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1

Endocrine disruptor contaminants in water and their adverse effects in humans

100%
Wesierska-Gadek J.
International Journal of Ecohydrology and Hydrobiology
|
2006
|
tom 06
|
nr 1-4
233-242
2

Role of poly[ADP-ribose] polymerase in the regulation of the stability of wild-type p53 protein and p53-mediated apoptosis

100%
Wesierska-Gadek J.
Cellular and Molecular Biology Letters
|
2000
|
tom 05
|
nr 2
3

The subcellular distribution of the p53 tumour suppressor, and organismal ageing

63%
Wesierska-Gadek J., Schmid G.
Cellular and Molecular Biology Letters
|
2005
|
tom 10
|
nr 3
4

Poly[ADP-ribose] polymerase-1 regulates the stability of the wild-type p53 protein

63%
Wesierska-Gadek J., Schmid G.
Cellular and Molecular Biology Letters
|
2001
|
tom 06
|
nr 2
5

Nowe oblicze bialek antyapoptotycznych. I. Bialko Mcl-1

51%
Bednarek J., Wesierska-Gadek J., Kilianska Z. M.
Postępy Biochemii
|
2007
|
tom 53
|
nr 3
228-238
6

Nowe oblicze bialek antyapoptotycznych. II. Surwiwina

51%
Wesierska-Gadek J., Bednarek J., Kilianska Z. M.
Postępy Biochemii
|
2007
|
tom 53
|
nr 3
239-253
7

Impact of roscovitine, a selective CDK inhibitor, on cancer cells: bi-functionality increases its therapeutic potential

51%
Wesierska-Gadek J., Brzoza A., Komina O., Maurer M.
Acta Biochimica Polonica
|
2009
|
tom 56
|
nr 3
495-501
 Increased expression and activity of proteins driving cell cycle progression as well as inactivation of endogenous inhibitors of cyclin-dependent kinases (CDKs) enhance the proliferative potential of cells. Escape of cells during malignant transformation from the proper cell cycle control rendering them independent from growth factors provides rationale for therapeutic targeting of CDKs. Exposure of rapidly growing human MCF-7 breast cancer and HeLa cervix cancer cells to roscovitine (ROSC), a selective inhibitor of CDKs, inhibits their proliferation by induction of cell cycle arrest and/or apoptosis. The outcome strongly depends on the intrinsic traits of the tumor cells, on their cell cycle status prior to the onset of treatment and also on ROSC concentration. At lower dose ROSC primarily inhibits the cell cycle-related CDKs resulting in a strong cell cycle arrest. Interestingly, ROSC arrests asynchronously growing cells at the G2/M transition irrespective of the status of their restriction checkpoint. However, the exposure of cancer cells synchronized after serum starvation in the late G1 phase results in a transient G1 arrest only in cells displaying the intact G1/S checkpoint. At higher dosage ROSC triggers apoptosis. In HeLa cells inhibition of the activity of CDK7 and, in consequence, that of RNA polymerase II is a major event that facilitates the initiation of caspase-dependent apoptosis. In contrast, in the caspase-3-deficient MCF-7 breast cancer cells ROSC induces apoptosis by a p53-dependent pathway. HIPK2-mediated activation of the p53 transcription factor by phosphorylation at Ser46 results in upregulation of p53AIP1 protein. This protein after de novo synthesis and translocation into the mitochondria promotes depolarization of the mitochondrial membrane.
8

Genetic inactivation and chemical inhibition of PARP-1 leads to increased cytotoxicity to antitumor triazoloacridone C-1305

51%
Sabisz M., Wesierska-Gadek J., Skladanowski A. M.
Acta Biochimica Polonica
|
2007
|
tom 54
|
nr Supplement 4
9
Content available remote

Physiological ageing: role of p53 and PARP-1 tumor suppressors in the regulation of terminal senescence

51%
Wesierska-Gadek J., Ranftler C., Schmid G.
Journal of Physiology and Pharmacology. Supplement
|
2005
|
tom 56
|
nr 2
77-88
Ageing of organisms is among the most complex processes currently known. Understanding the molecular mechanism of physiological ageing is one of the most essential issues in biology and medicine because it is not possible to predict when and how a certain individual will start ageing. In the past centuries human life expectancies increased. Extension of life span is associated with increased susceptibility to a number of chronic diseases. Insight into the cellular and molecular targets of the ageing process would offer the opportunity to prevent at least some of the destructive processes. In the present paper the involvement of two tumor suppressor proteins: wild-type p53 and poly(ADP-ribose)polymerase-1 (PARP-1) in the regulation of cellular senescence and physiological ageing was reviewed. Moreover, the interaction and cross-talk between p53 and PARP1-1 was discussed.
10

