofeedback of movement information through visual information and auditory information has been found effective as a method for drawing attention to appropriate somatic sensations. In this context, here, we propose a novel eccentric training system utilizing visual biofeedback of force information. We first develop a compact and highly portable rehabilitation robot for home use. The robot estimates the force on the tiptoe without the use of a force sensor, and a display connected to the robot presents the force information to the trainee. Clinical trials with two chronic hemiplegics have been conducted. The results show that the timed up and go tests of both trainees are shortened after training twice a week for three weeks (six times in total). Simultaneously, the co-contraction index scores of the tibialis anterior and gastrocnemius muscles decrease. These findings in conjunction with previous results suggest that training with visual biofeedback of force information may enhance reciprocal inhibition of the tibialis anterior muscle and reduces co-contraction.

Characterization of the effects of C-terminal pro-sequence on self-inactivation of Stereum purpureum endopolygalacturonase I.

Endpolygalacturonase I from Stereum purpureum has been identified as a causative substance for the silver-leaf disease in apples. It possesses a unique pro-sequence in the C-terminal region that lacks endpolygalacturonases from any other origin. In this study, we analyzed and compared enzymatic characteristics between pro-form (pro-endoPG I) and mature form processed by V8 protease (endoPG I) and described the suppression activity of the pro-sequence. Of note, the optimal pH for pro-endoPG I activity shifted to pH 4.0 from pH 4.5-5.0 of endoPG I. The kinetic parameters indicated that the activity inhibition resulted from a pH-independent decrease of substrate affinity and pH-dependent deterioration of velocity by the pro-sequence. Analysis of site-directed mutations within pro-endoPG I showed that its α-helical structure includes two glutamates (E364 and E366) and alanine (A365), and its orientation by prolines (especially P348) in the pro-sequence played a significant role in its suppression activity. As for mutations in the mature domain, a marked reduction of suppression was observed for enzymes with mutations in H150, R220 and K253, indicating that the pro-sequence interacts with the active cleft by a few ionic bonds.