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PURPOSE: To investigate the effect of systemic anti-androgen drugs on tear function tests and the ocular surface. METHODS: Sixty-four male subjects were included in this study. Subjects who were on anti-androgen treatment for prostate cancer (Group A, n: 31) and those who had received only surgical treatment for prostate cancer (Group B, n: 17) were recruited from the department of urology. Age-matched subjects who had never received anti-androgen treatment (Group C, n: 16) constituted the control group. Group A was divided into two subgroups according to the number of anti-androgen drugs used (Group A1: one drug, Group A2: two drugs). All cases underwent a complete ocular examination, including tear film break up time (TBUT), corneal and conjunctival staining, Schirmer 1 test, conjunctival impression cytology, and ocular surface disease index (OSDI) questionnaire. RESULTS: The mean Schirmer's values were 6.87mm, 11.41mm, and 13.03mm in Groups A, B, and C, respectively (P=0.001). TBUT was 5.45±2.01, 9.85±2.52 and 9.81±1.96seconds in Groups A, B, and C, respectively (P=0.001). Schirmer and TBUT were significantly lower, and corneal staining and OSDI questionnaire scores were higher in Group A compared to groups B and C (P<0.01). Conjunctival impression cytology results according to the Nelson grading system revealed no statistically significant difference between the groups (P=0.422). CONCLUSION: Anti-androgen drugs alter tear function tests, cause increased corneal and conjunctival staining scores and worsen complaints of dry eye in patients with prostate cancer.
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Síndromes de Ojo Seco , Neoplasias de la Próstata , Conjuntiva , Córnea , Síndromes de Ojo Seco/diagnóstico , Síndromes de Ojo Seco/tratamiento farmacológico , Síndromes de Ojo Seco/etiología , Humanos , Masculino , LágrimasRESUMEN
Abstract NUMEN proposes cross sections measurements of Heavy-Ion double charge exchange reactions as an innovative tool to access the nuclear matrix elements, entering the expression of the life time of Neutrinoless double beta decay (0νββ). A key aspect of the projectis the use at INFN-Laboratori Nazionali del Sud (LNS) of the Superconducting Cyclotron (CS) for the acceleration of the required high resolution and low emittance heavy-ion beams and of MAGNEX large acceptance magnetic spectrometer for the detection of the ejectiles. The experimental measurements of double charge exchange reactions induced by heavy ions present a number of challenging aspects, since such reactions are characterized by very low cross sections. First experimental results give encouraging indication on the capability to access quantitative information towards the determination of the Nuclear Matrix Elements for 0νββ decay.
Resumen NUMEN propone mediciones de secciones eficaces de reacciones de intercambio de carga doble de iones pesados como una herramienta innovadora para acceder a los elementos de la matriz nuclear, entrando en la expresión del tiempo de vida de la desintegración beta doble sin neutrino (0νββ). Un aspecto clave del proyecto es el uso en INFN-Laboratori Nazionali del Sud (LNS) del ciclotrón superconductor (CS) para la aceleración de los haces de iones pesados de alta resolución y baja emitancia requeridos y del espectrómetro magnético de gran aceptación MAGNEX para la detección de los residuos eyectados. Las mediciones experimentales de reacciones de intercambio de carga doble inducidas por iones pesados presentan una serie de aspectos desafiantes, ya que tales reacciones se caracterizan por secciones eficaces muy bajas. Los primeros resultados experimentales dan una indicación alentadora sobre la capacidad de acceder a información cuantitativa para la determinación de los Elementos de la Matriz Nuclear para la descomposición de 0νββ.
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Pseudomonas putida contains an amine dehydrogenase that is called a quinohemoprotein as it contains a quinone and two hemes c as redox active groups. Amino acid sequence analysis of the smallest (8.5 kDa), quinone-cofactor-bearing subunit of this heterotrimeric enzyme encountered difficulties in the interpretation of the results at several sites of the polypeptide chain. As this suggested posttranslational modifications of the subunit, the structural genes for this enzyme were determined and mass spectrometric de novo sequencing was applied to several peptides obtained by chemical or enzymatic cleavage. In agreement with the interpretation of the X-ray electronic densities in the diffraction data for the holoenzyme, our results show that the polypeptide of the small subunit contains four intrachain cross-linkages in which the sulfur atom of a cysteine residue is involved. Two of these cross-linkages occur with the beta-carbon atom of an aspartic acid, one with the gamma-carbon atom of a glutamic acid and the fourth with a tryptophanquinone residue, this adduct constituting the enzyme's quinone cofactor, CTQ. The thioether type bond in all four of these adducts has never been found in other proteins. CTQ is a novel cofactor in the series of the recently discovered quinone cofactors.
