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1

The role of - SH groups in the resistance of E.coli cells to cis-diamminedichloroplatinum [II] [cis-DDP]

100%
Zastawny T. H., Olinski R.
Acta Biochimica Polonica
|
1993
|
tom 40
|
nr 1
2

Platinum accumulation and DNA-protein cross-linking in the bacterial cells sensitive and resistant to cis-diamminedichloroplatinum (II)

86%
Zastawny T. H., Olinski R.
Applied Biology Communications. Lublin Scientific Center
|
1991
|
tom 01
|
nr 3
3

Lipid organization in cisplatin nanocapsules: lipid-coated aggregates of cisplatin with high cytotoxicity

86%
Chupin V., De Kroon A. I. P. M., De Kruijff B.
Cellular and Molecular Biology Letters
|
2005
|
tom 10
|
nr Suppl.
4

Cross-linking of nuclear proteins to DNA by platinum compounds

86%
Walter Z., Wozniak K., Kowalik J.
Cellular and Molecular Biology Letters
|
1997
|
tom 02
|
nr 4
In this work we investigated the lymphocyte nuclear proteins which participated in DNA-protein cross-links induced by three platinum compounds: cis-DDP, trans-DDP and carboplatin. Our studies indicated that many proteins were cross- linked to DNA in the intact cell. Trans-DDP was the most effective cross-linker. The cross-linking process depended on time of the cells incubation with aforementioned compounds. Carboplatin produced the DNA-protein cross-links more slowly and less effectively than cis-DDP. After incubation of the cells with cis-DDP, trans- DDP and carboplatin a similar protein pattern was obtained. In case of all compounds studied 34.5 kDa protein was abundantly represented.
5

Fractionation of DNA isolated from lymphocytes of patients under therapy with the antiblastic drug cis-diamminedichloroplatinum [II] using pulsed field gel electrophoresis

86%
Jaruga P., Zastawny T. H., Tujakowski J., Olinski R.
Acta Biochimica Polonica
|
1993
|
tom 40
|
nr 1
6

DNA damage and apoptosis induction in L1210 cells by cis-diamminedichloroplatinum [II] and its new aminoflavone analogue

72%
Ciesielska E., Studzian K., Zyner E., Ochocki J., Szmigiero L.
Cellular and Molecular Biology Letters
|
2000
|
tom 05
|
nr 4
441-450
This work compares the biological properties of cis-diammine- dichloroplatinum (cisplatin) and its new analogue cis-[Pt(AF)2Cl2] (AF stands for 3-aminoflavone), which contains two aminoflavone substituents as non-leaving ligands. Both compounds were tested for their antiproliferative activity against cultured L1210 cells, and their DNA interstrand crosslinking activity in cells and in a cell-free system. Cisplatin was found to be an approximately 6 times more cytotoxic drug than its new analogue. Platinum complexes reacted with purified calf thymus DNA in a cell-free system producing DNA interstrand crosslinks. The kinetics of crosslink formation was very similar for both compounds but the maximal level of crosslinks was 20% higher for cisplatin. In cells, however, crosslinks were produced by cisplatin, whereas this type of DNA lesion was almost undetected in cells treated with the aminoflavone analogue as assayed by DNA alkaline elution. At higher drug concentrations, strong degradation of DNA was observed in L1210 cells treated with cis- [Pt(AF)2Cl2] but not in the cells incubated with cisplatin. This DNA degradation seems to reflect very efficient apoptosis induction by cis-[Pt(AF)2Cl2] as the electrophoretic patterns of DNA from cells incubated with this drug showed a ladder typical for apoptotic cells.
7

DNA-nuclear matrix interactions analyzed by cross-linking reactions in intact nuclei from avian liver

72%
Ferraro A., Eufemi M., Cervoni L., Altieri F., Turano C.
Acta Biochimica Polonica
|
1995
|
tom 42
|
nr 2
To detect the interactions of DNA with the nuclear matrix proteins, DNA-protein cross-linkages were induced in intact nuclei from chicken liver by the use of ds-diammine dichloroplatinum. Methods have been devised for fast purification both of the proteins and of the DNA fragments involved in the cross-linked complexes. By Southern-Western blotting a number of matrix proteins isolated from the complexes have been shown to recognize specifically DNA sequences present in the cross-linked DNA fragments. This experimental approach not only allows to identify the nuclear matrix-DNA interactions existing in the nucleus before its disruption, but also provides a preparation of matrix proteins enriched in those species which are involved in such interactions and which can therefore be detected with high sensitivity.
8

