Wearable Power-Assist Locomotor for Gait Reconstruction in Patients With Spinal Cord Injury: A Retrospective Study.

Wearable robotic exoskeletons (WREs) have been developed from orthoses as assistive devices for gait reconstruction in patients with spinal cord injury. They can solve some problems encountered with orthoses, such as difficulty in independent walking and standing up and high energy consumption during walking. The Wearable Power-Assist Locomotor (WPAL), a WRE, was developed based on a knee-ankle-foot orthosis with a single medial hip joint. The WPAL has been updated seven times during the period from the beginning of its development, in 2005, to 2020. The latest version, launched as a commercialized model in 2016, is available for medical facilities. In this retrospective study, which included updated results from previous reports, all data were extracted from development research records from July 2007 to December 2020. The records were as follows: patient characteristics [the number of participants, injury level, and the American Spinal Injury Association Impairment Scale (AIS) score], the total number of WPAL trials when aggregating the cases with all the versions or only the latest version of the WPAL, and maximum walking performance (functional ambulation category [FAC], distance, and time of continuous walking). Thirty-one patients participated in the development research. The levels of spinal cord injury were cervical (C5-C8), upper thoracic (T3-T6), lower thoracic (T7-T12), and lumbar (L1) in 10, 5, 15, and 1 of the patients, respectively. The numbers of patients with AIS scores of A, B, C, and D were 20, 7, 4, and 0, respectively. The total number of WPAL trials was 1,785, of which 1,009 were used the latest version of the WPAL. Twenty of the patients achieved an FAC score of 4 after an average of 9 (median 8, range 2-22) WPAL trials. The continuous walking distance and time improved with the WPAL were compared to the orthosis. We confirmed that the WPAL improves walking independence in people with a wide range of spinal cord injuries, such as cervical spinal cord injuries. Further refinement of the WPAL will enable its long-term use at home.

Drastic changes in the ligand structure of the oxygen-evolving Mn cluster upon Ca2+ depletion as revealed by FTIR difference spectroscopy.

A Fourier transform infrared (FTIR) difference spectrum of the oxygen-evolving Mn cluster upon the S(1)-to-S(2) transition was obtained with Ca(2+)-depleted photosystem II (PSII) membranes to investigate the structural relevance of Ca(2+) to the Mn cluster. Previously, Noguchi et al. [Biochim. Biophys. Acta 1228 (1995) 189] observed drastic changes in the carboxylate stretching region of the S(2)/S(1) FTIR spectrum upon Ca(2+) depletion, whereas Kimura and co-workers [Biochemistry 40 (2001) 14061; ibid. 41 (2002) 5844] later claimed that these changes were not ascribed to Ca(2+) depletion itself but caused by the interaction of EDTA to the Mn cluster and/or binding of K(+) at the Ca(2+) site. In the present study, the preparation of the Ca(2+)-depleted PSII sample and its FTIR measurement were performed in the absence of EDTA and K(+). The obtained S(2)/S(1) spectrum exhibited the loss of carboxylate bands at 1587/1562 and 1364/1403 cm(-1) and diminished amide I intensities, which were identical to the previous observations in the presence of EDTA and K(+). This result indicates that the drastic FTIR changes are a pure effect of Ca(2+) depletion, and provides solid evidence for the general view that Ca(2+) is strongly coupled with the Mn cluster.

Structural perturbation of the carboxylate ligands to the manganese cluster upon Ca2+/Sr2+ exchange in the S-state cycle of photosynthetic oxygen evolution as studied by flash-induced FTIR difference spectroscopy.

A Ca(2+) ion is an indispensable element in the oxygen-evolving Mn cluster in photosystem II (PSII). To investigate the structural relevance of Ca(2+) to the Mn cluster, the effects of Sr(2+) substitution for Ca(2+) on the structures and reactions of ligands to the Mn cluster during the S-state cycle were investigated using flash-induced Fourier transform infrared (FTIR) difference spectroscopy. FTIR difference spectra representing the four S-state transitions, S(1) --> S(2), S(2) --> S(3), S(3) --> S(0), and S(0) --> S(1), were recorded by applying four consecutive flashes either to PSII core complexes from Thermosynechococcus elongatus or to PSII-enriched membranes from spinach. The spectra were also recorded using biosynthetically Sr(2+)-substituted PSII core complexes from T. elongatus and biochemically Sr(2+)-substituted PSII membranes from spinach. Several common spectral changes upon Sr(2+) substitution were observed in the COO(-) stretching region of the flash-induced spectra for both preparations, which were best expressed in Ca(2+)-minus-Sr(2+) double difference spectra. The significant intensity changes in the symmetric COO(-) peaks at approximately 1364 and approximately 1418 cm(-)(1) at the first flash were reversed as opposite intensity changes at the third flash, and the slight shift of the approximately 1446 cm(-)(1) peak at the second flash corresponded to the similar but opposite shift at the fourth flash. Analyses of these changes suggest that there are at least three carboxylate ligands whose structures are significantly perturbed by Ca(2+)/Sr(2+) exchange. They are (1) the carboxylate ligand having a bridging or unidentate structure in the S(2) and S(3) states and perturbed in the S(1) --> S(2) and S(3) --> S(0) transitions, (2) that with a chelating or bridging structure in the S(1) and S(0) states and perturbed also in the S(1) --> S(2) and S(3) --> S(0) transitions, and (3) that with a chelating structure in the S(3) and S(0) states and changes in the S(2) --> S(3) and S(0) --> S(1) transitions. Taking into account the recent FTIR studies using site-directed mutagenesis and/or isotope substitution [Chu et al. (2004) Biochemistry 43, 3152-3116; Kimura et al. (2005) J. Biol. Chem. 280, 2078-2083; Strickler et al. (2006) Biochemistry 45, 8801-8811], it was concluded that these carboxylate groups do not originate from either D1-Ala344 (C-terminus) or D1-Glu189, which are located near the Ca(2+) ion in the X-ray crystallographic model of the Mn cluster. It was thus proposed that if the X-ray model is correct, the above carboxylate groups sensitive to Sr(2+) substitution are ligands to the Mn ions strongly coupled to the Ca(2+) ion rather than direct ligands to Ca(2+).