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1.
BMC Anesthesiol ; 20(1): 141, 2020 06 03.
Artigo em Inglês | MEDLINE | ID: mdl-32493281

RESUMO

BACKGROUND: The volume effect of iso-oncotic colloid is supposedly larger than crystalloid, but such differences are dependent on clinical context. The purpose of this single center observational study was to compare the volume and hemodynamic effects of crystalloid solution and colloid solution during surgical manipulation in patients undergoing major abdominal surgery. METHODS: Subjects undergoing abdominal surgery for malignancies with intraoperative goal-directed fluid management were enrolled in this observational study. Fluid challenges consisted with 250 ml of either bicarbonate Ringer solution, 6% hydroxyethyl starch or 5% albumin were provided to maintain optimal stroke volume index. Hematocrit derived-plasma volume and colloid osmotic pressure was determined immediately before and 30 min after the fluid challenge. Data were expressed as median (IQR) and statistically compared with Kruskal-Wallis test. RESULTS: One hundred thirty-nine fluid challenges in 65 patients were analyzed. Bicarbonate Ringer solution, 6% hydroxyethyl starch and 5% albumin were administered in 42, 49 and 48 instances, respectively. Plasma volume increased 7.3 (3.6-10.0) % and 6.3 (1.4-8.8) % 30 min after the fluid challenge with 6% hydroxyethyl starch and 5% albumin and these values are significantly larger than the value with bicarbonate Ringer solution (1.0 (- 2.7-2.3) %) Colloid osmotic pressure increased 0.6 (0.2-1.2) mmHg after the fluid challenge with 6% hydroxyethyl starch and 0.7(0.2-1.3) mmHg with 5% albumin but decreased 0.6 (0.2-1.2) mmHg after the fluid challenge with bicarbonate Ringer solution. The area under the curve of stroke volume index after fluid challenge was significantly larger after 6% hydroxyethyl starch or 5% albumin compared to bicarbonate Ringer solution. CONCLUSIONS: Fluid challenge with 6% hydroxyethyl starch and 5% albumin showed significantly larger volume and hemodynamic effects compared to bicarbonate Ringer solution during gastrointestinal surgery. TRIAL REGISTRATION: UMIN Clinical Trial Registry UMIN000017964. Registered July 01, 2015.


Assuntos
Abdome/cirurgia , Albuminas/farmacologia , Soluções Cristaloides/farmacologia , Hidratação/métodos , Hemodinâmica/efeitos dos fármacos , Derivados de Hidroxietil Amido/farmacologia , Feminino , Humanos , Masculino , Estudos Prospectivos
2.
Artigo em Inglês | MEDLINE | ID: mdl-27604699

RESUMO

In wild Aplysia, the birthdate of animals can typically not be determined. Therefore, we sought a reliable index of old age by taking into consideration the distinguished Japanese seasons. Large amounts of eggs and dead bodies were present on the coast during and after the second half of May (MayS). Body mass decreased after May. We roughly classified animals collected before and after the MayS as mature and old animals. Plots of internalized shell length (S) against body mass (B) gave distinct best-fit curves for mature and old animals. The B/S significantly decreased in the second half of June, suggesting that body mass decreases with age but shell length is maintained in each animal. Therefore, the collected animals were classified into mature and old animals using the best-fit curves for animals classified by the collection period. We examined the amount of food intake every 2 h up to 8 h after providing food. The amounts increased linearly, and the rate was significantly lower in old animals than in mature animals. The amount of 1-day food intake was also significantly lower in old animals. These results suggest that food intake may decline with age and this may cause mass loss in old animals.


Assuntos
Envelhecimento/fisiologia , Aplysia/fisiologia , Ingestão de Alimentos/fisiologia , Comportamento Alimentar/fisiologia , Análise de Variância , Exoesqueleto/anatomia & histologia , Exoesqueleto/crescimento & desenvolvimento , Animais , Aplysia/anatomia & histologia , Aplysia/crescimento & desenvolvimento , Peso Corporal , Tamanho do Órgão , Análise de Regressão , Estações do Ano
3.
ACS Appl Mater Interfaces ; 6(21): 19355-9, 2014 Nov 12.
Artigo em Inglês | MEDLINE | ID: mdl-25296395

RESUMO

Water vapor barriers are important in various application fields, such as food packaging and sealants in electronic devices. Polymer/clay composites are well-studied water vapor barrier materials, but their transparency and mechanical strength degrade with increasing clay loading. Herein, we demonstrate films with good water vapor barrier properties, high transparency, and mechanical/thermal stability. Water vapor barrier films were prepared by the solution crystallization of siloxane hybrid lamellae. The films consist of highly crystallized organic/inorganic hybrid lamellae, which provide high transparency, hardness, and thermal stability and inhibit the permeation of water vapor. The water permeability of a 6 µm thick hybrid film is comparable to that of a 200 µm thick silicon rubber film.

4.
J Neuroimmunol ; 236(1-2): 27-38, 2011 Jul.
Artigo em Inglês | MEDLINE | ID: mdl-21641049

RESUMO

In Alzheimer's disease (AD), amyloid-ß (Aß) peptides accumulate in the brain in different forms, including fibrils and oligomers. Recently, we established three distinct conformation-dependent human single-chain Fv (scFv) antibodies, including B6 scFv, which bound to Aß42 fibril but not to soluble-form Aß, inhibiting Aß42 fibril formation. In this study, we determined the mimotopes of these antibodies and found a common mimotope sequence, B6-C15, using the Ph.D.-C7C phage library. The B6-C15 showed weak homology to the C-terminus of Aß42 containing GXXXG dimerization motifs. We synthesized the peptide of B6-C15 fused with biotinylated TAT at the N-terminus (TAT-B6-C15) and characterized its biochemical features on an Aß42-fibrillation reaction in vitro. We demonstrated that, first, TAT-B6-C15 inhibited Aß42 fibril formation; secondly, TAT-B6-C15 bound to prefibril Aß42 oligomers but not to monomers, trimers, tetramers, fibrils, or ultrasonicated fragments; thirdly, TAT-B6-C15 inhibited Aß42-induced cytotoxicity against human SH-SY5Y neuroblastoma cells; and, fourthly, when mice were administered B6-C15-phages dissolved in phosphate-buffered saline, the anti-Aß42 conformer IgG antibody response was induced. These results suggested that the B6-C15 peptide might provide unique opportunities to analyze the Aß42 fibrillation pathway and develop a vaccine vehicle for Alzheimer's disease.


Assuntos
Peptídeos beta-Amiloides/antagonistas & inibidores , Peptídeos beta-Amiloides/imunologia , Amiloide/antagonistas & inibidores , Amiloide/imunologia , Bacteriófago M13/metabolismo , Mimetismo Molecular/imunologia , Fragmentos de Peptídeos/fisiologia , Anticorpos de Cadeia Única/fisiologia , Sequência de Aminoácidos , Amiloide/biossíntese , Peptídeos beta-Amiloides/metabolismo , Animais , Especificidade de Anticorpos , Bacteriófago M13/imunologia , Linhagem Celular Tumoral , Humanos , Imunoglobulina G/biossíntese , Imunoglobulina G/fisiologia , Camundongos , Camundongos Endogâmicos BALB C , Camundongos Endogâmicos C57BL , Camundongos Transgênicos , Dados de Sequência Molecular , Fragmentos de Peptídeos/antagonistas & inibidores , Fragmentos de Peptídeos/síntese química , Fragmentos de Peptídeos/imunologia , Fragmentos de Peptídeos/metabolismo , Conformação Proteica , Anticorpos de Cadeia Única/biossíntese
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