Advantage of a baculovirus expression system for protein-protein interaction studies. Involvement of posttranslational phosphorylation in the interaction between wt p53 protein and poly[ADP-ribose] polymerase-1

51%
Schmid G., Wojciechowski J., Wesierska-Gadek J.
Acta Biochimica Polonica
|
2005
|
tom 52
|
nr 3
We recently observed an interaction between poly(ADP-ribose) polymerase-1 (PARP-1) and the tumor suppressor p53 protein. However, more extensive studies on both proteins, especially those on characterization of their domains involved in the interaction were difficult due to very low expression levels of p53 in mammalian cells. Therefore, we generated recombinant proteins for such studies. To clarify which domains of human PARP-1 and of human wild-type (wt) p53 were involved in this protein-protein interaction, we generated baculoviral constructs encoding full length or distinct functional domains of both proteins. Full length PARP-1 was simultaneously coexpressed in insect cells with full length wt p53 protein or its distinct truncated fragments and vice versa. Reciprocal immunoprecipitation of Sf9 cell lysates revealed that the central and carboxy-terminal fragments of p53 each were sufficient to confer binding to PARP-1, whereas the amino-terminal part harbouring the transactivation functional domain was dispensable. On the other hand, the amino-terminal and central fragments of PARP-1 were both necessary for complex formation with p53 protein. Since the most important features of p53 protein are regulated by phosphorylation, we addressed the question whether its phosphorylation is essential for the binding between the two proteins. Baculovirally expressed wt p53 was post-translationally modified. At least six distinct p53 isomers were resolved by immunoblotting following two-dimensional separation of baculovirally expressed wt p53 protein. Using specific phospho-serine antibodies, we identified phosphorylation of baculovirally expressed p53 protein at five distinct sites. To define the role of p53 phosphorylation, pull-down assays using untreated and dephosphorylated p53 protein were performed. Dephosphorylated p53 failed to bind PARP-1, indicating that complex formation between the two proteins was regulated by phosphorylation of p53. The marked phosphorylation of p53 at Ser392 observed in unstressed cells suggests that the phosphorylated carboxy-terminal part of p53 undergoes complex formation with PARP-1 resulting in masking of the NES and thereby preventing its export.
11

Autoantibodies against constituents of nuclear pore complexes in patients with primary biliary cirrhosis and autoimmune hepatitis

51%
Wesierska-Gadek J., Hohenauer H., Hitchman E., Penner E.
Acta Biochimica Polonica
|
1995
|
tom 42
|
nr 2
Sera obtained from patients with autoimmune liver disease were screened in indirect immunofluorescence microscopy for the presence of autoantibodies. Patients' sera, which strongly stained nuclei (ANA) with peripheral accentuation, were used for further experiments to define the corresponding antigen(s). Nuclei and nuclear subfractions were isolated from HeLaS3 cells and used as antigen source. Immunoblotting experiments were performed after separation of nuclear proteins by one- and two-dimensional polyacrylamide gel electrophoresis. Some ANA positive sera recognized the nuclear protein with molecular mass of approximately 200 kDa. Further analysis revealed that the patients' sera reacted with gp210, an integral protein of the nuclear pores. The incidence and clinical significance of these antibodies is discussed.
12

Phenol red in the culture medium strongly affects the susceptibility of human MCF-7 cells to roscovitine

45%
Wesierska-Gadek J., Schreiner T., Maurer M., Waringer A., Ranftler C.
Cellular and Molecular Biology Letters
|
2007
|
tom 12
|
nr 2
Estrogens play an important role in the growth and terminal differentiation of the mammary gland. Prolonged exposure to estrogens seems to predispose women to breast cancer. It recently became evident that not only the intrinsic hormonal status but also external factors such as the occurrence of pharmaceuticals and chemicals with hormone activity in the environment may put women at greater risk of developing breast cancer. We focused on the interference of endocrine disruptors in breast cancer therapy. We observed that phenol red added to the culture medium strongly promoted the cell proliferation and cell cycle progression of human cells expressing the estrogen receptor, and affected their susceptibility to chemotherapy.
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