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1.
Artigo em Inglês | MEDLINE | ID: mdl-36078778

RESUMO

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 (n = 30) or the intervention groups (n = 30). Before discharge, the control group was treated with general physiotherapy for their disease characteristics. The intervention group received the same programs before discharge; additionally, a simple house evaluation was conducted using the subject's home floor plan. A six-month follow-up survey was conducted on falls and near-falls after discharge, completed by 51 of the 60 subjects (85%). Within two months, falls occurred in 7.7% of the control group but not in the intervention group, after which, falls occurred in the intervention group, and no significant difference was noted between the two groups (three-month (p = 0.322) and six-month (p = 0.931) follow-ups). The intervention group had significantly fewer near-falls than the control group within three months (p = 0.034), but no significant difference was observed after three months. The results suggested that our program effectively expanded the role of an acute care hospital for discharged patients who need to transition from hospital care to home health care.


Assuntos
Serviços de Assistência Domiciliar , Modalidades de Fisioterapia , Idoso , Hospitais , Humanos
2.
Artigo em Inglês | MEDLINE | ID: mdl-35162608

RESUMO

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 (n = 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. A follow-up survey of falls and near-falls at home was performed using a monthly fall calendar for the 1-month period after discharge. Data on 81.5% of participants remained for the final analyses. No falls occurred in the intervention group; however, 4.3% of those in the control group experienced a fall. Near-falls were reported by 3.7% and 26.9% of the participants in the intervention and control groups, respectively. The proportion of participants who did not experience near-falls in the 1st month after discharge was lower in the intervention than in the control group (p = 0.018). In conclusion, the tailored fall-prevention program using home floor plans in multiple acute-care hospitals was effective in reducing falls and near-falls in discharged orthopedic patients.


Assuntos
Terapia por Exercício , Exercício Físico , Idoso , Humanos
3.
J Physiol Anthropol ; 26(2): 201-7, 2007 Mar.
Artigo em Inglês | MEDLINE | ID: mdl-17435366

RESUMO

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). The index of tryptophan taken at breakfast (Trp-Index) was calculated as tryptophan amount per one meal based on the tryptophan included in each 100 g of the foods and a standard amount of food per one meal. A significant positive-correlation between M-E scores and Trp-Index was not shown by relatively older students, aged 9-15 yrs (Pearson's test, r=0.044-0.123, p=0.071-0.505), whereas a significant positive correlation was shown by infants and young elementary school students aged 0-8 yrs (r=0.180, 0.258, p<0.001). The more frequently the infants had difficulty falling asleep at bedtime and waking up in the morning, the less the Trp-Indices taken at breakfast were (Kruskall-Wallis-test, p=0.027 for difficulty falling asleep; p=0.008 for difficulty waking up). The more frequently infants became angry even by a little trigger, or depressed, the lower (more evening-typed) the M-E scores were (Kruskal-Wallis test: p

Assuntos
Ritmo Circadiano/fisiologia , Ingestão de Alimentos , Processos Mentais/fisiologia , Triptofano/administração & dosagem , Adolescente , Criança , Pré-Escolar , Feminino , Humanos , Lactente , Recém-Nascido , Japão , Masculino , Sono/fisiologia , Inquéritos e Questionários , Triptofano/metabolismo
4.
Nature ; 432(7015): 361-8, 2004 Nov 18.
Artigo em Inglês | MEDLINE | ID: mdl-15448704

RESUMO

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 2.3 A resolution the structure of the calcium-ATPase of skeletal muscle sarcoplasmic reticulum, a representative P-type ATPase that is crystallized in the absence of Ca2+ but in the presence of magnesium fluoride, a stable phosphate analogue. This and other crystal structures determined previously provide atomic models for all four principal states in the reaction cycle. These structures show that the three cytoplasmic domains rearrange to move six out of ten transmembrane helices, thereby changing the affinity of the Ca2+-binding sites and the gating of the ion pathway. Release of ADP triggers the opening of the lumenal gate and release of phosphate its closure, effected mainly through movement of the A-domain, the actuator of transmembrane gates.


Assuntos
ATPases Transportadoras de Cálcio/química , ATPases Transportadoras de Cálcio/metabolismo , Fosfatos/química , Difosfato de Adenosina/metabolismo , Trifosfato de Adenosina/metabolismo , Sítios de Ligação , Cálcio/metabolismo , Catálise , Cristalização , Cristalografia por Raios X , Fluoretos/química , Fluoretos/metabolismo , Ativação do Canal Iônico , Compostos de Magnésio/química , Compostos de Magnésio/metabolismo , Modelos Moleculares , Fosforilação , Estrutura Secundária de Proteína , Estrutura Terciária de Proteína , Retículo Sarcoplasmático/enzimologia , Relação Estrutura-Atividade
5.
FEBS Lett ; 555(1): 106-10, 2003 Nov 27.
Artigo em Inglês | MEDLINE | ID: mdl-14630328

RESUMO

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.


