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1.
Patol Fiziol Eksp Ter ; (1): 48-51, 2010.
Artigo em Russo | MEDLINE | ID: mdl-20731127

RESUMO

The mechanisms of mitochondrial dysfunction development in vessels upon peroxodized LDL (pLDL) influence are discussed. Is is shown that the components of pLDL induce the formation of covalent complexes with cell proteins and destabilize cellular membrane microdomain structure that leads to membrane proteins dysfunction, Ca2+ liberation into cytosol from its stores, endoplasmic reticulum stress, increase in reactive oxygen species production by NADPH-oxidases. These effects cause disturbances in mitochondria of target cells, increases in reactive oxygen species production, mitochondrial pathway of cell death. The processes under discussion contribute to the atherosclerotic leisure development.


Assuntos
Aterosclerose/metabolismo , Vasos Sanguíneos/metabolismo , Mitocôndrias/metabolismo , Doenças Mitocondriais/metabolismo , Peróxidos/metabolismo , Animais , Aterosclerose/patologia , Vasos Sanguíneos/patologia , Cálcio/metabolismo , Morte Celular , Humanos , Microdomínios da Membrana/metabolismo , Microdomínios da Membrana/patologia , Proteínas de Membrana/metabolismo , Mitocôndrias/patologia , Doenças Mitocondriais/patologia
3.
Mol Biol (Mosk) ; 42(1): 88-95, 2008.
Artigo em Russo | MEDLINE | ID: mdl-18389624

RESUMO

We conducted a comparative study of the properties of topoisomerase I isolated from maize nuclei and mitochondria. We found that nuclear and mitochondrial enzymes possess different ability to bind single stranded DNA. Study of the enzyme activity dependence on Mg2+ demonstrated an absolute dependence of the mitochondrial topoisomerase activity. Contrary, nuclear enzyme activity was not absolutely dependent but stimulated by the magnesium cation. Mitochondrial topoisomerase formed covalent bond with the 5'-end of the cleaved DNA what is unique property of prokaryotic topoisomerase I. Nuclear enzyme bound covalently to the 3'-end like all eukaryotic topoisomerases I. The search through databases revealed genes which could encode mitochondrial topoisomerase I in the genomes of higher plants. Using both cDNA sequencing and in silico methods we demonstrated an existence of the ortholog gene in the maize genome. This gene shares significant homology with prokaryotic topoisomerase I genes that may explain differences in the properties of the mitochondrial and nuclear enzyme. Data obtained is of a significant interest both from the point of view of plant organelle evolution and mitochondrial genome expression mechanisms study.


Assuntos
Núcleo Celular/enzimologia , DNA Topoisomerases Tipo I/metabolismo , Mitocôndrias/enzimologia , Proteínas Mitocondriais/metabolismo , Proteínas Nucleares/metabolismo , Proteínas de Plantas/metabolismo , Zea mays/enzimologia , Núcleo Celular/química , Núcleo Celular/genética , Clonagem Molecular , DNA Topoisomerases Tipo I/química , DNA Topoisomerases Tipo I/genética , DNA Complementar/genética , DNA de Cadeia Simples/química , DNA de Cadeia Simples/metabolismo , Evolução Molecular , Genoma Mitocondrial/fisiologia , Magnésio/química , Magnésio/metabolismo , Mitocôndrias/química , Mitocôndrias/genética , Proteínas Mitocondriais/química , Proteínas Mitocondriais/genética , Proteínas Nucleares/química , Proteínas Nucleares/genética , Proteínas de Plantas/química , Proteínas de Plantas/genética , Zea mays/genética
6.
Mol Biol (Mosk) ; 39(3): 394-402, 2005.
Artigo em Russo | MEDLINE | ID: mdl-15981569

RESUMO

We purified DNA binding proteins which interact with the promoter region of cox1 gene from maize mitochondria. Presence of poly[dIdC-dIdC] and KCl in concentrations up to 500 mM had no influence on binding efficiency demonstrating high specificity of complexes formed. Surprisingly, we did not detect DNA binding when probes containing promoter regions of other mitochondrial genes (cox3, rrn26) were used. Mobility shift competition studies also suggest that the protein posseses binding specificity towards cox1 promoter. The core motif AAGTA proved to be necessary for DNA binding. Using combination of EMSA and elution of proteins from PAG we showed that DNA-protein complex formed contains three polypeptides with molecular mass 60, 44 and 22 kD. We suggest that the isolated proteins may play an important role in the regulation of plant cox1 gene transcription.


