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1.
Eur J Gynaecol Oncol ; 19(1): 93-7, 1998.
Artículo en Inglés | MEDLINE | ID: mdl-9476071

RESUMEN

Concentrations of receptors of insulin-like growth factor-I (IGF-I-R), epithelial growth factor (EGF-R), oestrogen (ER), and progesterone (PR) in the adenomyosis foci, endometrium and myometrium of women during the menstrual cycle were studied. Cell membrane levels of IGF-I-R and EGF-R, cytosol and nuclear oestrogen (ERc and ERn, respectively) and cytosol progesterone (PRc) receptors were assayed in 37 samples of adenomyosis foci, 46 of endometrium and 50 of myometrium using the radioligand method. It was found that concentrations of ER and PR in all studied tissues were significantly higher in the proliferative phase than in the secretory phases. In the endometrium a similar difference concerned only the ERn but not the ERc. Adenomyosis foci as compared to endometrium and myometrium showed the highest ERn and PRc concentrations during the proliferative and secretory phase. Adenomyosis foci and myometrium contained significantly higher concentrations of IGF-I-R in the proliferative phase than in the secretory phase. In the endometrium a menstrual cycle-related difference in concentration of IGF-I-R was not significant. In the endometrium however the concentration of EGF-R was over twice as high in the proliferative phase than in the secretory phase. No significant difference in the concentrations of EGF-R in adenomyosis foci and in myometrium during the menstrual cycle was noted. The findings show that changes in regulation of the concentrations of IGF-I-R, EGF-R, ER and PR in the uterus of women during menstrual cycles are related to the tissular localization of these receptors.


Asunto(s)
Endometriosis/metabolismo , Endometrio/metabolismo , Receptores ErbB/metabolismo , Ciclo Menstrual/metabolismo , Miometrio/metabolismo , Receptor IGF Tipo 1/metabolismo , Receptores de Estrógenos/metabolismo , Receptores de Progesterona/metabolismo , Adulto , Femenino , Humanos , Persona de Mediana Edad
2.
Arch Immunol Ther Exp (Warsz) ; 39(1-2): 41-50, 1991.
Artículo en Inglés | MEDLINE | ID: mdl-1725104

RESUMEN

Serum levels of haptoglobin (HP), sialic acid total (NAN) and lipid-bound (NAL), seromucoid (SER), its content in total protein (%SER), as well as circulating immune complexes (CIC), were measured in sera of women with ovarian carcinoma, prior to their treatment and through the course of chemotherapy, remission and recurrence of malignancy, respectively. Control groups consisted of healthy women and patients with benign tumors (ovarian cysts and uterine myomas). Pretreatment measurements of acute phase reactants discriminated cancers (FIGO stages I+II, III, IV) from healthy group, however differences between benign tumors and stages of ovarian cancer were not so distinct. Changes in the examined parameters (acute phase reactants) indicated satisfactorily a response to the administered chemotherapy and early signs of the progression of the disease. Because of great variations in serum CIC concentrations, they were found to be of no value either in diagnosis or in the surveillance of the disease status.


Asunto(s)
Proteínas de Fase Aguda/metabolismo , Complejo Antígeno-Anticuerpo/sangre , Neoplasias Ováricas/sangre , Adulto , Anciano , Biomarcadores de Tumor/sangre , Femenino , Haptoglobinas/metabolismo , Humanos , Persona de Mediana Edad , Recurrencia Local de Neoplasia/sangre , Recurrencia Local de Neoplasia/diagnóstico , Recurrencia Local de Neoplasia/inmunología , Orosomucoide/metabolismo , Neoplasias Ováricas/diagnóstico , Neoplasias Ováricas/inmunología , Ácidos Siálicos/sangre
3.
Ginekol Pol ; 60(7-9): 415-20, 1989.
Artículo en Polaco | MEDLINE | ID: mdl-2484660

RESUMEN

In the serum of 21 women with malignant ovarian tumours, 13 with uterine myomas and 16 with cysts the concentrations were determined of alpha 1 inhibitor of proteases and alpha 2 macroglobulin by immunodiffusion, and the functional activity of both inhibitors which made possible calculation of the specific activity (units of inhibitory activity per one gram of inhibitor protein). In women with malignant tumours the specific activity of alpha 1 inhibitor was decreased, suggesting that a part of the inhibitor was functionally inactive. This decrease was statistically significant in relation to the control group and the groups of myomas and cysts, but was independent of the degree of disease progression. The specific activity of alpha 2 macroglobulin was significantly decreased only in patients with grade IV degrees of clinical progression (according to FIGO) in relation to the control group and to the group with cysts.


