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Wyszukujesz frazę "liver" wg kryterium: Temat


Tytuł:
Influence of oleic acid in different solvent media on BRL 3A cell growth and viability
Autorzy:
Liu, Runqi
Yang, Wei
Xia, Cheng
Chen, Yuanyuan
Gao, Sansi
Dong, Zhihao
Huang, Baoyin
Li, Ruirui
He, Ping
Xu, Chuang
Powiązania:
https://bibliotekanauki.pl/articles/1038377.pdf
Data publikacji:
2018
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
oleic acid
non-alcoholic fatty liver disease
liver lipid deposition
Opis:
Oleic acid (OA) is widely used in pathology studies of hepatocellular lipid deposition. Identifying the effects of different solvents on OA-induced liver lipid deposition would be beneficial for studies on hepatocytes. We treated BRL 3A cells with OA dissolved in different solvents. After 12 h incubation, cell viability was assessed using MTT assays. Reactive oxygen species (ROS), triglyceride (TG) and total cholesterol (TC) counts, and the expression level of glucose regulated protein (GRP78), sterol regulatory element binding protein (SREBP-1C) and fatty acid synthase (FAS) were analyzed. Water, PBS and DMSO were disadvantageous to the dissolution of OA and did not cause an OA-induced response in hepatocytes. In the alcohol+OA-treated cells, the severe ER stress, oxidative stress and cellular fat deposition were significantly increased. BSA promoted cell growth and the cells treated with 1.2% BSA+OA showed a lower grade TG and endoplasmic reticulum stress compared with KOH+OA and alcohol+OA treatments. KOH had no significant influence on BRL 3A cells viability. When treated with OA dissolved in KOH, BRL 3A cells showed a typical hepatocyte damage. KOH was considered the suitable choice for an OA solvent for BRL 3A cells in hepatic lipidosis research.
Źródło:
Acta Biochimica Polonica; 2018, 65, 3; 443-447
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Arginase isoenzymes in human cirrhotic liver
Autorzy:
Chrzanowska, Alicja
Gajewska, Beata
Barańczyk-Kuźma, Anna
Powiązania:
https://bibliotekanauki.pl/articles/1040542.pdf
Data publikacji:
2009
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
arginase activity
liver cirrhosis
isoenzyme expression
Opis:
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.
Źródło:
Acta Biochimica Polonica; 2009, 56, 3; 465-469
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
The effects of galactosamine on UTP levels in the livers of young, adult and old rats.
Autorzy:
Kmieć, Zbigniew
Smoleński, Ryszard
Zych, Marek
Myśliwski, Andrzej
Powiązania:
https://bibliotekanauki.pl/articles/1044358.pdf
Data publikacji:
2000
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
liver
UTP
rat aging
galactosamine
nucleotides
Opis:
Galactosamine (GalN), a well-known hepatotoxin that depletes the cellular pool of uracil nucleotides, was previously shown to have greater impact on the inhibition of protein synthesis in hepatocytes of old rats as compared with young animals (Kmieć 1994, Ann. N.Y. Ac. Sci. 717, 216-225). In the present study we compared the effects of GalN on the nucleotide content (measured by ion-exchange HPLC) in the livers of young (4 months), adult (12 months), and old (24-26 months old) rats two hours after its intraperitoneal administration. UTP content of the livers of old control rats was significantly lower (by 28%) than that of young animals. GalN administration decreased the UTP content in the livers of young, adult and old rats by, respectively, 55%, 65% and 89%, and increased the content of UDP-sugars by 189%, 175% and 305%. The hepatic content of ATP, ADP, AMP, NAD, GTP except CTP did not differ significantly among the age groups of rats studied, and was not changed by GalN treatment. The content of CTP was significantly higher in old rats (P < 0.03) upon GalN treatment. The lower hepatic content of UTP may partially explain the increased sensitivity of hepatocytes and livers of old rats to the action of galactosamine, and possibly to other hepatotoxic compounds that decrease transcription in the liver.