Assuntos
Proteínas de Ligação a DNA/química , Mitocôndrias/química , Proteínas de Plantas/química , Regiões Promotoras Genéticas , Prostaglandina-Endoperóxido Sintases/genética , Zea mays/química , Ciclo-Oxigenase 1 , Proteínas de Ligação a DNA/isolamento & purificação , Mitocôndrias/genética , Proteínas de Plantas/isolamento & purificação , Zea mays/genética
7.
Mol Biol (Mosk) ; 38(3): 420-8, 2004.
Artigo em Russo | MEDLINE | ID: mdl-15285610

RESUMO

With PCR, RT-PCR, and direct sequencing, complete nucleotide sequences were established for the Elymus sibiricus mitochondrial cytochrome c oxidase subunit 3 gene (cox3) and its cDNA. The cox3 transcript was shown to have 12 editing sites with changes affecting the amino acid sequence of the protein product. The editing of the primary cox3 transcript was found to change the position of a site of protein-protein interactions. The results demonstrate again the important role of mRNA editing in posttranscriptional regulation of the expression of plant mitochondrial genes.


Assuntos
Complexo IV da Cadeia de Transporte de Elétrons/genética , Elymus/genética , Proteínas de Membrana/genética , Mitocôndrias/genética , Edição de RNA , RNA Mensageiro/genética , Proteínas de Saccharomyces cerevisiae/genética , Sequência de Aminoácidos , Sequência de Bases , DNA Complementar , DNA de Plantas , Complexo IV da Cadeia de Transporte de Elétrons/química , Proteínas de Membrana/química , Dados de Sequência Molecular , Proteínas de Saccharomyces cerevisiae/química , Homologia de Sequência de Aminoácidos
8.
Genetika ; 39(10): 1322-7, 2003 Oct.
Artigo em Russo | MEDLINE | ID: mdl-14658336

RESUMO

To reconstruct the systematic relationships of larch Larix sukaczewii, we used the chloroplast trnK intron sequences of L. decidua, L. sukaczewii, L. sibirica, L. czekanovskii, and L. gmelinii. Analysis of phylogenetic trees constructed using the maximum parsimony and maximum likelihood methods showed a clear divergence of the trnK intron sequences between L. sukaczewii and L. sibirica. This divergence reaches intraspecific level, which supports a previously published hypothesis on the taxonomic isolation of L. sukaczewii.


Assuntos
DNA de Cloroplastos/genética , Íntrons , Larix/genética , Proteínas de Plantas/genética , Sequência de Bases , Primers do DNA , Reação em Cadeia da Polimerase , Especificidade da Espécie
9.
Izv Akad Nauk Ser Biol ; (3): 306-10, 2003.
Artigo em Russo | MEDLINE | ID: mdl-12816062

RESUMO

Conditions and kinetic characteristics of nucleic acid synthesis were studied in the isolated mitochondria of Elymus sibiricus from different natural populations. The results showed the reciprocal dependence of RNA and DNA synthesis rates in the mitochondrial genetic system of E. sibiricus seedlings of different genotypes.