Asunto(s)
Leiomioma/sangre , Neoplasias Ováricas/sangre , Neoplasias Uterinas/sangre , alfa 1-Antitripsina/metabolismo , alfa-Macroglobulinas/metabolismo , Adolescente , Adulto , Anciano , Quistes/sangre , Femenino , Humanos , Persona de Mediana Edad , Enfermedades Uterinas/sangre
5.
Arch Immunol Ther Exp (Warsz) ; 35(5): 623-9, 1987.
Artículo en Inglés | MEDLINE | ID: mdl-3455651

RESUMEN

The synthetic factor based on determinations of 10 parameters in sera of patients with ovarian carcinoma, was constructed. The factor was found to be useful in evaluation of the effectiveness of the cytotoxic treatment and in indication of the recurrence of the malignancy. Reduction of the number of biochemical markers to five (haptoglobin, seromucoid, lactate dehydrogenase, alkaline phosphatase, aspartate aminotransferase), according to significance of particular markers in the laboratory diagnostics of ovarian cancer did not affect the diagnostic sensitivity of the synthetic factor.


Asunto(s)
Biomarcadores de Tumor/análisis , Carcinoma/terapia , Neoplasias Ováricas/terapia , Estadística como Asunto , Fosfatasa Alcalina/análisis , Aspartato Aminotransferasas/análisis , Carcinoma/análisis , Femenino , Haptoglobinas/análisis , Humanos , L-Lactato Deshidrogenasa/análisis , Orosomucoide/análisis , Neoplasias Ováricas/análisis , Pronóstico
7.
Arch Immunol Ther Exp (Warsz) ; 31(4): 565-74, 1983.
Artículo en Inglés | MEDLINE | ID: mdl-6422903

RESUMEN

Cobalt-activated acylase form-2 from human uterine myosarcoma, lung adenocarcinoma and the adjacent tissue was isolated, purified and characterized. It was found, that the enzyme from the malignant neoplasms differed both from the normal tissue and benign tumor acylase-2 in its Km value, temperature optimum and effect of some ions. Some abnormal properties (pH dependence, activation by cobalt and thermostability) were common for benign and malignant tumors. In lung tissue adjacent to adenocarcinoma, some deviations of acylase properties were observed, similar to that found in tumor, indicating that biochemical changes may be present also in tissues unaffected by the neoplastic growth by the histopathological criteria.


Asunto(s)
Adenocarcinoma/enzimología , Amidohidrolasas/metabolismo , Neoplasias Pulmonares/enzimología , Miosarcoma/enzimología , Neoplasias Uterinas/enzimología , Amidohidrolasas/antagonistas & inhibidores , Amidohidrolasas/aislamiento & purificación , Cobalto/farmacología , Estabilidad de Medicamentos , Ácido Edético/farmacología , Activación Enzimática , Femenino , Humanos , Temperatura
9.
Neoplasma ; 26(6): 737-43, 1979.
Artículo en Inglés | MEDLINE | ID: mdl-44348

RESUMEN

The following enzymatic activities were measured in serum of patients with benign and malignant ovarian tumors before treatment: alkaline and acid phosphatases, aspartyl (AspAT) and alanyl (AlAT) aminotransferases, leucyl (LAP) and alanyl (AAP) aminopeptidases, lactate dehydrogenase (LDH), gamma-glutamyl transpeptidase, cathepsin, alkaline ribonuclease (RNase) and beta-glucuronidase. It was shown that at least three determinations (phosphatases and LAP) are practically useless in a discrimination between the examined groups. RNase in combination with AspAT (AlAT) or RNase with AAP and LDH were found to give the best results as marker enzymes.


Asunto(s)
Adenocarcinoma/enzimología , Aminopeptidasas/sangre , L-Lactato Deshidrogenasa/sangre , Mioma/enzimología , Neoplasias Ováricas/enzimología , Transaminasas/sangre , Adolescente , Adulto , Anciano , Catepsinas/sangre , Femenino , Glucuronidasa/sangre , Humanos , Persona de Mediana Edad , Ribonucleasas/sangre , gamma-Glutamiltransferasa/sangre
10.
Neoplasma ; 26(1): 63-72, 1979.
Artículo en Inglés | MEDLINE | ID: mdl-431757

RESUMEN

Cobalt-activated acylase was isolated from human uterine muscle and myoma. The enzyme was purified by ammonium sulphate precipitation, and subsequent chromatography on DEAE-cellulose, Sephadex G-150 and DEAE-Sephadex. The comparison of muscle acylase and acylase obtained from myoma has shown differences in the enzyme stability, the dependence of activity on pH and in the susceptibility to the effect of activators and inhibitors. Only one molecular form of cobalt-activated acylase has been found in both tissues.


Asunto(s)
Aminopeptidasas/metabolismo , Cobalto/farmacología , Leiomioma/enzimología , Neoplasias Uterinas/enzimología , Aciltransferasas/aislamiento & purificación , Aminopeptidasas/antagonistas & inhibidores , Activación Enzimática/efectos de los fármacos , Femenino , Glutamatos , Humanos , Cinética , Músculo Liso/enzimología , Útero/enzimología
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