Análisis de los factores de riesgo del cáncer de mama desde la farmacia comunitaria / Evaluation of risk factors of breast cancer in comunitary pharmacies

Introducción: El cáncer de mama es la neoplasia maligna más frecuente entre las mujeres, y en España es la que produce mayor número de muertes al año. La detección precoz propicia tratamientos menos agresivos y mayores tasas de curación. El objetivo de este estudio es analizar los factores de riesgo de las mujeres que acudieron a las ofi inas de farmacia participantes en el estudio: antecedentes familiares, edad y sexo, edad de concepción, enfermedad mamaria benigna, sobrepeso u obesidad, terapia hormonal (anticonceptivos orales o terapia hormonal sustitutiva), tabaco y alcohol. Material y métodos: En el estudio participaron cinco oficinas de farmacia de distintas provincias. Para el análisis de los factores de riesgo se entregó a las mujeres una breve encuesta que debían completar. Resultados y conclusiones: Tras analizar los factores de riesgo, se concluye que un 12% de las mujeres participantes tiene un riesgo elevado de padecer cáncer de mama. Desde la farmacia se puede informar a las mujeres sobre los factores de riesgo del cáncer de mama, con el fin de que apliquen las medidas necesarias para prevenir y/o detectar a tiempo esta enfermedad(AU)

Introduction: Cancer of breast is the malignant neoplasia more frequent between the women; in Spain it is the one that produces major number of deaths in a year. Early detection enables less aggressive treatments and the cure rate is greater. Objectives: In this study we analyze the following factors of risk: familiar precedents, age and sex, age of conception, mammary benign disease, overweight or obesity, hormonal therapy (oral contraceptives or hormonal substitute therapy), tobacco and alcohol of the women that came to the pharmacies. Material and methods: In the study there took part five pharmacies of different provinces. For the analysis of the factors of risk the woman was completing a brief questionnaire. Results and conclusions: The results indicate that 12% of the women participants have high risk of suffering cancer of breast. The pharmacist can form women on the risk factors of breast cancer to implement the necessary measures to prevent and/or detect early this disease(AU)

Educación sanitaria en la farmacia comunitaria: estudio controlado en la provincia de Castellón / No disponible

Introducción: La educación para la salud es una de las actividades que debe realizar el farmacéutico comunitario orientada hacia el paciente. Con el objetivo de conocer la influencia de la educación sanitaria en los pacientes, se realizó un estudio controlado en farmacias comunitarias de la provincia de Castellón.Material y métodos: En el estudio participaron catorce oficinas de farmacia (siete en el grupo control y siete en el grupo intervención). En todas ellas se realizó una encuesta inicial a los pacientes sobre educación para la salud. En las farmacias del grupo intervención se realizaron cinco campañas de educación sanitaria y al finalizar cada campaña los pacientes completaron una encuesta para valorar la educación sanitaria recibida. En las farmacias del grupo control se pasaron las encuestas a los pacientes pero no se realizaron las campañas de educación sanitaria.Resultados y discusión: Los pacientes están significativamente más satisfechos con la formación que reciben en las farmacias que realizan educación sanitaria. Además, se incrementa significativamente la percepción que tiene la población del farmacéutico en la oficina de farmacia como punto de referencia a la hora de ayudar a resolver sus problemas de salud. La educación sanitaria permite que los pacientes reciban formación completa acerca de temas de salud que les preocupan y les proporciona más capacidad para resolverlos por ellos mismos(AU)

Introduction: Health education is one of the roles of the community pharmacist.A controlled study of pharmacies in the Spanish province of Castellón was carried out with the aim of determining the influence of health education on the general public.Material and methods: Fourteen pharmacies took part in the study: seven in the group control and seven in the intervention group. An initial survey about health education was conducted among the patients of all fourteen pharmacies. In the pharmacies in the intervention group five campaigns of health education were instigated; after each campaign patients answered a survey to evaluate the health education received. In the pharmacies in the control group the same surveys were carried out without the implementation of any educational campaigns.Results and discussion: Patients of the pharmacies in the intervention group were significantly more satisfied with their level of knowledge about health matters than those in the control other group. In addition, the same patients had a significantly more satisfied with the formation they received in the pharmacies that implemented the educational campaigns. In addition, patients of the pharmacies in the intervention group had a significantly better perception of the pharmacist and of the pharmacy as a reference point with respect to resolving their health problems. Health education informs patients about aspects of health and endows them with the aptitude to make decisions related to their health problems(AU)

Transdermal iontophoresis of dexamethasone sodium phosphate in vitro and in vivo: effect of experimental parameters and skin type on drug stability and transport kinetics.