Assuntos
DNA Mitocondrial/biossíntese , DNA de Plantas/biossíntese , Elymus/metabolismo , Mitocôndrias/metabolismo , RNA de Plantas/biossíntese , RNA/biossíntese , Elymus/citologia , Elymus/genética , Genótipo , RNA Mitocondrial
10.
Zh Obshch Biol ; 61(2): 157-62, 2000.
Artigo em Inglês | MEDLINE | ID: mdl-10778389

RESUMO

The nucleotide sequence of mitochondrial ribosomal protein rps13 gene from wild perennial grass Elymus sibiricus is presented. It was determined by the method of PCR amplification with specific oligonucleotide primers and the direct sequencing of the amplification product. The sequence of E. sibiricus mitochondrial gene for S13 predicts a hydrophobic ribosomal protein of 116 amino acids that shows strong similarity to those of wheat (99.7% identity) and maize (98%). The deduced amino acid sequence of S13 protein from E. sibiricus and homologous plant's (Zea mays, Daucus carota, Nicotiana tabacum, Marchantia polymorpha) and nonplant's (Escherichia coli) proteins shows the presence of hydrophobic amino acids' motif -L-X10-L-X10-M-X10-L-X10-L-. Slightly modified it can be found in many other ribosomal proteins. This conserved motif is presumed to be particularly important for association of the ribosomal S13 protein with other proteins in the small subunit of the mitochondrial ribosome.


Assuntos
Aminoácidos/genética , DNA Mitocondrial/genética , DNA de Plantas/genética , Poaceae/genética , Sequência de Aminoácidos , Sequência de Bases , Escherichia coli/genética , Dados de Sequência Molecular , Reação em Cadeia da Polimerase
12.
Biokhimiia ; 57(10): 1467-71, 1992 Oct.
Artigo em Russo | MEDLINE | ID: mdl-1457594

RESUMO

The amino acid sequences of subunit 9 of plant mitochondrial ATP-synthase contain a leucine motif which differs from the leucine repeat earlier detected within the composition of proteinaceous products of Myc, Fos, and Jun proto-oncogens. The structural organization of this repeat in proteolipid sequences can be modified via transformation of serine triplets into leucine ones as a result of editing of an appropriate mRNA.


Assuntos
Leucina/química , Mitocôndrias/enzimologia , Plantas/enzimologia , ATPases Translocadoras de Prótons/química , RNA Mensageiro/química , Sequência de Aminoácidos , Genes fos , Genes jun , Genes myc , Dados de Sequência Molecular , Edição de RNA
15.
Vopr Med Khim ; 26(4): 498-502, 1980.
Artigo em Russo | MEDLINE | ID: mdl-7456389

RESUMO

Kinetic patterns of oxydative phosphorylation were studied in rat liver mitochondria in dynamics of cholestasis and after addition of bile acids to mitochondria in vitro. Within the 1 and 3 days of cholestasis mitochondrial synthesis of ATP was decreased due to inhibition of ATP and ADP transport by the bile acids. At the period within 3 and 15 days uncoupling of the oxidative phosphorylation occurred; the phenomenon observed might be a result of impairment in the structure of inner mitochondrial membrane.


Assuntos
Colestase Extra-Hepática/metabolismo , Mitocôndrias Hepáticas/metabolismo , Fosforilação Oxidativa , Nucleotídeos de Adenina/metabolismo , Animais , Ácidos e Sais Biliares/farmacologia , Carnitina/farmacologia , Humanos , Masculino , Translocases Mitocondriais de ADP e ATP/metabolismo , Ratos , Soroalbumina Bovina/farmacologia , Succinatos/metabolismo
16.
Biull Eksp Biol Med ; 82(10): 1200-2, 1976 Oct.
Artigo em Russo | MEDLINE | ID: mdl-1029502

RESUMO

Experiments were conducted on freshly isolated rat liver mitochondria and mitochondria subjected to ageing by two different methods. It was shown that the work of the mitochondrial system of fatty acid activation could lead to inhibition of the adenine nucleotide transport through the internal mitochondrial membrane. Inhibition of adenine nucleotide translocase was eliminated by preincubation of mitochondria with carnitine. The presence in the mitochondrial preparations of fatty acids in the concentration adequate for induction of inhibition of addition of CoA and ATP served as a preculiarity of adenine nucleotide translocase inhibition of the ageing mitochondria. The data obtained permitted to make a supposition on the participation of acyl-CoA formed by the mitochondrial acyl-CoA-synthetase in the regulation of adenine nucleotide transport into the mitochondria.


