RESUMEN
BACKGROUND: Patient satisfaction represents an essential part of quality management. Measuring the degree of patient satisfaction can be achieved with a variety of tools such as postoperative visits and patient questionnaires. The primary aim of this study was to quantify the degree of patient satisfaction with anaesthesia. A secondary aim was to compare the questionnaire technique with standardised face-to-face interviewing. METHODS: The authors prospectively studied 700 patients on the second postoperative day. Patients were randomised and allocated to complete either a written questionnaire or to answer the same questions during a standardised face-to-face interview. The questionnaire was subdivided into a set of questions on anaesthesia-related discomfort and another set on satisfaction with anaesthesia care in general. The questions on discomfort were assessed on a 3-point scale, and those on patient satisfaction on a 4-point scale. RESULTS: Response rate was 84% (589 of 700 patients). Internal consistency, as measured by Cronbach's alpha, was 0.84. When evaluating the questions on anaesthesia-related discomfort, the most frequent sensations were "drowsiness" (>75%), "pain at the surgical site" (>55%), and "thirst" (>50%). The data on patient satisfaction showed a high degree of satisfaction (>90%). The responses to questions on anaesthesia-related discomfort revealed only minor differences between the questionnaire and the face-to-face interview. The questions on satisfaction with anaesthesia, however, were answered consistently in a more critical manner during the interview (P<0.0001). CONCLUSIONS: The standardised interview may be more suited to determine patient satisfaction than a questionnaire. Quality improvements are possible for emergence from anaesthesia, postoperative pain therapy, and the treatment of postoperative nausea and vomiting.
Asunto(s)
Anestesia , Satisfacción del Paciente/estadística & datos numéricos , Interpretación Estadística de Datos , Humanos , Entrevistas como Asunto , Garantía de la Calidad de Atención de Salud , Reproducibilidad de los Resultados , Encuestas y CuestionariosRESUMEN
Interleukin-5 (IL-5), expressed primarily by type-2 T helper (Th2) cells, plays an important role in the development of allergic diseases, such as allergic asthma. Studying the regulation of IL-5 gene expression by Ets transcription factors, we found that Ets1 and Ets2, but not Elf-1, were able to activate the human IL-5 promoter in Jurkat T-cells. This required the presence of either phorbol 12-myristate acetate (PMA) plus ionomycin or PMA plus the viral protein HTLV-I Tax1. By mutation studies, it could be shown that Ets1 and Ets2 exerted their effects on the IL-5 promoter through a GGAA motif within the Cle0 element. In myeloid Kasumi cells, Ets1 and Ets2 failed to stimulate IL-5 promoter activity, unless the T-cell specific transcription factor GATA3 was added. These results show, for the first time, that Ets1 and Ets2 are able to cooperate with GATA3. Both ionomycin and Tax1 increased the combined effect of GATA3 with Ets1 and Ets2 in the presence of PMA. The data further demonstrate that, in addition to Ets1, Ets2 is also able to functionally cooperate with Tax1. The synergism of GATA3 with either Ets1 or Ets2 may play an important role in calcium- or Tax1-dependent regulation of IL-5 expression in Th2 cells or in HTLV-I transformed adult T-cell leukemia cells, respectively.
Asunto(s)
Proteínas de Unión al ADN/metabolismo , Productos del Gen tax/metabolismo , Interleucina-5/genética , Regiones Promotoras Genéticas , Transactivadores/metabolismo , Factores de Transcripción/metabolismo , Secuencia de Bases , Células Cultivadas , Cartilla de ADN , Factor de Transcripción GATA3 , Humanos , Ionomicina/farmacología , Células Jurkat , Acetato de Tetradecanoilforbol/farmacología , Activación Transcripcional/efectos de los fármacosRESUMEN
Mutants of lactose permease of Escherichia coli with amino acid changes (Gly-24----Glu; Gly-24----Arg; Pro-28---Ser; Gly-24, Pro-28----Glu-Ser and Gly-24, Pro-28----Arg-Ser) within a putative membrane-spanning alpha-helix (Phe-Gly-Leu-Phe-Phe-Phe-Phe-Tyr-Phe-Phe-Ile-Met-Gly- Ala-Tyr-Phe-Pro-Phe-Phe-Pro-Ile) are incorporated into the cytoplasmic membrane. The mutant proteins retain the ability to bind galactosides, and the affinity for several substrates is actually increased. However, the rate of active transport is decreased to 0.01% of the wild-type rate in the mutants carrying Arg-24 or Arg-24, Ser-28. Kinetic analysis demonstrates that the two mutants require 10 min to cause occupied binding sites for galactoside and H+ to change their exposure from the periplasm to the cytoplasm as compared to 50 ms in the wild type. The effect is less pronounced when these sites are unoccupied.