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Cisteína/química , Indolquinonas , Oxidorreductasas actuantes sobre Donantes de Grupo CH-NH/química , Pseudomonas putida/enzimología , Sulfuros/química , Triptófano/análogos & derivados , Secuencia de Aminoácidos , Aminoácidos/química , Clonación Molecular , Reactivos de Enlaces Cruzados/farmacología , Ácido Glutámico/química , Hemo/química , Espectrometría de Masas , Modelos Químicos , Modelos Genéticos , Datos de Secuencia Molecular , Sistemas de Lectura Abierta , Oxidación-Reducción , Oxidorreductasas actuantes sobre Donantes de Grupo CH-NH/genética , Oxidorreductasas actuantes sobre Donantes de Grupo CH-NH/metabolismo , Péptidos/química , Unión Proteica , Procesamiento Proteico-Postraduccional , Quinonas/química , Análisis de Secuencia de ADN , Homología de Secuencia de Aminoácido , Espectrometría de Masa por Ionización de Electrospray , Triptófano/química , Rayos XRESUMEN
Quinohemoprotein amine dehydrogenase (AMDH) was purified and crystallized from the soluble fraction of Pseudomonas putida IFO 15366 grown on n-butylamine medium. AMDH gave a single component in analytical ultracentrifugation showing an intrinsic sedimentation coefficient of 5.8s. AMDH showed a typical absorption spectrum of cytochrome c showing maxima at 554, 522, 420, and 320 nm in the reduced form and one peak at 410 nm, a shoulder at 350 nm, and a broad hill around 530 nm in the oxidized form. The oxidized enzyme was specifically reduced by the addition of amine substrate. AMDH was composed of three different subunits, 60, 40, and 20 kDa, with the total molecular weight of 120,000. Two moles of heme c were detected per mole of AMDH and the 60-kDa subunit was found to be the heme c-carrying subunit. By redox-cycling quinone staining, a positive reaction band corresponding to the 20-kDa subunit was detected after developed by SDS-PAGE, but the 20 kDa band was scarcely stained by conventional protein staining. Only a silver staining method was possible to detect the subunit after the protein was developed by SDS-PAGE. p-Nitrophenylhydrazine-inhibited AMDH was dissociated into subunits and the 20-kDa subunit showed an absorption maximum at 455 nm, indicating Schiff base formation between the carbonyl cofactor in AMDH and the carbonyl reagent. Thus, AMDH is different from nonheme quinoprotein methylamine dehydrogenase and aromatic amine dehydrogenase in many respects. The presence of an azurin-like blue protein was identified and purified from the same cell-free extract of P. putida as AMDH was purified. The blue protein was reduced specifically during AMDH reaction, suggesting that the blue protein is the direct electron acceptor in amine oxidation. The amine oxidation system was reconstituted successfully only by AMDH, the blue protein, and the cytoplasmic membranes of the organism. The function of the 40-kDa subunit is unknown at the moment. The properties of AMDH were compared with other bacterial amine dehydrogenases so far reported.
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Calcium levels were determined in sera of patients suffering from various lung diseases. Healthy volunteers served as controls. Significant differences were found between the serum calcium levels of patients with active lung tuberculosis and those of controls (P less than 0.01). After treatment, serum calcium levels decrease to normal values in these patients. It was also found that there were significant differences in serum calcium levels of patients with primary lung carcinoma (P less than 0.01) and of patients with metastatic lung carcinoma as compared to controls (P less than 0.01). On the other hand, normal serum calcium levels were found in patients with pulmonary diseases with or without an infection. In conclusion, it seems likely that a combination of mechanisms plays a role in the pathogenesis of hypercalcaemia in pulmonary tuberculosis and primary and metastatic lung carcinoma.
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Calcio/sangre , Enfermedades Pulmonares/sangre , Humanos , Neoplasias Pulmonares/sangre , Metástasis de la Neoplasia , Tuberculosis/sangreRESUMEN
Fifty volunteers among the students of the Faculty of Pharmacy at Ankara and Gazi Universities were taken 2 grams of Vitamin C per day at regular time intervals for two months. Blood and urine samples were collected in the beginning, one month and 2 months after vitamin administration. The whole blood, plasma and leucocyte ascorbic acid levels were increased after one and 2 months treatment. The urine ascorbic acid were also increased significantly. Urine oxalic acid were not elevated after vitamin C intake.