Assuntos
Ácidos Graxos/metabolismo , Mitocôndrias Hepáticas/metabolismo , Translocases Mitocondriais de ADP e ATP/metabolismo , Nucleotidiltransferases/metabolismo , Difosfato de Adenosina/antagonistas & inibidores , Difosfato de Adenosina/metabolismo , Trifosfato de Adenosina/antagonistas & inibidores , Trifosfato de Adenosina/metabolismo , Trifosfato de Adenosina/farmacologia , Envelhecimento , Animais , Transporte Biológico , Carnitina/farmacologia , Coenzima A/farmacologia , Masculino , Translocases Mitocondriais de ADP e ATP/antagonistas & inibidores , Ratos
17.
Biull Eksp Biol Med ; 82(9): 1059-61, 1976 Sep.
Artigo em Russo | MEDLINE | ID: mdl-990457

RESUMO

After 4 injections of phenobarbital (PB), 3-methylcholantrene in olive oil (MC) or olive oil alone the corresponding concentrations of acyl-CoAs in the liver (in per cent to control) were: 73, 167, 230. The liver mitochondria from rats injected with oil and MC showed inhibition of the metabolic state 3 respiratory rate after Chance, Preincubation with carnitine elimated this inhibition. In accordance with these data the blood ketone body level in the administration of PB, MC and oil were 31, 136, and 342%, respectively. The phosphate potential value declined only after the injections of olive oil when the ATP concentration in the liver was markedly diminished. The AMP concentration doubled in the liver of rats after the PB and oil injection. Comparison of the data on the induction of microsomal monoxigenases by PB and MC permitted to draw a conclusion that there was a different metabolic fate of acyl-CoAs in these two cases.


Assuntos
Fígado/metabolismo , Metilcolantreno/farmacologia , Fenobarbital/farmacologia , Difosfato de Adenosina/metabolismo , Monofosfato de Adenosina/metabolismo , Trifosfato de Adenosina/metabolismo , Animais , Coenzima A/metabolismo , Corpos Cetônicos/metabolismo , Masculino , Mitocôndrias Hepáticas/metabolismo , Consumo de Oxigênio/efeitos dos fármacos , Ratos , Compostos de Sulfidrila/metabolismo
18.
Biull Eksp Biol Med ; 81(2): 166-8, 1976 Feb.
Artigo em Russo | MEDLINE | ID: mdl-1276407

RESUMO

Studies with liver mitochondria from rats which starved for 48 hours showed the rate of ADP-stimulated respiration to be 20% lower than in the presence of an uncoupler. This effect was eliminated by preincubation of mitochondria with carnitine. Mitochondria from fed rats were characterized by a considerable decrease of states 3 and 4 respiration. In this case carnitine produced no effect. Preincubation of mitochondria from the liver of fed rats with alpha-ketoglutarate resulted in a substantial increase of the states 3 and 4 respiratory rates. There proved to exist at least two types of regulation of adenine nucleotide transport through the inner mitochondrial membrane depending on the metabolic state of the organism, i.e. by inhibition of adenine-nucleotide translocase by cytoplasmic acyl-CoAs and by control of intramitochondrial adenine nucleotide pool.


Assuntos
Nucleotídeos de Adenina/metabolismo , Mitocôndrias Hepáticas/metabolismo , Consumo de Oxigênio , Inanição/metabolismo , Difosfato de Adenosina/metabolismo , Monofosfato de Adenosina/metabolismo , Trifosfato de Adenosina/metabolismo , Animais , Transporte Biológico Ativo , Carnitina/uso terapêutico , Ácidos Cetoglutáricos/metabolismo , Ratos , Inanição/tratamento farmacológico , Succinatos/metabolismo
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