Assuntos
ATPases Transportadoras de Cálcio/química , ATPases Transportadoras de Cálcio/metabolismo , Retículo Sarcoplasmático/enzimologia , Animais , Técnicas In Vitro , Transporte de Íons , Modelos Moleculares , Conformação Proteica , Estrutura Terciária de Proteína , Coelhos
6.
Transfusion ; 43(9): 1276-85, 2003 Sep.
Artigo em Inglês | MEDLINE | ID: mdl-12919431

RESUMO

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. STUDY DESIGN AND METHODS: One-day-old WBC-reduced whole-blood-derived PCs (WBPCs) were inoculated with bacteria at 100 to 500 CFU per mL. After 30 minutes, 2- to 3-mL aliquots were processed through a PLT-reducing filter into a sample pouch containing sodium polyanethol sulfonate and entrained air. After incubation at 35 degrees C for at least 24 hours, the %O2 was measured within the pouch. Noninoculated WBC-reduced WBPCs (n = 155), confirmed free of bacteria by routine culture, were tested in a like manner. Results from the latter group of WBC-reduced WBPCs were used to distinguish contaminated from noncontaminated units. RESULTS: After a 24-hour incubation at 35 degrees C, 195 (96.5%) of the 202 sample pouches obtained from inoculated units were detected by the BDS. After an additional 6 hours at room temperature, those that remained and were tested were found positive. None of the noninoculated controls produced a positive reading. CONCLUSION: The BDS is easy to use and provides good levels of sensitivity and specificity.


Assuntos
Bactérias/isolamento & purificação , Infecções Bacterianas/prevenção & controle , Técnicas Bacteriológicas/métodos , Plaquetas/microbiologia , Leucócitos/citologia , Oxigênio/análise , Bactérias/crescimento & desenvolvimento , Infecções Bacterianas/diagnóstico , Infecções Bacterianas/transmissão , Técnicas Bacteriológicas/instrumentação , Biomarcadores , Humanos , Transfusão de Plaquetas , Sensibilidade e Especificidade
7.
Ann N Y Acad Sci ; 986: 1-8, 2003 Apr.
Artigo em Inglês | MEDLINE | ID: mdl-12763767

RESUMO

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.


Assuntos
ATPases Transportadoras de Cálcio/química , Sítios de Ligação , Membrana Celular/enzimologia , Cristalografia por Raios X , Modelos Moleculares , Conformação Proteica , Estrutura Secundária de Proteína , ATPases Transportadoras de Cálcio do Retículo Sarcoplasmático , Tapsigargina/farmacocinética
8.
Biochemistry ; 41(38): 11405-10, 2002 Sep 24.
Artigo em Inglês | MEDLINE | ID: mdl-12234183

RESUMO

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. The ATPase protein in the E1-Ca(2) state is cleaved efficiently by Fe(2+) with H(2)O(2) and ascorbate assistance, yielding a 70-75 kDa carboxyl end fragment. Cleavage of the ATPase protein in the E2-TG state occurs within the same region, but with a more diffuse pattern, yielding multiple fragments within the 65-85 kDa range. When Fe(2+) catalysis is assisted by ascorbate only (in the absence of H(2)O(2)), cleavage at the same protein site occurs much more slowly, and is facilitated by ATP (or AMP-PNP) and Ca(2+). Amino acid sequencing indicates that protein cleavage occurs at and near Ser346, and is attributed to Fe(2+) bound to a primary Mg(2+) site near Ser346 and neighboring Glu696. In addition, incubation with Fe(2+) and ascorbate produces Ca(2+)- and ATP-dependent oxidation of the Thr441 side chain, as demonstrated by NaB(3)H(4) incorporation and analysis of fragments obtained by extensive trypsin digestion. This oxidation is attributed to bound Fe(2+)-ATP complex, as shown by structural modeling of the Mg(2+)-ATP complex at the substrate site.


Assuntos
Adenosina Trifosfatases/metabolismo , ATPase de Ca(2+) e Mg(2+)/química , ATPase de Ca(2+) e Mg(2+)/metabolismo , Ferro/farmacologia , Magnésio/farmacologia , Retículo Sarcoplasmático/enzimologia , Adenosina Trifosfatases/química , Trifosfato de Adenosina/metabolismo , Animais , Sítios de Ligação , ATPases Transportadoras de Cálcio/metabolismo , Ativação Enzimática , Cinética , Modelos Moleculares , Músculo Esquelético/enzimologia , Oxirredução , Conformação Proteica
9.
Nature ; 418(6898): 605-11, 2002 Aug 08.
Artigo em Inglês | MEDLINE | ID: mdl-12167852

RESUMO

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. Here we describe the structure of this ion pump at 3.1 A resolution in a Ca(2+)-free (E2) state, and compare it with that determined previously for the Ca(2+)-bound (E1Ca(2+)) state. The structure of the enzyme stabilized by thapsigargin, a potent inhibitor, shows large conformation differences from that in E1Ca(2+). Three cytoplasmic domains gather to form a single headpiece, and six of the ten transmembrane helices exhibit large-scale rearrangements. These rearrangements ensure the release of calcium ions into the lumen of sarcoplasmic reticulum and, on the cytoplasmic side, create a pathway for entry of new calcium ions.


Assuntos
ATPases Transportadoras de Cálcio/química , ATPases Transportadoras de Cálcio/metabolismo , Cálcio/metabolismo , Animais , Sítios de Ligação , ATPases Transportadoras de Cálcio/antagonistas & inibidores , Cristalografia por Raios X , Citoplasma/metabolismo , Ligação de Hidrogênio , Modelos Moleculares , Ligação Proteica , Estrutura Secundária de Proteína/efeitos dos fármacos , Estrutura Terciária de Proteína/efeitos dos fármacos , Coelhos , Retículo Sarcoplasmático/enzimologia , Tapsigargina/metabolismo , Tapsigargina/farmacologia
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