Źródło:
Acta Biochimica Polonica; 2000, 47, 2; 349-353
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Molecular cloning and expression analysis of a new gene for short-chain dehydrogenase/reductase 9
Autorzy:
Liu, Shen
Huang, Chaoqun
Li, Dawei
Ren, Weihua
Zhang, Haoxing
Qi, Meiyan
Li, Xin
Yu, Long
Powiązania:
https://bibliotekanauki.pl/articles/1041143.pdf
Data publikacji:
2007
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
liver
clone
short-chain dehydrogenase/reductase
Opis:
We report here the cloning and characterization of a novel human short-chain dehydrogenases/reductase gene SCDR9, isolated from a human liver cDNA library, and mapped to 4q22.1 by browsing the UCSC genomic database. SCDR9 containing an ORF with a length of 900 bp, encoding a protein with a signal peptide sequence and an adh_short domain. GFP localization shows SCDR9 protein concentrated in some site of the cytoplasm, but not in the ER. Expression pattern in eighteen tissues revealed that SCDR9 is expressed highly in liver. Soluble recombinant protein was successfully purified from Escherichia coli using pET28A(+) expression vector. Our data provides important information for further study of the function of the SCDR9 gene and its products.
Źródło:
Acta Biochimica Polonica; 2007, 54, 1; 213-218
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Prognostic value of perioperative assessment of plasma cardiac troponin I in patients undergoing liver transplantation
Autorzy:
Jankowski, Krzysztof
Trzebicki, Janusz
Bielecki, Maksymilian
Łągiewska, Beata
Kurnicka, Katarzyna
Koczaj-Bremer, Magdalena
Pacholczyk, Marek
Pruszczyk, Piotr
Powiązania:
https://bibliotekanauki.pl/articles/1038657.pdf
Data publikacji:
2017
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
cardiac troponin I
liver transplantation
surgery time
Opis:
Abstract. An elevation in plasma cardiac troponins is an indicator of increased perioperative risk in orthopaedic and vascular surgery, however, data on liver transplantation (LTx) are scarce. The aim of the study was to evaluate the prevalence of cardiac troponin I (cTnI) elevation in the perioperative period of LTx, and its potential relationship with 1-year mortality. Material and methods. Analysis included 79 patients with liver cirrhosis. During LTx all patients underwent hemodynamic measurements. cTnI level was determined before the operation, 24, 48 and 72 hours afterwards. One-year mortality was assessed. Results. 12.7% patients died, all during in-hospital period. cTnI level on day 1. was identified as the most promising marker of increased death risk with optimal cut-off value of 0.215 ng/mL (the sensitivity of 60.0%, specificity of 87.0%, positive predictive value of 40.0%, negative predictive value of 93.8%). The most important predictor of cTnI increase was the duration of the LTx procedure followed by amount of packed red blood cells transfused, basic stroke volume index, and cardiac output index. In conclusion: value of cTnI level assessed 24 hours post-surgery was a reliable predictor of death following LTx with optimal cut-off value of 0.215 ng/mL. The surgery time was the most important predictor of cTnI elevation.
Źródło:
Acta Biochimica Polonica; 2017, 64, 2; 331-337
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Influence of acetaminophen and trichloroethylene on liver cytochrome P450-dependent monooxygenase system.
Autorzy:
Plewka, Andrzej
Zielińska-Psuja, Barbara
Kowalówka-Zawieja, Joanna
Nowaczyk-Dura, Grażyna
Plewka, Danuta
Wiaderkiewicz, Anna
Kamiński, Marcin
Orłowski, Jerzy
Powiązania:
https://bibliotekanauki.pl/articles/1044264.pdf
Data publikacji:
2000
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
trichloroethylene
liver
rat
acetaminophen
cytochrome P450,glutathione
Opis:
The aim of the study was to evaluate the effect of acetaminophen (APAP) and/or trichloroethylene (TRI) on the liver cytochrome P450-dependent monooxygenase system, CYP2E1 and CYP1A2 (two important P450 isoforms), and liver glutathione (GSH) content in rats. Rats were given three different doses of APAP (250, 500 and 1000 mg/kg b...) and then the above-mentioned parameters were measured for 48 h. The lowest APAP dose produced small changes in the cytochrome P450 content of liver. At 500 mg/kg APAP increased the cytochrome P450 content to 230% of the control. The inductive effect was seen at 1000 mg/kg dose but at 24 h and later. NADPH-cytochrome P450 reductase activity was the highest after the lowest dose of APAP, while after the highest dose it was equal to the control value. TRI increased both the cytochrome P450 content and the NADPH-cytochrome P450 reductase activity. When TRI was combined with APAP, both these parameters increased in the first hours of observation, but they returned to the control values at 24 h. When APAP was given at 250 mg/kg, GSH levels decreased to 55% of the control at 8 h and returned to the control values at 24 h. The higher doses of APAP decreased GSH levels more than the lowest dose, but after 24 h GSH levels did not differ from those of the control. When TRI was given at 250 mg/kg, the GSH levels decreased to 68% of the control at 2 h and then they increased gradually and tended to exceed the control values at 48 h. The effect of TRI combined with APAP on the level of GSH was virtually the same as that of APAP alone given at 500 mg/kg.
