Your browser doesn't support javascript.
loading
Mostrar: 20 | 50 | 100
Resultados 1 - 15 de 15
Filtrar
Mais filtros








Base de dados
Intervalo de ano de publicação
1.
Fiziol Cheloveka ; 43(1): 55-62, 2017 Jan.
Artigo em Inglês, Russo | MEDLINE | ID: mdl-29509363

RESUMO

We investigated the effect of different breathing strategies on postural performance in the patients with joint mobility limitations. The amplitude and velocity of thecenter-of-pressure movements in the frontal.and sagittal planes were measured by the force platform in48 healthy volunteers. The stability of vertical posture was estimated during normal breathing, inspiratory and expiratory breath holding and hyperventilation with immobilization of the neck, trunk, hip and knee joints, and without immobilization. In general, the restriction of mobility caused a reduction in the postural stability in the sagittal plane, while the frontalbody swayamplitude decreased. These results suggest that body immobilization reduces the ability to compensate the effect of respiration on the stability of vertical posture in the sagittal plane and, on the contrary, facilitatesthe balance in the frontal plane.


Assuntos
Suspensão da Respiração , Hiperventilação/fisiopatologia , Equilíbrio Postural , Restrição Física/fisiologia , Adolescente , Feminino , Voluntários Saudáveis , Humanos , Articulações , Masculino , Pressão , Adulto Jovem
2.
Biochemistry (Mosc) ; 80(6): 763-8, 2015 Jun.
Artigo em Inglês | MEDLINE | ID: mdl-26531021

RESUMO

Contemporary concepts on a possible mechanism of erythrocyte hemolysis induced by photooxidized psoralen - the medicinal photosensitizing furocoumarin - are reviewed. The hypothesis on the mechanochemical mechanism of hemolysis is considered in view of recent data on photoinduced aggregation in photooxidized psoralen solutions. Appropriate chemical structures of photoproduct hemolysins and aggregating photoproducts are discussed.


Assuntos
Eritrócitos/efeitos dos fármacos , Furocumarinas/farmacologia , Hemólise/efeitos dos fármacos , Fármacos Fotossensibilizantes/farmacologia , Animais , Morte Celular/efeitos dos fármacos , Eritrócitos/patologia , Proteínas Hemolisinas/sangue , Humanos , Oxirredução
3.
Fiziol Cheloveka ; 40(1): 90-5, 2014.
Artigo em Russo | MEDLINE | ID: mdl-25272773

RESUMO

The influence of breath holding and voluntary hyperventilation on the classic stabilometric parameters and the frequency characteristic of stabilographic signal were studied. We measured the stabilometric parameters on the force platform ("Ritm", Russia) on the healthy volunteers (n = 107) during quiet breath, voluntary hyperventilation (20 seconds) and maximal inspiratory breath holding (20 seconds). Respiratory frequency, respiratory amplitude and ventilation were estimated with strain gauge. We found that antero-posterior and medio-lateral sway amplitude and velocity as well as sway surface at breath-holding and at quiet breathing were the same, so breath holding didn't influence the postural stability. However the spectral parameters shifted to the high frequency range due to alteration of the respiratory muscles contractions during breath-holding versus quiet breath. Voluntary hyperventilation caused significant increase of all stabilographic indices that implied an impairment of postural stability, which was due to the increase of respiration frequency and amplitude. We also found that the spectral indices moved toward the high-frequency range with more pronounced degree of this shift versus breath holding. Besides, amplitudes of spectral peaks also increased. Perhaps such change of spectral indices was due to distortion of proprioceptive information because of increased excitability of nerve fibers during hyperventilation. Maximal inspiration breath holding causes strain of the postural control mechanisms that is reflected as elevation of postural sway frequency with no postural stability changes. Hyperventilation leads to the most prominent strain of balance function and decrease of steadiness that is manifested as increase of center of pressure oscillations amplitude and frequency.


Assuntos
Suspensão da Respiração , Hiperventilação , Postura/fisiologia , Adulto , Feminino , Humanos , Masculino , Músculos Respiratórios/fisiologia , Federação Russa
4.
Fiziol Cheloveka ; 37(3): 132-4, 2011.
Artigo em Russo | MEDLINE | ID: mdl-21780690

