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Bioavailability of mesalazine from two coated formulation tablets

100%
Hermann T. W., Główka F. K., Hermann J., Zabel M.
Acta Poloniae Pharmaceutica - Drug Research
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2019
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vol. 76
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issue 1
67-73
EN
HPLC methodology with a fluorescent detector is suitable for bioavailability studies of investigated generic tablets Mesalazine 250 mg (Jelfa, Poland) versus standard Salofalk tablets (Dr. Falk, Germany). The investigations were completed in ten healthy subjects in a double way crossover design. Only one bioavailability parameter – time for maximum mesalazine plasma concentration (tmax ) and overall elimination rate constants are significantly greater for the above standard tablets. The parameters like maximum plasma drug concentration (Cmax), lag time for absorption (Tlag), biological half-life time (t1/2 ) are also more favorable for the standard, but these values are not significantly different.
2
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Molecular basis of mechanisms of steroid resistance in children with nephrotic syndrome

88%
Świerczewska M., Ostalska-Nowicka D., Kempisty B., Nowicki M., Zabel M.
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2013
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vol. 60
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issue 3
339-344
EN
Steroid therapy, due to a wide range of anti-inflammatory properties of steroids, is a basic field of treatment in many human diseases including the nephrotic syndrome in children. However, not all patients respond positively to therapy which divides them into steroid sensitive (SS) and steroid resistance (SR) individuals. Many potential factors associated with steroid resistance have been identified so far. It seems that genetic factors associated with glucocorticoid receptor α (GRα), the structure of heterocomplex of GR as well as glycoprotein P or cytochrome P450 may play a role in the induction of glucocorticoid resistance. Here we described several of the molecular mechanisms, which can regulate glucocorticoid sensitivity and resistance. Moreover, we presented genetic defects, which can lead to various effects of treatment and, in a longer perspective, enable clinicians to individualize therapies.
3
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Inhibitors of N-glycosylation as a potential tool for analysis of the mechanism of action and cellular localisation of glycoprotein P

76%
Wojtowicz K., Szaflarski W., Januchowski R., Zawierucha P., Nowicki M., Zabel M.
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EN
Multidrug resistance has for many years attracted attention of numerous investigators. Attempts have also been made to increase efficiency of anti-neoplastic therapy. For this reason, most of efforts have been devoted to analysing proteins engaged in the mechanism of multidrug resistance such as the N-glycosylated membrane protein glycoprotein P. Interestingly, glycosylation probably plays a significant role in the intracellular location and activity of modified proteins. Inhibitors of glycosylation have been demonstrated to alter the activity of glycoprotein P in various ways, depending on the cell line examined. These inhibitors markedly reduce multidrug resistance of cancer cells, thus promoting success of anti-neoplastic therapy. Here, we review the basic knowledge on N-glycosylation inhibitors, their effect on glycoprotein P and their therapeutic potential.
4
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Alternative 3' acceptor site in the exon 2 of human PAX8 gene resulting in the expression of unknown mRNA variant found in thyroid hemiagenesis and some types of cancers

64%
Szczepanek-Parulska E., Szaflarski W., Piątek K., Budny B., Jaszczyńska-Nowinka K., Biczysko M., Wierzbicki T., Skrobisz J., Zabel M., Ruchała M.
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2013
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vol. 60
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issue 4
573-578
EN
PAX8 gene encodes one of the transcription factors engaged in the regulation of proper development of thyroid gland as well as Müllerian and renal/upper urinary tracts. So far, six alternatively spliced transcripts were reported, however, sequences of only four were deposited in the NCBI database. Here, we evaluate a fragment of a novel variant of PAX8 mRNA formed by an alternative 3' acceptor site located in the second exon. The molecular outcome encompasses extension of the 5' untranslated region of exon two by 97 nucleotides as is evident from mRNA. This new insert may impair binding of mRNA to the ribosome and in consequence significantly decrease expression of the PAX8 protein. Here, we show for the first time that the novel insert in exon two might be associated with congenital thyroid hemiagenesis and influence development of different types of cancer.
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