Źródło:
Acta Biochimica Polonica; 2000, 47, 4; 1129-1136
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Tissue variation of mitochondrial oxidative phosphorylation efficiency in cold-acclimated ducklings
Autorzy:
Salin, Karine
Teulier, Loïc
Rey, Benjamin
Rouanet, Jean-Louis
Voituron, Yann
Duchamp, Claude
Roussel, Damien
Powiązania:
https://bibliotekanauki.pl/articles/1040299.pdf
Data publikacji:
2010
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
liver
skeletal muscle
thermogenesis
mitochondrial oxidative phosphorylation
proton conductance
Opis:
We investigated the oxidative phosphorylation efficiency of liver and gastrocnemius muscle mitochondria in thermoneutral and cold-acclimated ducklings. The yield of oxidative phosphorylation was lower in muscle than in liver mitochondria, a difference that was associated with a higher proton conductance in muscle mitochondria. Cold exposure did not affect oxidative phosphorylation efficiency or basal proton leak in mitochondria. We conclude that the basal proton conductance of mitochondria may regulate mitochondrial oxidative phosphorylation efficiency, but is not an important contributor to thermogenic processes in cold-acclimated ducklings.
Źródło:
Acta Biochimica Polonica; 2010, 57, 4; 409-412
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Paraoxonase 1 and dietary hyperhomocysteinemia modulate the expression of mouse proteins involved in liver homeostasis
Autorzy:
Suszyńska-Zajczyk, Joanna
Jakubowski, Hieronim
Powiązania:
https://bibliotekanauki.pl/articles/1039222.pdf
Data publikacji:
2014
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
Pon1
high-methionine diet
hyperhomocysteinemia
mouse liver proteome
Opis:
Homocysteine (Hcy), a product of methionine metabolism, is elevated by the consumption of a high-methionine diet that can cause fatty liver disease. Paraoxonase 1 (Pon1), a hydrolase expressed mainly in the liver and carried in the circulation on high-density lipoprotein, participates in Hcy metabolism. Low Pon1 activity is linked to fatty liver disease. We hypothesize that hyperhomocysteinemia and low Pon1 induce changes in gene expression that could impair liver homeostasis. To test this hypothesis, we analyzed the liver proteome of Pon1-/- and Pon1+/+ mice fed a high methionine diet (1% methionine in the drinking water) for 8 weeks using 2D IEF/SDS-PAGE gel electrophoresis and MALDI-TOF mass spectrometry. We identified seven liver proteins whose expression was significantly altered in Pon1-/- mice. In animals fed with a control diet, the expression of three liver proteins involved in lipoprotein metabolism (ApoE), iron metabolism (Ftl), and regulation of nitric oxide generation (Ddah1) was up-regulated by the Pon1-/- genotype. In mice fed with a high-methionine diet, expression of four liver proteins was up-regulated and of three proteins was down-regulated by the Pon1-/- genotype. The up-regulated proteins are involved in lipoprotein metabolism (ApoE), energy metabolism (Atp5h), oxidative stress response (Prdx2), and nitric oxide regulation (Ddah1). The down-regulated proteins are involved in energy metabolism (Gamt), iron metabolism (Ftl), and catechol metabolism (Comt). Expression of one protein (Ftl) was up-regulated both by the Pon1-/- genotype and a high-methionine diet. Our findings suggest that Pon1 interacts with diverse cellular processes - from lipoprotein metabolism, nitric oxide regulation, and energy metabolism to iron transport and antioxidant defenses - that are essential for normal liver homeostasis and modulation of these interactions by a high-methionine diet may contribute to fatty liver disease.