Binding of the anticancer drug cis-diamminedichloroplatinum [II] to mammalian mitochondrial DNA

72%
Walter Z., Grabowska M., Majsterek I.
Acta Biologica Cracoviensia. Series Zoologia
|
1998
|
tom 40
9

Changes in the enzymatic activity of glutathione S-transferases from human peripheral blood lymphocytes after the action of cis-and trans-diamminedichloroplatinum [II]

72%
Walter Z., Kargas C.
Acta Biologica Cracoviensia. Series Zoologia
|
2001
|
tom 43
10

Platinum-induced changes in F0F1 ATPase activity in mitochondria

72%
Walter Z., Grabowska M., Majsterek I.
Acta Biologica Cracoviensia. Series Zoologia
|
2002
|
tom 44
11

Characterization of a novel protein that specifically binds to DNA modified by N-acetoxy-acetylaminofluorene and cis-diamminedichloroplatinum

72%
Pietrowska M., Widlak P.
Acta Biochimica Polonica
|
2005
|
tom 52
|
nr 4
Proteins recognizing DNA damaged by the chemical carcinogen N-acetoxy-acetylaminofluorene (AAAF) were analyzed in nuclear extracts from rat tissues, using a 36 bp oligonucleotide as a substrate and electrophoretic mobility shift and Southwestern blot assays. One major damage-recognizing protein was detected, whose amount was estimated as at least 105 copies per cell. Levels of this protein were similar in extracts from brain, kidney and liver, but much lower in extracts from testis. The affinity of the detected protein for DNA damaged by AAAF was about 70-fold higher than for undamaged DNA. DNA damaged by cis-diamminedichloroplatinum (cis-DDP), benzo(a)pyrene diolepoxide (BPDE) or UV-radiation also bound this protein with an increased affinity, the former more strongly and the latter two more weakly as compared to AAAF-damaged DNA. The detected AAAF/DDP-damaged-DNA-binding (AAAF/DDP-DDB) protein had a molecular mass of about 25 kDa and was distinct from histone H1 or HMGB proteins, which are known to have a high affinity for cis-DDP-damaged DNA. The level of this damage-recognizing protein was not affected in rats treated with the carcinogen 2-acetylaminofluorene. The activity of an AAAF/DDP-DDB protein could also be detected in extracts from mouse liver cells but not from the Hep2G human hepatocellular carcinoma.
12

DNA adduct repair in mammalian mitochondria after cis- and trans-diamminechloroplatinum [II] treatment

72%
Majsterek I., Walter Z.
Acta Biologica Cracoviensia. Series Zoologia
|
2001
|
tom 43
13

Cis-DDP induced alteration of DNA structure studied by scanning tunneling microscopy

72%
Zastawny T. H., Olejniczak W., Olinski R.
Acta Biochimica Polonica
|
1993
|
tom 40
|
nr 4
Scanning tunneling microscopy (STM) was used to study the structural changes of DNA induced by the antitumor drug cts-diamminedichloroplatinum. The STM image showed a dramatic structural perturbation of the DNA by complexed Pt with the characteristic bend of the double helix.
14

Differences in the inhibition of neuritic outgrowth in organotypic cultures of rat foetal dorsal root ganglia treated with cisplatin and carboplatin: a comparative study

72%
Jirsova K., Mandys V.
Folia Histochemica et Cytobiologica
|
1997
|
tom 35
|
nr 4
15

DNA-platinum-DNA cross-links formation induced by cis and trans-diamminedichloroplatinum in isolated leukocyte nuclei

72%
Walter Z., Spychala M.
Acta Biochimica Polonica
|
1992
|
tom 39
|
nr 1
16

DNA damage and apoptosis induction in L1210 cells by cis-diamminedichloroplatinum[II] and its new aminoflavone analogue

72%
Ciesielska E., Studzian K., Zyner E., Ochocki J., Szmigiero L.
Cellular and Molecular Biology Letters
|
2000
|
tom 05
|
nr 2
17
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The effect of cis-diamminedichloroplatinum, selenite and a conjugate of cisplatin with selenite [[NH3]2Pt[SeO3]] on oxidative stress in blood platelets measured by chemiluminescence method

58%
Olas B., Zbikowska H. M., Wachowicz B., Buczynski A., Krajewski T.
Journal of Physiology and Pharmacology
|
1999
|
tom 50
|
nr 2
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