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  1. 5 Acta Biochimica Polonica

  2. 3 Folia Biologica

  3. 3 Folia Histochemica et Cytobiologica

  4. 2 Cellular and Molecular Biology Letters

  5. 1 Acta Parasitologica

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  1. 1 Bartosz G.

  2. 1 Carnevale S.

  3. 1 Chaudhuri S.

  4. 1 Chen J.

  5. 1 Chen T.

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  1. 1 2021

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1

Mechanism of peroxynitrite interaction with cytochrome C

100%
Gebicka L., Didik J.
Acta Biochimica Polonica
|
2003
|
tom 50
|
nr 3
Kinetics of the reaction of peroxynitrite with ferric cytochrome c in the absence and presence of bicarbonate was studied. It was found that the heme iron in ferric cytochrome c does not react directly with peroxynitrite. The rates of the absorbance changes in the Soret region of cytochrome c spectrum caused by peroxynitrite or peroxynitrite/bicarbonate were the same as the rate of spontaneous isomerization of peroxynitrite or as the rate of the reaction of peroxynitrite with bicarbonate, respec­tively. This means that intermediate products of peroxynitrite decomposition, OH/ NO2 or, in the presence of bicarbonate, CO3- / NO2, are the species responsible for the absorbance changes in the Soret band of cytochrome c. Modifications of the heme center of cytochrome c by radiolytically produced radicals, OH, NO2 or CO3- , were also studied. The absorbance changes in the Soret band caused by radiolytically produced OH or CO3- were much more significant that those observed after peroxy­nitrite treatment, compared under similar concentrations of radicals. NO2 produced radiolytically did not interact with the heme center of cytochrome c. Cytochrome c ex­hibited an increased peroxidase-like activity after reaction with peroxynitrite as well as with radiolytically produced OH, NO2 or CO3- radicals. This means that modifi­cation of protein structure: oxidation of amino acids and/or tyrosine nitration, facili­tates reaction of H2O2 with the heme iron of cytochrome c, followed by reaction with the second substrate.
2

Proteins involved in maturation pathways of plant mitochondrial and plastid c-type cytochromes

75%
Rurek M.
Acta Biochimica Polonica
|
2008
|
tom 55
|
nr 3
417-433
c-type cytochromes are characterized by the presence of two covalent bonds linking heme to apocytochrome and by the heme attachment motif in the apoprotein. Several molecular systems for the maturation of c-type cytochromes have evolved in different organisms. The best characterized are three of them: system I, system II and system III. Heme is synthesized in bacterial cytoplasm, in plastids, and in animal and fungal mitochondria. Therefore the maturation of bacterial and plastid c-type cytochromes involves the transport of heme and apocytochrome from the n-side to the p-side of the respective biological membranes and the formation of the covalent bond at the p-side. It should be underlined that the site of the c-type apocytochrome synthesis is also distinct from the site of its functioning. The aim of this review is to present the current state of knowledge concerning the structure and function of two systems – system I and system II – in the maturation of plant mitochondrial and plastid c-type cytochromes, respectively.
3

The condition of Chorzow hypotrophic and born-at-term infants in relation to the morphochemical features of the placentae

75%
Kasznia-Kocot J., Zamorska L., Zolnierek M., Niwelinski J.
Polish Journal of Environmental Studies
|
1993
|
tom 02
|
nr 4
Morphochemical tests of placentae and clinical examinations of babies born-at-term with intrauterine hypotrophy and of normal body weight were conducted. A decreased activity of cytochrome c oxidase in syncytiotrophoblast, cytotrophoblast extravillous, amniotic epithelium as well as in decidual cells was observed. In all placenta samples we found a diminished percentage of intesvillous space, disordered maturing of villi, lower epithelial plates and striking loss of cytochrome c oxidase activity. It was concluded that diminished metabolic efficiency of placentae is the decisivee risk factor for hypotrophy in chemically polluted areas.
4

Molecular diagnosis of natural fasciolosis by DNA detection in sheep faeces

63%
Carnevale S., Pantano M. L., Kamenetzky L., Malandrini J. B., Soria C. C., Velasquez J. N.
Acta Parasitologica
|
2015
|
tom 60
|
nr 2
5

Does repeated gold-nanoparticles administration affect pars distalis hormonal and folliculo-stellate cells in adult male albino rats?