The aim of this study was to investigate the cathodal iontophoresis of dexamethasone sodium phosphate (DEX-P) in vitro and in vivo and to determine the feasibility of delivering therapeutic amounts of the drug for the treatment of chemotherapy-induced emesis. Stability studies, performed to investigate the susceptibility of the phosphate ester linkage to hydrolysis, confirmed that conversion of DEX-P to dexamethasone (DEX) upon exposure to samples of human, porcine and rat dermis for 7 h was limited (82.2+/-0.4%, 72.5+/-4.8% and 78.6+/-6.0% remained intact) and did not point to any major inter-species differences. Iontophoretic transport of DEX-P across dermatomed porcine skin (0.75 mm thickness) was studied in vitro as a function of concentration (10, 20, 40 mM) and current density (0.1, 0.3, 0.5 mA cm(-2)) using flow-through diffusion cells. Increasing concentration of DEX-P from 10 to 40 mM resulted in a approximately 4-fold increase in cumulative permeation (35.65+/-23.20 and 137.90+/-53.90 microg cm(-2), respectively). Good linearity was also observed between DEX-P flux and the applied current density (i(d); 0.1, 0.3, 0.5 mA cm(-2); J(DEX) (microg cm(2) h(-1))=237.98 i(d)-21.32, r(2)=0.96). Moreover, separation of the DEX-P formulation from the cathode compartment by means of a salt bridge - hence removing competition from Cl(-) ions generated at the cathode - produced a 2-fold increase in steady-state iontophoretic flux (40 mM, 0.3 mA cm(-2); 20.98+/-7.96 and 41.82+/-11.98 microg cm(-2) h(-1), respectively). Pharmacokinetic parameters were determined in Wistar rats (40 mM DEX-P; 0.5 mA cm(-2) for 5h with Ag/AgCl electrodes and salt bridges). Results showed that DEX-P was almost completely converted to DEX in the bloodstream, and significant DEX levels were achieved rapidly. The flux across rat skin in vivo (1.66+/-0.20 microg cm(-2) min(-1)), calculated from the input rate, was not statistically different from the flux obtained in vitro across dermatomed porcine skin (1.79+/-0.49 microg cm(-2) min(-1)). The results suggest that DEX-P delivery rates would be sufficient for the management of chemotherapy-induced emesis.

Structure of the Fe-heme in the hemodimeric hemoglobin from Scapharca inaequivalvis and in the T721 mutant: an X-ray absorption spectroscopic study at low temperature.

The Fe site structure in the recombinant wild-type and T721 mutant of the cooperative homodimeric hemoglobin (HbI) of the mollusc Scapharca itnaequivalvis has been investigated by measuring the Fe K-edge X-ray absorption near edge structure (XANES) spectra of their oxy, deoxy and carbonmonoxy derivatives, and the cryogenic photoproducts of the carbonmonoxy derivatives at T = 12 K. According to our results, the Fe site geometry in T72I HbI-CO is quite similar to that of human carbonmonoxy hemoglobin (HbA-CO), while in native HbI-CO it seems intermediate between that of HbA-CO and sperm whale MbCO. The XANES spectra of oxy and deoxy derivatives are similar to the homologous spectra of human HbA, except for T72I HbI, for which the absorption edge is blue-shifted (about + 1 eV) towards the spectrum of the oxy form. XANES spectra of the cryogenic photoproducts of HbA-CO (HbA*), HbI-CO (HbI*) and mutant HbI-CO (T72I HbI*) were acquired under continuous illumination at 12 K. The Fe-heme structures of the three photoproducts are similar; however, while in the case of HbA* and HbI* the data indicate incomplete structural relaxation of the Fe-heme towards its deoxy-like (T) form, the relaxation in T72I HbI* is almost completely towards the proposed "high affinity" Fe-heme structure of T72I HbI. This evidence suggests that minor tertiary restraints affect the Fe-heme dynamics of T72I HbI, corresponding to a reduction of the energy necessary for the T --> R structural transition, which can contribute to the observed dramatic enhancement in oxygen affinity of this hemoprotein, and the decreased cooperativity.

Heterotropic effectors exert more significant strain on monoligated than on unligated hemoglobin.

