Publications by authors named "Hiromi Nomura"

We provided fall prevention programs using home floor plans for older adult patients discharged from an acute-care hospital and verified the fall prevention measures' effectiveness six months after discharge. The research design was a preliminary randomized controlled trial. Orthopedic patients with a falls' history were randomized to the control ( = 30) or the intervention groups ( = 30).

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This multicenter, preliminary, randomized controlled trial investigated the effect of a tailored fall-prevention program using home floor plans for discharged orthopedic patients aged ≥65 years who experienced ≥1 fall(s) in the past year ( = 72) at five acute-care hospitals. The control group received standard care (exercise to prevent recurrent falls), whereas the intervention group received a tailored fall-prevention program in addition to usual care. A physical therapist conducted the tailored education program using each patient's home floor plans before discharge.

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Tryptophan can be metabolized via 5-hydroxytryptamine=serotonin to melatonin by a series of 4 enzymes in pineal body. Lack of serotonin in body fluid in the brain during daytime can lead to several psychiatric disorders, while shortage of plasma-melatonin at night can be related to sleep disorders. The Morning-Evening (M-E) questionnaire and the original questionnaire including questions on sleep habits, mental symptoms, and contents of meals were administered to 1055 infants aged 0-6 yrs, 751 students attending an elementary school, and 473 students attending junior high school in Kochi City (33 degrees N).

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P-type ion transporting ATPases are ATP-powered ion pumps that establish ion concentration gradients across biological membranes. Transfer of bound cations to the lumenal or extracellular side occurs while the ATPase is phosphorylated. Here we report at 2.

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The structures of the Ca(2+)-ATPase (SERCA1a) have been determined for five different states by X-ray crystallography. Detailed comparison of the structures in the Ca(2+)-bound form and unbound (but thapsigargin-bound) form reveals that very large rearrangements of the transmembrane helices take place accompanying Ca2+ dissociation and binding and that they are mechanically linked with equally large movements of the cytoplasmic domains. The meanings of the rearrangements of the transmembrane helices and those of the cytoplasmic domains, and the mechanistic roles of the phosphorylation are now becoming clear.

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Background: The risk of receiving a PLT concentrate (PC) contaminated with bacteria may be 1000-fold greater than that of pathogenic viral transmission, yet surveillance for this risk is not generally practiced. A novel bacteria detection system (BDS) that overcomes the limitations of current systems is described. The BDS monitors percent oxygen (%O2) in air above aliquots of PCs that have been filtered to remove the confounding effect of respiring PLTs and residual WBCs.

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The structures of the Ca(2+)-ATPase (SERCA1a) in different physiological states were determined by X-ray crystallography. Detailed comparison of the structures in the Ca(2+)-bound form and unbound (but thapsigargin bound) form reveals that very large rearrangements of the transmembrane helices take place accompanying Ca(2+) dissociation and binding and that they are mechanically linked with equally large movements of the cytoplasmic domains. The meaning of the rearrangement of the transmembrane helices becomes apparent by homology modeling of the Na(+)K(+)-ATPase.

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Fe(2+) can substitute for Mg(2+) in activation of the sarcoplasmic reticulum (SR) ATPase, permitting approximately 25% activity in the presence of Ca(2+). Therefore, we used Fe(2+) to obtain information on the binding sites for Mg(2+) and the Mg(2+)-ATP complex within the enzyme structure. When the ATPase is incubated with Fe(2+) in the presence of H(2)O(2) and/or ascorbate, specific patterns of Fe(2+)-catalyzed oxidation and cleavage are observed in the SR ATPase, depending on its Ca(2+)-bound (E1-Ca(2)) or Ca(2+)-free conformation (E2-TG), as well as on the presence of ATP.

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In skeletal muscle, calcium ions are transported (pumped) against a concentration gradient from the cytoplasm into the sarcoplasmic reticulum, an intracellular organelle. This causes muscle cells to relax after cytosolic calcium increases during excitation. The Ca(2+) ATPase that carries out this pumping is a representative P-type ion-transporting ATPase.

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