Źródło:
Acta Biochimica Polonica; 2014, 61, 4; 815-823
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Graves disease, celiac disease and liver function abnormalities in a patient - clinical manifestation and diagnostic difficulties
Autorzy:
Góra-Gębka, Magdalena
Woźniak, Małgorzata
Cielecka-Kuszyk, Joanna
Korpal-Szczyrska, Maria
Sznurkowska, Katarzyna
Zagierski, Maciej
Jankowska, Irena
Plata-Nazar, Katarzyna
Kamińska, Barbara
Liberek, Anna
Powiązania:
https://bibliotekanauki.pl/articles/1039288.pdf
Data publikacji:
2014
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
autoimmune disease
Graves' disease
celiac disease
liver abnormalities
children
Opis:
Autoimmune diseases due to probable common pathogenesis tend to coexist in some patients. Complex clinical presentation with diverse timing of particular symptoms and sophisticated treatment with numerous side effects, may cause diagnostic difficulties, especially in children. The paper presents diagnostic difficulties and pitfalls in a child with Graves' disease, celiac disease and liver function abnormalities.
Źródło:
Acta Biochimica Polonica; 2014, 61, 2; 281-284
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Influence of 4-hydroxynonenal and spleen cells on primary hepatocyte culture and a novel liver-derived cell line resembling hepatocyte stem cells
Autorzy:
Cipak, Ana
Borovic, Suzana
Jaganjac, Morana
Bresgen, Nikolaus
Kirac, Iva
Grbesa, Ivana
Mrakovcic, Lidija
Cindric, Marina
Scukanec-Spoljar, Mira
Gall-Troselj, Koraljka
Coric, Marijana
Eckl, Peter
Zarkovic, Neven
Powiązania:
https://bibliotekanauki.pl/articles/1040402.pdf
Data publikacji:
2010
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
novel-liver derived cell line
spleen
4-hydroxynonenal
hepatocyte
Opis:
Liver is a unique mammalian organ with a great capacity of regeneration related to its function. After surgical resection or injury, hepatic cells, especially hepatocytes, can proliferate rapidly to repair the damage and to regenerate the structure without affecting the function of the liver. Loss of catalase activity during regeneration indicates that oxidative stress is present in the liver not only in pathological conditions but also as a 'physiological' factor during regeneration. As we have shown in our previous work, liver stem cell-like cells treated with 4-hydroxynonenal (HNE), a cytotoxic and growth regulating lipid peroxidation product, recover in the presence of spleen cells. In the current study we characterized this novel cell line as liver-derived progenitor/oval-like cells, (LDP/OCs), i.e. functional liver stem-like cells. We showed that LDP/OC were OV6 positive, with abundant glycogen content in the cytoplasm and expressed α-fetoprotein, albumin, biliverdin reductase and γ-glutamyl transferase. Also, we compared their growth in vitro with the growth of cultured primary hepatocytes stressed with HNE and co-cultured with autologous spleen cells. The influence of spleen cells on HNE-treated primary hepatocytes and on LDP/OCs showed that spleen cells support in a similar manner the recovery of both types of liver cells indicating their important role in regeneration. Hence, LDP/OC cells may provide a valuable tool to study cell interactions and the role on HNE in liver regeneration.
Źródło:
Acta Biochimica Polonica; 2010, 57, 2; 185-191
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Selenium, glutathione and glutathione peroxidases in blood of patients with chronic liver diseases.
Autorzy:
Czuczejko, Jolanta
Zachara, Bronisław
Staubach-Topczewska, Ewa
Halota, Waldemar
Kędziora, Józef
Powiązania:
https://bibliotekanauki.pl/articles/1043405.pdf
Data publikacji:
2003
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
selenium
glutathione peroxidase
chronic liver disease
glutathione
oxidative stress
Opis:
Disturbances in the antioxidant system could play a role in pathogenesis of chronic liver disease. The aim of our study was to evaluate the levels/activities of antioxidants in blood of patients with chronic liver disease. We estimated selenium and glutathione concentrations and glutathione peroxidase activities in blood of 59 patients with chronic hepatitis B or C virus infection (group 1) and 64 patients with alcoholic, autoimmune or cryptogenic chronic liver disease (group 2). The results were compared with 50 healthy controls. Whole blood and plasma selenium and red cell glutathione concentrations were significantly lower in the patients compared with the controls. Red cell glutathione peroxidase activity was slightly reduced in both subgroups of group 1 and in group 2 with normal alanine aminotransferase values. Plasma glutathione peroxidase activity was slightly but significantly higher in patients with elevated aminotransferase values. The findings suggest that disturbances in antioxidant parameters in blood of patients with chronic liver disease may be the cause of the peroxidative damage of cells.