RESUMO

The bioimpedance spectroscopy (BIS) parameters of the suspensions of young and old erythrocytes were studied. The separation of the erythrocytes by age was made by density gradient. The BIS parameters: extracellular (Re) and intracellular (Ri) fluid resistance, characteristic frequency (Fchar), cell membranes capacitance (Cm) and Alpha parameter of concentrate suspensions of young and old erythrocytes were measured on the BIA analyzer ABC-01 "Medass" in the frequency range 5-500 kHz. It was found that Re (300.4 +/- 30.0 Ohm and 261.2 +/- 21.8 Ohm for old and young respectively, p < 0.05), Ri (86.6 +/- 9.1 Ohm and 73.4 +/- 7.3 Ohm for old and young respectively, p < 0.001) and Alpha (0.305 +/- 0.003 and 0.302 +/- 0.001 for old and young respectively, p < 0.05) of the old erythrocytes suspensions were higher, than of the young one, and Fchar (308.3 +/- 42.0 kHz and 347.4 +/- 48.0 kHz for old and young respectively, p <0.05) and Cm (99.3 +/- 10.1 pF and 112.8 +/- 6.3 pF for old and young respectively, p < 0.01) of the old erythrocytes were lower, than of the young one. The found differences between electrical properties of the suspensions of young and old erythrocytes were obviously determined by the alterations of the red blood cells during aging (growth of intracellular hemoglobin concentration, erythrocytes rapprochement because of diminishing of surface negative charge, increase of red blood cell sphericity and cell membrane permeability for ions). Thus the BIS parameters are related to the erythrocyte aging.


Assuntos
Permeabilidade da Membrana Celular/fisiologia , Senescência Celular/fisiologia , Espectroscopia Dielétrica , Eritrócitos/metabolismo , Hemoglobinas/metabolismo , Humanos
5.
Klin Lab Diagn ; (1): 20-3, 2011 Jan.
Artigo em Russo | MEDLINE | ID: mdl-21427942

RESUMO

The purpose of the study was to determine the capability of bioimpedance spectroscopy (BIS) to evaluate the hematological and biochemical parameters of blood. BIS readings were estimated on an ABC-01 Medass hardware-computer complex; blood hematological and biochemical parameters (n = 46) were determined on automated analyzers. The BIS readings were found to be closely correlated with packed cell volume and hemoglobin and red blood cell values, but weakly related to plasma biochemical parameters and white blood cell counts. BIS readings may be used to calculate red blood cell counts taken in units of measurement in hematological practice, by applying the multiple regression equations. Thus, the blood BIS technique may be employed to estimate basic hematological parameters (hemoglobin concentration, red blood cell counts, and packed cell volume).


Assuntos
Análise Química do Sangue/métodos , Sangue/metabolismo , Espectroscopia Dielétrica/métodos , Eritrócitos/metabolismo , Hemoglobinas/metabolismo , Eritrócitos/química , Feminino , Hemoglobinas/química , Humanos , Masculino
6.
Biofizika ; 49(2): 322-38, 2004.
Artigo em Russo | MEDLINE | ID: mdl-15129631

RESUMO

Furocoumarins (psoralens) are photosensitizers of plant origin, which increase the sensitivity of biological objects to near ultraviolet (UV-A, 320-400 nm). In combination with UV-A, they are successfully used for treating many dermal and autoimmune diseases (PUVA therapy and photophoresis). Along with therapeutic effects, the furocoumarin photochemotherapy induces a number of side-effects (erythema, edema, hyperpigmentation, and premature aging of skin). All photobiological effects of furocoumarins result from their photochemical reactions. Therefore, in order to advance the therapy, it is necessary to know the photochemical mechanisms of induction of both side- and therapeutic effects. The types of photoreactions of furocoumarins classified with respect to reactive photoproducts interacting with substrate were considered. Primary emphasis was placed on reactions proceeding with the participation of photooxidation products of furocoumarins. Among these photoproducts, at least two types can be distinguished. Some of them possess membranotoxic properties, others produce the immunosuppressory action in vivo. The photochemical mechanisms of the formation of the photoproducts of furocoumarins are different. It was found that, by varying the illumination conditions (intensity of UV-A radiation or the concentration of the photosensitizer), it is possible to obtain the photoproducts of furocoumarins that have either membranotoxic or immunosuppressory properties. It was found that the mechanisms of the immunosuppressive action of the photooxidation products of furocoumarins have some features in common with those underlying the PUVA therapy and photophoresis. It is assumed that the photochemical basis of the therapeutic action of furocoumarins is the reactions with the involvement of the products of their photooxidation.


