Wyniki wyszukiwania - Biblioteka Nauki

1

Wlasciwosci transferazy glutationowej z mozgu swini

100%

Sawicki J. , Baranczyk-Kuzma A.

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nr 03

300-302

2

Glutathione conjugation in male reproductive system: studies on glutathione-S-transferase of bull and boar epididymis

100%

Ciszewska-Pilczynska A. , Baranczyk-Kuzma A.

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nr 1

EN

Male reproductive organs are extremely sensitive to the negative influence of toxic environmental factors as well as drugs, and until now not many attempts have been made at studying the detoxication enzymes and the relationship between the activity of those enzymes and spermatozoa fertility. In the present work we studied cytosolic glutathione-S-transferases (GST, EC 2.5.1.18) from different parts (head, corpus and tail) of bull and boar epididymis. We isolated two molecular forms of GST from each part of epididymis, characterized their biochemical properties and examined the mechanism of the catalyzed reaction. On the basis of their substrate specificity and isoelectric point, the isoforms were found to belong to the near neutral GST class mi. All examined GST forms exhibited higher affinity towards GSH than towards 1-chloro-2,4-dinitrobenzene (CDNB) and bull epididymis GST forms showed biphasic Lineweaver-Burk double reciprocal curves in the presence of GSH as a variable substrate. Boar epididymis anionic GST had the -SH groups both in the GSH and the CDNB binding place, whereas the cationic GST form arginine residues in the CDNB binding place. Bull epididymis GST forms contained neither thiol nor arginine residues essential for catalytic activity.

3

Heterogeneity of the bovine brain glutathione-S-transferase

100%

Baranczyk-Kuzma A. , Drobisz D.

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nr 1

4

Glutathione-S-transferase from boar testis: properties of the cytosolic and microsomal forms

100%

Ciszewska-Pilczynska A. , Baranczyk-Kuzma A.

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1992

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tom 39

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nr 1

5

Antioxidant status human brain intoxicated by heroin and psychotropic drugs

80%

Gutowicz M. , Pokorska-Lis M. , Szymczakowski S. , Baranczyk-Kuzma A.

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nr Supplement 1

6

Arginase isoenzymes in human cirrhotic liver

80%

Chrzanowska A. , Gajewska B. , Baranczyk-Kuzma A.

Acta Biochimica Polonica

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2009

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tom 56

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nr 3

465-469

EN

Cirrhosis leads to an inability of the liver to perform its biochemical functions. It can also lead to hepatocellular carcinoma in which, as we showed lately, arginase isoenzyme pattern changes. The present work presents our results on arginase isoenzymes and their possible role in liver cirrhosis. The study was performed on tissues obtained during liver transplantation from 60 patients with liver cirrhosis, and on samples of histologically normal liver (control) from 40 patients with benign or colorectal cancer liver metastases removed during surgery, 6-7 cm from the tumor border. Arginase isoenzymes AI (so-called liver-type arginase) and AII (called extrahepatic arginase) were identified by Western blotting and isolated by ion-exchange chromatography. Their expression on mRNA level was studied by RT-PCR. A significant decrease in arginase activity, dependent of the liver clinical stage, was observed in cirrhotic tissue. Arginase AI activity and its mRNA level were significantly decreased in cirrhotic liver, whereas the activity and expression of arginase AII were concurrently raised, as compared to normal liver. Since arginase AI is a key enzyme of the urea cycle, whereas arginase AII most probably takes part in the biosynthesis of ornithine and polyamines, the defective ammonia inactivation and increased collagen biosynthesis observed in cirrhotic liver may be related to the changes in arginase AI and AII levels, respectively.

7

Wplyw zatrucia heroina na aktywnosc i ekspresje transferazy S-glutationowej w korze mozgowej czlowieka

80%

Gutowicz M. , Kazmierczak B. , Baranczyk-Kuzma A.

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tom 39

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nr 4

377-381

8

Wplyw narkotykow i etanolu na sprzeganie z glutationem w korze mozgowej czlowieka

80%

Gutowicz M. , Siwinska-Ziolkowska A. , Baranczyk-Kuzma A.