63%
Omar A. I., Kamar S. S.
Folia Histochemica et Cytobiologica
|
2021
|
tom 59
|
nr 2
6

The relationships within the Poecilimon ornatus group (Orthoptera: Phaneropterinae) based on the cytochrome C oxidase I gene

63%
Kocinski M.
Folia Biologica
|
2020
|
tom 68
|
nr 1
7

Activation of the intrinsic and extrinsic pathways in high pressure-induced apoptosis of murine erythroleukemia cells

63%
Yamaguchi T., Hashiguchi K., Katsuki S., Iwamoto W., Tsuruhara S., Terada S.
Cellular and Molecular Biology Letters
|
2008
|
tom 13
|
nr 1
49-57
We previously demonstrated that caspase-3, an executioner of apoptosis, is activated in the pressure-induced apoptosis of murine erythroleukemia (MEL) cells (at 100 MPa). Here, we examined the pathway of caspase-3 activation using peptide substrates and caspase inhibitors. Using the substrates of caspases-8 and -9, it was found that both are activated in cells under high pressure. The production of nuclei with sub-G1 DNA content in 100 MPa-treated MEL cells was suppressed by inhibitors of caspases-8 and -9, and pan-caspase. In 100 MPa-treated cells, pan-caspase inhibitor partially prevented the cytochrome c release from the mitochondria and the breakdown of mitochondrial membrane potential. These results suggest that the intrinsic and extrinsic pathways are activated in apoptotic signaling during the high pressure-induced death of MEL cells.
8

Changes of mitochondrial pathway in hypoxia-reoxygenation induced cardiomyocytes apoptosis

63%
He A., Wang J., Gui C., Jiang Y., Sun Y., Chen T.
Folia Histochemica et Cytobiologica
|
2007
|
tom 45
|
nr 4
397-400
9

Synthesis short-living ATP on plasma membranes in responses to growth factors and cytokines: the role 5'-p-fluorosulfonylbenzoyl adenosine [FSBA] in its detection

63%
Karelin A. A., Demidova V. S., Globa A. G.
Cellular and Molecular Biology Letters
|
1998
|
tom 03
|
nr 3
10

Correlation of mATPase, parvalbumin, and cytochrome c oxidase in rat skeletal muscle fibres

63%
Zawadowska B., Muntener M.
Folia Biologica
|
1997
|
tom 45
|
nr 3-4
11
Content available remote

Effect of 5-week moderate intensity endurance training on the oxidative stress, muscle specific uncoupling protein (UCP3) and superoxide dismutase (SOD2) contents in vastus lateralis of young, healthy men

51%
Majerczak J., Rychlik B., Grzelak A., Grzmil P., Karasinski J., Pierzchalski P., Pulaski L., Bartosz G., Zoladz J. A.
Journal of Physiology and Pharmacology
|
2010
|
tom 61
|
nr 6
12

TLRs and Bcl-2 family proteins in neutrophils of oral cavity cancer patients

51%
Jablonska E., Garley M.
Folia Histochemica et Cytobiologica
|
2009
|
tom 47
|
nr 4
13
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Content available

Morphological and physiological characterization of the delta-psaL mutant of cyanobacterium Synechocystis PCC6803

51%
Klodawska K., Kis M., Malec P., Kovacs L., Gombos Z., Strzalka K.
BioTechnologia. Journal of Biotechnology Computational Biology and Bionanotechnology
|
2013
|
tom 94
|
nr 3
14

Interaction of an anticancer ruthenium complex HInd[RuInd2CI4] with cytochrome C

51%
Trynda-Lemiesz L.
Acta Biochimica Polonica
|
2004
|
tom 51
|
nr 1
Cytochrome c is an important electron transfer protein in the respiratory chain, shuttling electrons from cytochrome c reductase to cytochrome c oxidase. Extensive chemical modification studies indicate significant electrostatic interactions between these proteins and show that all structural and conformational changes of cytochrome c can influence the electron transport. In the present work we examine the effect of an anticancer ruthenium complex, trans-Indazolium (bisindazole) tetra- chlororuthenate(III) (HInd[RuInd2Cl4]), on the conformation of cytochrome c, the state of the heme moiety, formation of the protein dimer and on the folding state of apocytochrome c. For this purpose, gel-filtration chromatography, absorption sec­ond derivative spectroscopy, circular dichroism (CD) and inductively coupled plasma atomic emission spectroscopy (ICP(AES)) were used. The present data have revealed that binding of the potential anticancer drug HInd[RuInd2Cl4] complex to cytochrome c induces a conformation of the protein with less organized secondary and tertiary structure.
15