The effect of allosteric effectors, such as inositol hexakisphosphate and/or bezafibrate, has been investigated on the unliganded human adult hemoglobin both spectroscopically (employing electronic absorption, circular dichroism, resonance Raman, and x-ray absorption near-edge spectroscopies) and functionally (following the kinetics of the first CO binding step up to a final 4% ligand saturation degree). All data indicate that the unliganded T-state is not perturbed by the interaction with either one or both effectors, suggesting that their functional influence is only exerted when a ligand molecule is bound to the heme. This is confirmed by the observation that CO dissociation from partially liganded hemoglobin (

Structural differences of ovalbumin and S-ovalbumin revealed by denaturing conditions.

We found, by circular dichroism and Raman spectroscopy measurements, that the secondary structure of the native ovalbumin and of its heat-stable form, called S-ovalbumin, is a probe of the structural differences between the two proteins. Small angle X-ray scattering and circular dichroism measurements performed on the two proteins under denaturing conditions, with different concentrations of guanidine hydrochloride, show the changes of the tertiary and secondary structure and a different pathway in the unfolding process. These experimental data confirm that the conversion of native ovalbumin into S-ovalbumin is irreversible and reveal that the response of the two proteins to the same chemical environment is different.

The dinuclear copper site structure of Agaricus bisporus tyrosinase in solution probed by X-ray absorption spectroscopy.

We have measured the x-ray absorption near edge structure (XANES) spectra of the enzyme tyrosinase from the mushroom Agaricus bisporus in solution in the oxy and deoxy forms. The spectra, obtained under the same conditions as the analogous forms of mollusc hemocyanin (Hc), show that the oxidation state of copper changes from Cu(II) (oxy form) to Cu(I) (deoxy form), and the copper active site(s) of A. bisporus tyrosinase in solution undergoes the same main conformational changes as Hc. We have applied the multiple scattering theory to simulate the XANES spectra of various alternative geometries of the copper site, accounting for the residual differences between Hc and tyrosinase. While oxy-Hc is reasonably fitted only by the pseudo-square-pyramidal geometry reported by its crystallographic data, oxytyrosinase can be fitted, starting from the Hc coordinates, either by distortions toward a pseudo-tetrahedral geometry, with inequivalent copper sites, or by an apically distorted square-pyramidal geometry (with an elongation of the apical distance of no more than 0.2 A).

Conformational changes involved in the switch from ovalbumin to S-ovalbumin.

For the first time a comparative study on conformational differences between native ovalbumin and its heat-stable form, called S-ovalbumin, using small angle x-ray scattering, is reported. To detect a different pathway in the folding mechanism of the two proteins, scattering measurements have been performed on ovalbumin and S-ovalbumin denatured with different concentrations of guanidine hydrochloride, and by heating the proteins at acid pH. The intensity scattering curves provide evidence that the intermediate states in the unfolding process are globular for both proteins while their compactness changes. The reported experimental results suggest that the ovalbumin to S-ovalbumin transformation can be considered a protein-switch triggered by changes in the chemical conditions of the protein environment. Because the conformational changes are likely to be of functional importance, we infer that the occurrence in vivo of S-ovalbumin is thus determined by the transformation of ovalbumin, with a functional role for embryonic development, into a new protein with a different function.

X-ray small angle scattering of the human transferrin protein aggregates. A fractal study.

X-ray small angle scattering experiments, using a pin hole SAXS camera with Synchrotron radiation source, have been performed to study the conformational changes of lyophilized samples of Apo-, Mono-, and Diferric- human transferrin. We report the experimental evidence that the analysis of the scattered intensity through the fractal theory may give information on the particle size and its variation upon iron binding.

Influence of globin structure on the heme in dromedary carbonmonoxyhemoglobin.

By use of X-ray absorption near-edge structure (XANES), circular dichroism, and visible absorption spectroscopies, dromedary carbonmonoxyhemoglobin has been characterized structurally and functionally. By consideration of the experimental results the following view emerges: (i) the quaternary structure is not the unique factor determining the tertiary environment around the heme, and (ii) the multiplicity of interactions between hemoglobin and solvent components induces a large number of globin conformations, which somehow affect the conformation of the heme such that the structural parameters (i.e., the doming of porphyrins, the movements of the iron relative to the heme plane, the distortion of the ligand field, and the change in the Fe-C-O angle) can be uncoupled.