Bromatologia i Chemia Toksykologiczna

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2004

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tom 37

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nr 1

59-64

PL

W pracy przedstawiono aktywność transferazy glutationowej i seleno-niezależnej peroksydazy glutationowej oraz poziom zredukowanego glutationu w różnych częściach kory mózgowej człowieka. Badania prowadzono na tkankach otrzymywanych z autopsji osób zmarłych na skutek zatrucia amfetaminą, kokainą i/lub etanolem.

EN

In the present work we examined activity of glutathione-S-transferase, determined with 1-chloro-2,4- dinitrobenzene as an electrophilic substrate (transferase activity, GST) and with cumene peroxide (selene-independent peroxidase activity, GSHPx), as well as the level of reduced glutathione (GSH) in human brain cortex. Studies were conducted on variuos parts of brain cortex obtained by autopsy from cases intoxicated by amphetamine, cocaine and/or ethanol. We observed decreased activity of GST in all studied brains. In brains intoxicated by narcotics and ethanol (at low concentration) GSHPx activity and the level of GSH were higher than in control brains. In brain intoxicated by high, lethal dose of ethanol, the peroxidase activity was unchanged, whereas the level of glutathine was lowered.

9

Changes in kinesin expression in the CNS of mice with dynein heavy chain 1 mutation

80%

Kuzma-Kozakiewicz M. , Kazmierczak B. , Usarek E. , Baranczyk-Kuzma A.

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2013

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tom 60

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nr 1

EN

Dysfunction of fast axonal transport, vital for motor neurons, may lead to neurodegeneration. Anterograde transport is mediated by N-kinesins (KIFs), while retrograde transport by dynein 1 and, to a minor extent, by C-kinesins. In our earlier studies we observed changes in expression of N- and C-kinesins (KIF5A, 5C, C2) in G93ASOD1-linked mouse model of motor neuron degeneration. In the present work we analyze the profile of expression of the same kinesins in mice with a dynein 1 heavy chain mutation (Dync1h1, called Cra1), presenting similar clinical symptoms, and in Cra1/SOD1 mice with milder disease progression than SOD1 transgenics. We found significantly higher levels of mRNA for KIF5A and KIF5C but not the KIFC2 in the frontal cortex of symptomatic Cra1/+ mice (aged 365 days) compared to the wild-type controls. No changes in kinesin expression were found in the spinal cord of any age group and only mild changes in the hippocampus. The expression of kinesins in the cerebellum of the presymptomatic and symptomatic mice (aged 140 and 365 days, respectively) was much lower than in age-matched controls. In Cra1/SOD1 mice the changes in KIFs expression were similar or more severe than in the Cra1/+ groups, and they also appeared in the spinal cord. Thus, in mice with the Dync1h1 mutation, which impairs dynein 1-dependent retrograde transport, expression of kinesin mRNA is affected in various structures of the CNS and the changes are similar or milder than in mice with double Dync1h1/hSOD1G93A mutations.

10

Wplyw zwiazkow fenolowych na transferazy glutationowe z mozgu ssakow

80%

Sawicki J. , Kuzma M. , Baranczyk-Kuzma A.

Bromatologia i Chemia Toksykologiczna

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2001

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tom 34

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nr 2

149-154

PL

W pracy badano wpływ fenolu i jego pochodnych (siarczan fenolu, 1-naftol, siarczan 1-naftolu, p-nitrofenol, siarczan p-nitrofenolu, p-nitroanizol, p-aminofenol, fenacetyna, paracetamol) na aktywność obojętnej izoformy transferazy glutationowej (GST) [EC 2.5.1.18] wyizolowanej z kory mózgu wołu i świni. Stwierdzono, że pochodne fenolu silniej hamują aktywność badanego enzymu niż sam fenol. Wrażliwość GST na działanie tych związków w mniejszym stopniu zależy od mózgowej lokalizacji enzymu niż od ich budowy chemicznej.