Asunto(s)
Proteínas de Escherichia coli , Escherichia coli/enzimología , Proteínas de Transporte de Membrana/genética , Proteínas de Transporte de Monosacáridos , Simportadores , Translocación Genética , Secuencia de Aminoácidos , Transporte Biológico , ADN Bacteriano/análisis , Galactósidos/metabolismo , Cinética , Proteínas de Transporte de Membrana/metabolismo , MutaciónRESUMEN
The pharmacokinetics of CGP 15 210 G, a new 5-HT uptake inhibitor in poor and extensive metabolisers of debrisoquine, give indirect evidence of an association between its metabolism and polymorphic hydroxylation of the debrisoquine type.
Asunto(s)
Debrisoquina/metabolismo , Isoquinolinas/metabolismo , Piperidinas/metabolismo , Adulto , Evaluación de Medicamentos , Femenino , Humanos , Hidroxilación , Cinética , Masculino , Fenotipo , Polimorfismo Genético , Serotonina/metabolismoRESUMEN
The previously described hybrid plasmid pC7 which carries lacI+O+delta(Z)Y+A+ on a 12.3 X 10(6)-Mr DNA fragment [Teather et al. (1978) Mol. Gen. Genet. 159, 239-248] was partially digested with the restriction endonuclease EcoRI under conditions reducing the recognition sequence to d(A-A-T-T) and ligated to the vector pB322. lac Y-carrying inserts of various sized (Mr 1.5-4.7 X 10(6)) were obtained. Hybrid plasmid pTE18 (2300-base-pair insert) carries part of the I (repressor) gene, the promotor-operator region, part of the Z (beta-galactosidase) gene, the Y (lactose carrier) gene and part of the A (transacetylase) gene. Upon induction of pTE18-harbouring strains the Y-gene product is expressed at a nearly constant rate for several generations and accumulates to a level of 12-16% of the total cytoplasmic membrane protein. Integration into the membrane leads to active carrier as judged by binding and transport measurements.
Asunto(s)
Proteínas Bacterianas/genética , Proteínas Portadoras/genética , Operón Lac , Proteínas de Transporte de Membrana/genética , Plásmidos , Clonación Molecular/métodos , Enzimas de Restricción del ADN/metabolismo , Genes , Lactosa/metabolismo , Proteínas de la Membrana/genéticaRESUMEN
The elevated level of lactose carrier protein present in cytoplasmic membranes derived from Escherichia coli strain T31RT, which carries the Y gene of the lac operon on a plasmid vector (Teather, R. M., et al. (1978) Mol. Gen. Genet. 159, 239--248), has allowed the detection of a complex between the carrier and the fluorescent substrate 2'-(N-dansyl)-aminoethyl beta-D-thiogalactopyranoside (Dns2-S-Gal). Binding is accompanied by a 50-nm blue shift in the emission maximum of the dansyl residue. The complex (dissociation constant, KD = 30 micron) rapidly dissociates upon addition of competing substrates such as beta-D-galactopyranosyl 1-thio-beta-D-galactopyranoside or upon reaction with the thiol reagent p-chloromercuribenzenesulfonate. Binding of both Dns2-S-Gal and p-nitrophenyl alpha-D-galactopyranoside (alpha-NPG) occurs spontaneously in the absence of an electrochemical potential gradient across the membrane. Comparison of equilibrium binding experiments using Dns2-S-Gal or alpha-NPG and differential labeling of the carrier with radioactive amino acids shows that the carrier binds 1 mol of substrate per mol of polypeptide (molecular weight 30 000). In addition to specific binding to the lactose carrier, Dns2-S-gal binds unspecifically to lipid vesicles or membranes, as described by a partition coefficient, K = 60, resulting in a 25-nm blue shift in the emission maximum of the dansyl group. Both Dns2-S-Gal and alpha-NPG are not only bound by the lactose carrier but also transported across the membrane by this transport protein in cells and membrane vesicles. The fluorescence changes observed with dansylated galactosides in membrane vesicles in the presence of an electrochemical gradient (Schuldiner et al. (1975) J. Biol. Chem. 250, 1361--1370)) are interpreted as an increase in unspecific binding after translocation.
Asunto(s)
Proteínas Portadoras/metabolismo , Escherichia coli/metabolismo , Glicósidos/metabolismo , Lactosa/metabolismo , Proteínas de Transporte de Membrana/metabolismo , Nitrofenilgalactósidos/metabolismo , Tiogalactósidos/metabolismo , Tioglicósidos/metabolismo , Transporte Biológico Activo , Membrana Celular/metabolismo , Cinética , Peso Molecular , Unión Proteica , EspectrofotometríaRESUMEN
The isolation and properties of a hybrid plasmid carrying the Y gene of the lac operon of Escherichia coli are described. The lactose carrier protein, coded for by the Y gene, is readily identified upon lac operon induction in strains carrying the plasmid. The protein comprises about 15% of the cytoplasmic membrane protein synthesized in the first generation after induction, compared with a wild type strain induced under the same conditions where lactose carrier protein comprises 1.4% of the cytoplasmic membrane protein.