Non-linear phase different control for precise output force of bi-articularly actuated manipulators

Bi-articular actuators – actuator spanning two joints – play fundamental role in robot arms designed under the human musculoskeletal actuation paradigm. Unlike kinematic redundancy, actuator redundancy resulting from bi-articular actuation brings advantages such as increasing stability, reducing link's inertia, and decreasing non-linearity of the end-effector force with respect to the force direction. The traditional phase different control (PDC) resolves actuator redundancy on the basis of a linearized model derived from measured human muscle activity. Such linear model produces a non-zero error in calculation between a desired output force and necessary inputs. In this paper, the non-linear phase different control (NLPDC) is proposed to resolve actuator redundancy with no error. The maximum end-effector force of BiWi, bi-articularly actuated, and wire-driven arm, is measured using both PDC and NLPDC. When the robot arm moves towards singular configurations, the measured error in output force remains within the modeling error if using NLPDC, while such error increases significantly for PDC. Furthermore, unlike PDC, the proposed NLPDC allows design of joint stiffness and torque independently, reduction of necessary total muscle input force, and precise calculation of maximum output force.     

Identification of melanoma‐specific serological markers using proteomic analyses

The discovery of novel melanoma markers for not only early detection but also monitoring disease status is promising to improve the clinical outcome of patients. In the present study, we performed proteomic comparative analysis of plasma proteins between healthy volunteers and melanoma patients using NanoLC and MALDI‐TOF‐MS. As a result, we were successful in identifying nine proteins that were specifically expressed in melanoma plasma compared with healthy plasma, most of which had not previously been identified as plasma markers of melanoma. The mRNA expression levels of four proteins [pro‐platelet basic protein precursor (PPBP), serum amyloid A2 (SAA2), complement factor H‐related protein 1 precursor (FHR1), inter‐alpha‐trypsin inhibitor heavy chain H4 precursor (IAIH4)] were prominently up‐regulated in several melanoma cell lines compared with melanocytes. Moreover, two proteins (PPBP, SAA) were shown to be expressed in tumor specimens from melanoma patients. In the survival time analysis regarding melanoma patients, the semi‐quantified plasma PPBP levels were statistically negatively correlated with the survival time. Most interestingly, the significant survival benefit was seen in low PBPP level group (< index 20) versus high level (≥ index 20) group. The results suggest that PPBP might be a novel promising serological marker and a prognostic factor specific to melanomas.     

Synthesis of Hexabenzo[a,cd,f,j,lm,o]perylene

Hexabenzo[a,cd,f,j,lm,o]perylene (HBP), an undecacyclic condensed polycyclic aromatic hydrocarbon with two severely crowded fjord regions, was synthesized by Clar's method; the starting material 8H-benzo[fg]-naphthacene-8-one was newly prepared by the glycerol condensation of 5,12-dihydro-naphthacene-5,12-dione. ¹H and ¹³C NMR spectra of HBP were measured and the chemical shifts were completely assigned. Absorption and fluorescence spectra of HBP were also measured and the effects of nonplanarity on its spectroscopic properties was discussed.     

Transport of carnitine and acetylcarnitine by carnitine/organic cation transporter (OCTN) 2 and OCTN3 into epididymal spermatozoa

Carnitine and acetylcarnitine are important for the acquisition of motility and maturation of spermatozoa in the epididymis. In this study, we examined the involvement of carnitine/organic cation transporter (OCTN) in carnitine and acetylcarnitine transport in epididymal spermatozoa of mice. Uptake of both compounds by epididymal spermatozoa was time-dependent and partially Na(+)-dependent. Kinetic analyses revealed the presence of a high-affinity transport system in the spermatozoa, with K(m) values of 23.6 and 6.57 muM for carnitine and acetylcarnitine respectively in the presence of Na(+). Expression of OCTN2 and OCTN3 in epididymal spermatozoa was confirmed by immunofluorescence analysis. The involvement of these two transporters in carnitine and acetylcarnitine transport was supported by a selective inhibition study. We conclude that both Na(+)-dependent and -independent carnitine transporters, OCTN2 and OCTN3, mediate the supply of carnitine and acetylcarnitine to epididymal spermatozoa in mice.