EN

Phenol and 1-naphthol do not affect, or slightly decrease, the in vitro activity of the neutral forms of glutathione-5-transferase (GST) isolated from bovine and pig brain cortex. Phenol and naphthol sulfates are much stronger, competitive inhibitors of those enzymes. Among the studied chemicals, p-nitrophenol has the strongest GST-inhibiting effect and, like p-aminophenol, its reduced derivative, inhibits the enzyme non-competitively. Sulfation or methylation of the -OH group decreases the inhibiting effect of p-nitrophenol and changes the site of its binding to the enzyme. Acetylation of the amino group of p-aminophenol lowers the inhibitory effect of this compound; thus the phenacetin and paracetamol analgetics do not at all, or only slightly, inactivate brain glutathione-S-transferases. GST sensitivity to phenols depends on the chemical structure of the latter rather than on enzyme location in the brain.

11

Zmiany statusu antyoksydacyjnego w korze mozgowej czlowieka po zatruciu heroina

61%

Gutowicz M. , Cholojczyk M. , Siwinska-Ziolkowska A. , Pokorska-Lis M. , Szymczakowski S. , Sadurska B. , Baranczyk-Kuzma A.

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nr 3

277-282

PL

W pracy przedstawiono aktywność seleno-niezależnej peroksydazy glutationowej i katalazy, poziom zredukowanego glutationu, dialdehydu malonowego i grup karbonylowych W rożnych częściach kory mózgowej człowieka. Badania prowadzono na tkankach otrzymywanych z autopsji osób zmarłych na skutek zatrucia heroiną

EN

In the present work we examined selenium-independent glutathione peroxidase (GSHPx) and catalase (CAT) activities, as well as levels of reduced glutathione (GSH), malondialdehyde (MDA), and the amount of carbonyl groups (CO) in human brain cortex. Various parts of brain cortex (frontal, parietal, temporal, occipital ) obtained by autopsy from 9 cases intoxicated by heroin and from 7 control brains were examined. We found a significant increase in GSHPx activity in the heroin-intoxicated brains, accompanied by decreased level of GSH. No changes in CAT activity or in the amount of carbonyl groups were observed, whereas the level of MDA was almost 2 times higher in heroin-intoxicated brains vs. controls. Thus, the results indicate that heroin intoxication changes the antioxidant status in human brain cortex. The changes comprise increased lipid peroxidation and disturbed organic peroxide inactivation.

12

Zmiany w ekspresji izoform bialka tau w mozgu myszy w zaleznosci od wieku

61%

Usarek E. , Kuzma M. , Kazmierczak B. , Muench C. , Ludolph A. C. , Baranczyk-Kuzma A.

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tom 62

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nr 02

231-233

EN

au is a microtubule-associated protein important for the assembly and stabilization of microtubules. Six tau isoforms are produced in the central nervous system from one single gene as a result of the alternative splicing of exons 2, 3 (N-terminal part) and exon 10 (C-terminal part). The shortest isoform (2-3-10-, 0N 3R) is characteristic for fetal brains, whereas the remaining (2+3-10-, 1N 3R; 2+3+10-, 2N 3R; 2-3-10+, 0N 4R; 2+3-10+, 1N 4R; 2+3+10+, 2N 4R) for adult brains. The aim of the study was to establish a profile of tau protein variants in the C57BL/6J mouse frontal cortex during the aging process. The total RNA was isolated from tissues, followed by reverse transcription and PCR reaction. It was found that the sequence encoded by exon 10 was absent in the youngest 5-day old newborns (isoform 3R), while it was present in 21, 70 and 140-day old animals (isoform 4R). The most abundant isoform in 5-day old mice was 1N and accounted for 66% of the total tau protein. The percentage of 1N isoforms lowered with age and was 31% in 140-day old animals. The total percentage of 0N isoforms was 11% in 5-day old mice and was approximately threefold lower than in each of the older groups. It may be concluded that alternative splicing of the tau protein undergoes age-dependent regulation in the mouse brain cortex.