Źródło:
Acta Biochimica Polonica; 2003, 50, 4; 1147-1154
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Enzymatic oxidation of phthalazine with guinea pig liver aldehyde oxidase and liver slices: inhibition by isovanillin
Autorzy:
Panoutsopoulos, Georgios
Beedham, Christine
Powiązania:
https://bibliotekanauki.pl/articles/1041506.pdf
Data publikacji:
2004
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
xanthine oxidase
phthalazine
aldehyde oxidase
liver slices
disulfiram
isovanillin
allopurinol
Opis:
The enzymes aldehyde oxidase and xanthine oxidase catalyze the oxidation of a wide range of N-heterocycles and aldehydes. These enzymes are widely known for their role in the metabolism of N-heterocyclic xenobiotics where they provide a protective barrier by aiding in the detoxification of ingested nitrogen-containing heterocycles. Isovanillin has been shown to inhibit the metabolism of aromatic aldehydes by aldehyde oxidase, but its inhibition towards the heterocyclic compounds has not been studied. The present investigation examines the oxidation of phthalazine in the absence and in the presence of the inhibitor isovanillin by partially purified aldehyde oxidase from guinea pig liver. In addition, the interaction of phthalazine with freshly prepared guinea pig liver slices, both in the absence and presence of specific inhibitors of several liver oxidizing enzymes, was investigated. Aldehyde oxidase rapidly converted phthalazine into 1-phthalazinone, which was completely inhibited in the presence of isovanillin (a specific inhibitor of aldehyde oxidase). In freshly prepared liver slices, phthalazine was also rapidly converted to 1-phthalazinone. The formation of 1-phthalazinone was completely inhibited by isovanillin, whereas disulfiram (a specific inhibitor of aldehyde dehydrogenase) only inhibited 1-phthalazinone formation by 24% and allopurinol (a specific inhibitor of xanthine oxidase) had little effect. Therefore, isovanillin has been proved as an inhibitor of the metabolism of heterocyclic substrates, such as phthalazine, by guinea pig liver aldehyde oxidase, since it had not been tested before. Thus it would appear from the inhibitor results that aldehyde oxidase is the predominant enzyme in the oxidation of phthalazine to 1-phthalazinone in freshly prepared guinea pig liver slices, whereas xanthine oxidase only contributes to a small extent and aldehyde dehydrogenase does not take any part.
Źródło:
Acta Biochimica Polonica; 2004, 51, 4; 943-951
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Methylation demand: a key determinant of homocysteine metabolism.
Autorzy:
Brosnan, John
Jacobs, Rene
Stead, Lori
Brosnan, Margaret
Powiązania:
https://bibliotekanauki.pl/articles/1043276.pdf
Data publikacji:
2004
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
total plasma homocysteine
liver
creatine synthesis
phospholipid synthesis
S-adenosylmethionine
Opis:
Elevated plasma homocysteine is a risk factor for cardiovascular disease and Alzheimer's disease. To understand the factors that determine the plasma homocysteine level it is necessary to appreciate the processes that produce homocysteine and those that remove it. Homocysteine is produced as a result of methylation reactions. Of the many methyltransferases, two are, normally, of the greatest quantitative importance. These are guanidinoacetate methyltransferase (that produces creatine) and phosphatidylethanolamine N-methyltransferase (that produces phosphatidylcholine). In addition, methylation of DOPA in patients with Parkinson's disease leads to increased homocysteine production. Homocysteine is removed either by its irreversible conversion to cysteine (transsulfuration) or by remethylation to methionine. There are two separate remethylation reactions, catalyzed by betaine:homocysteine methyltransferase and methionine synthase, respectively. The reactions that remove homocysteine are very sensitive to B vitamin status as both the transsulfuration enzymes contain pyridoxal phosphate, while methionine synthase contains cobalamin and receives its methyl group from the folic acid one-carbon pool. There are also important genetic influences on homocysteine metabolism.