Overexpression of BimSs3, the novel isoform of Bim, can trigger cell apoptosis by inducing cytochrome c release from mitochondria

51%
Liu L., Chen J., Zhang J., Ji C., Zhang X., Gu S., Xie Y., Mao Y.
Acta Biochimica Polonica
|
2007
|
tom 54
|
nr 3
Bim is defined as the pro-apoptotic BH3-only protein of the Bcl-2 family, which is a critical sensor and mediator in the mitochondrial-dependent apoptosis. In a previous work, we have cloned a novel transcript of Bim (GenBank accession number: AY305716) from the fetal brain cDNA, which is widely expressed in some carcinoma tissues and normal human tissues. According to the sequence analysis and the newly-defined nomenclature system of Bim isoforms (Adachi et al., 2005, Cell Death Differ 2: 192), we term it BimSs3 according to its characteristic structure. The subcellular location analysis indicated that the fused protein GFP-BimSs3 is distributed in the whole cell, mainly to the nucleus. Overexpression of BimSs3 in HEK293 cells causes apoptosis (28.16 ± 1.55%) compared to the negative control (5.44 ± 2.63%). It also causes cytochrome c release from the mitochondrial fraction to the cytosolic fraction during apoptosis. Western blotting assay indicates the molecular mass of GFP-BimSs3 is approximately 31.0 kDa (GFP: 27 kDa). Hence the open reading frame of BimSs3 may initiate at the second ATG and encodes a 36 amino-acid peptide with BH3 domain.
16

Differential peroxidase activity in the thyroid gland and oviduct of a wild avian species, the tree pie [Dendrocitta vagabunda]

51%
Chaudhuri S., Maiti B. R.
Folia Biologica
|
1997
|
tom 45
|
nr 1-2
17

Current views on apoptosis in theory and medical practice

51%
Szpringer E., Lutnicki K.
Polish Journal of Veterinary Sciences
|
2003
|
tom 06
|
nr 1
Apoptosis is a kind of cell death essential for normal functioning and survival of most multicellular organisms. Apoptosis plays an important role in physiological processes and in pathophysiology of some chronic diseases, including autoimmunity, cancer, lymphoma, AIDS, neurodegeneration and others. The present paper describes the interdisciplinary pathogenesis of programmed cell death, the mechanisms inducing apoptosis and the role of apoptosis in some physiological phenomena and in medical practice.
18

Probing protein structure by limited proteolysis

51%
Fontana A., Polverino de Laureto P., Spolaore B., Frare E., Picotti P., Zambonin M.
Acta Biochimica Polonica
|
2004
|
tom 51
|
nr 2
Limited proteolysis experiments can be successfully used to probe conformational features of proteins. In a number of studies it has been demonstrated that the sites of limited proteolysis along the polypeptide chain of a protein are characterized by enhanced backbone flexibility, implying that proteolytic probes can pinpoint the sites of local unfolding in a protein chain. Limited proteolysis was used to analyze the partly folded (molten globule) states of several proteins, such as apomyoglobin, a-lactalbumin, calcium-binding lysozymes, cytochrome c and human growth hor­mone. These proteins were induced to acquire the molten globule state under spe­cific solvent conditions, such as low pH. In general, the protein conformational fea­tures deduced from limited proteolysis experiments nicely correlate with those deriv­ing from other biophysical and spectroscopic techniques. Limited proteolysis is also most useful for isolating protein fragments that can fold autonomously and thus be­have as protein domains. Moreover, the technique can be used to identify and pre­pare protein fragments that are able to associate into a native-like and often func­tional protein complex. Overall, our results underscore the utility of the limited pro- teolysis approach for unravelling molecular features of proteins and appear to prompt its systematic use as a simple first step in the elucidation of structure-dynamics- function relationships of a novel and rare protein, especially if available in minute amounts.
19

Wlasciwosci pepsyny jako bialka polianionowego. Cz.III. Degradacja przez pepsyne kompleksujacych z nia bialek zasadowych

38%
Roszkowska-Jakimiec W., Gacko M., Worowska A., Greczaniuk A.
Bromatologia i Chemia Toksykologiczna
|
1998
|
tom 31
|
nr 1
71-74
Określono zdolność pepsyny do degradacji kompleksującej z nią protaminy, histonu całkowitego, histonu H1, H2A, H2B, H3 i H4, cytochromu c, lizozymu i rybonukleazy. Wykazano, że tworzenie kompleksów pepsyny z białkami zasadowymi nie znosi jej aktywności proteolitycznej.
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