Źródło:
Acta Biochimica Polonica; 2004, 51, 2; 405-413
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
The 35 kDa acid metallophosphatase of the frog Rana esculenta liver: studies on its cellular localization and protein phosphatase activity.
Autorzy:
Szalewicz, Agata
Strzelczyk, Barbara
Sopel, Mirosław
Kubicz, Aleksandra
Powiązania:
https://bibliotekanauki.pl/articles/1043638.pdf
Data publikacji:
2003
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
metallophosphatase
acid phosphatase
frog liver
protein phosphatase
tyrosine protein phosphatase
Opis:
The cellular localization of the 35 kDa, low molecular mass acid metallophosphatase (LMW AcPase) from the frog (Rana esculenta) liver and its activity towards P-Ser and P-Tyr phosphorylated peptides were studied. This enzyme was localized to the cytoplasm of hepatocytes but did not appear in other cells of liver tissue (endothelium, macrophages, blood cells). This LMW AcPase does not display activity towards 32P-phosphorylase a under conditions standard for the enzymes of PPP family. Proteins containing P-Ser: rabbit 32P-phosphorylase a and phosvitin are hydrolysed only at acidic pH and are poor substrates for this enzyme. The frog AcPase is not inhibited by okadaic acid and F- ions, the Ser/Thr protein phosphatase inhibitors. Moreover, the frog enzyme does not cross-react with specific antisera directed against N-terminal fragment of human PP2A and C-terminal conserved fragment of the eukaryotic PP2A catalytic subunits. These results exclude LMW AcPase from belonging to Ser/Thr protein phosphatases: PP1c or PP2Ac. In addition to P-Tyr, this enzyme hydrolyses efficiently at acidic pH P-Tyr phosphorylated peptides (hirudin and gastrin fragments). Km value for the hirudin fragment (7.55 ± 1.59 × 10-6 M) is 2-3 orders of magnitude lower in comparison with other substrates tested. The enzyme is inhibited competitively by typical inhibitors of protein tyrosine phosphatases (PTPases): sodium orthovanadate, molybdate and tungstate. These results may suggest that the LMW AcPase of frog liver can act as PTPase in vivo. A different cellular localization and different response to inhibition by tetrahedral oxyanions (molybdate, vanadate and tungstate) provide further evidence that LMW AcPase of frog liver is distinct from the mammalian tartrate-resistant acid phosphatases.
Źródło:
Acta Biochimica Polonica; 2003, 50, 2; 555-566
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Glutathione and GSH-dependent enzymes in patients with liver cirrhosis and hepatocellular carcinoma
Autorzy:
Czeczot, Hanna
Ścibior, Dorota
Skrzycki, Michał
Podsiad, Małgorzata
Powiązania:
https://bibliotekanauki.pl/articles/1041298.pdf
Data publikacji:
2006
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
malondialdehyde
glutathione S-transferase
glutathione reductase
liver cirrhosis
glutathione peroxidase
glutathione
hepatocellular carcinoma
Opis:
We investigated glutathione level, activities of selenium independent GSH peroxidase, selenium dependent GSH peroxidase, GSH S-transferase, GSH reductase and the rate of lipid peroxidation expressed as the level of malondialdehyde in liver tissues obtained from patients diagnosed with cirrhosis or hepatocellular carcinoma. GSH level was found to be lower in malignant tissues compared to adjacent normal tissues and it was higher in cancer than in cirrhotic tissue. Non-Se-GSH-Px activity was lower in cancer tissue compared with adjacent normal liver or cirrhotic tissue, while Se-GSH-Px activity in cancer was found to be similar to its activity in cirrhotic tissue and lower compared to control tissue. An increase in GST activity was observed in cirrhotic tissue compared with cancer tissue, whereas the GST activity in cancer was lower than in adjacent normal tissue. The activity of GSH-R was similar in cirrhotic and cancer tissues, but higher in cancer tissue compared to control liver tissue. An increased level of MDA was found in cancer tissue in comparison with control tissue, besides its level was higher in cancer tissue than in cirrhotic tissue. Our results show that the antioxidant system of cirrhosis and hepatocellular carcinoma is severely impaired. This is associated with changes of glutathione level and activities of GSH-dependent enzymes in liver tissue. GSH and enzymes cooperating with it are important factors in the process of liver diseases development.
Źródło:
Acta Biochimica Polonica; 2006, 53, 1; 237-242
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł

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