Assuntos
Furocumarinas/farmacologia , Luz , Fármacos Fotossensibilizantes/farmacologia , Animais , Furocumarinas/efeitos adversos , Furocumarinas/química , Hemólise/efeitos dos fármacos , Hemólise/efeitos da radiação , Humanos , Imunossupressores/efeitos adversos , Oxirredução , Fotoquímica , Fármacos Fotossensibilizantes/efeitos adversos , Fármacos Fotossensibilizantes/química , Relação Estrutura-Atividade
7.
IUBMB Life ; 51(2): 93-7, 2001 Feb.
Artigo em Inglês | MEDLINE | ID: mdl-11463170

RESUMO

The expression of the cytM gene, which encodes cytochrome cM in Synechocystis sp. PCC 6803, is induced under stress conditions such as low temperature. Results of spectrophotometric studies revealed that cytochrome cM was oxidized by light absorbed by photosystem I in cells that had acclimatized to a low temperature. However, no similar light-induced oxidation of cytochrome cM was observed in delta cytM mutant cells. The kinetics of the oxidation and reduction of P700 before and after acclimation of Synechocystis cells to low temperature suggested that cytochrome cM might donate electrons to photooxidized P700. Our observations indicate that cytochrome cM is synthesized under low-temperature stress and that it might carry electrons directly to P700+ in photosystem I.


Assuntos
Proteínas de Bactérias , Cianobactérias/enzimologia , Grupo dos Citocromos c/biossíntese , Genes Bacterianos , Grupo dos Citocromos c/metabolismo , Grupo dos Citocromos c/efeitos da radiação , Cinética , Luz , Oxirredução , Espectrofotometria Ultravioleta
8.
FEBS Lett ; 444(2-3): 281-4, 1999 Feb 12.
Artigo em Inglês | MEDLINE | ID: mdl-10050775

RESUMO

The cytM gene for cytochrome cM was previously found in Synechocystis sp. PCC 6803. Northern blotting analysis revealed that the cytM gene was scarcely expressed under normal growth conditions but its expression was enhanced when cells were exposed to low temperature or high-intensity light. By contrast, the expression of the genes for cytochrome c6 and plastocyanin was suppressed at low temperature or under high-intensity light. These observations suggest that plastocyanin and/or cytochrome c6, which are dominant under non-stressed conditions, are replaced by cytochrome cM under the stress conditions.


Assuntos
Proteínas de Bactérias , Cianobactérias/genética , Grupo dos Citocromos c/genética , Citocromos/genética , Regulação Bacteriana da Expressão Gênica/genética , Plastocianina/genética , Citocromos f , Genes Bacterianos/genética , Luz , RNA Mensageiro/metabolismo , Temperatura , Transcrição Gênica/genética
9.
Photochem Photobiol ; 65(4): 694-700, 1997 Apr.
Artigo em Inglês | MEDLINE | ID: mdl-9114746

RESUMO

The kinetics of the formation of biologically active psoralen photooxidation (POP) products were analyzed by the biological effects produced. Effects of the UV light fluence rate and psoralen concentration during the preirradiation were investigated to assess the yield of POP products, which were active in vivo (inducing suppression of delayed-type hypersensitivity [DTH] reaction to sheep red blood cells) and in vitro (altering the human erythrocyte membrane permeability). It was shown that the reciprocity law of the irradiation fluence rate and time was not valid in the case of POP-induced hemolysis and DTH suppression. Immunosuppressive POP products were more efficiently formed at low fluence rate (20.8 W/m2), whereas POP hemolysins were more efficiently produced at a high fluence rate (180 W/m2) of UV light. The yield of immunosuppressive POP products was enhanced in dilute psoralen solutions, while the POP hemolysins yield increased with increasing psoralen concentration. A kinetic scheme for psoralen photoproduct formation was proposed. Kinetic analysis showed that a labile intermediate was produced as the result of excitation of psoralen. This intermediate was either converted to a stable immunosuppressive POP product, or two intermediates combined to form a POP hemolysin. It is proposed that PUVA therapy conditions are more favorable for the formation of immunosuppressive rather than membrane-damaging psoralen photooxidation products.


Assuntos
Furocumarinas/efeitos adversos , Hemólise/efeitos dos fármacos , Hipersensibilidade Tardia/prevenção & controle , Animais , Proteínas Hemolisinas/biossíntese , Humanos , Hipersensibilidade Tardia/induzido quimicamente , Hipersensibilidade Tardia/metabolismo , Técnicas In Vitro , Masculino , Camundongos , Camundongos Endogâmicos C57BL , Camundongos Endogâmicos CBA , Oxirredução
10.
Biochim Biophys Acta ; 1273(2): 84-6, 1996 Feb 15.
Artigo em Inglês | MEDLINE | ID: mdl-8611593

RESUMO

The cyanobacterial coxD gene for heme O synthase was cloned from Synechocystis sp. PCC 6803 and its nucleotide sequence was determined. The deduced amino-acid sequence of the gene was homologous to the amino-acid sequences of bacterial heme O synthesis. In contrast to the genes for heme O synthases in other prokaryotes, which are clustered together with genes for the structural subunit(s) of cytochrome oxidase, the coxD gene is not linked to such genes on the chromosome of Synechocystis.


Assuntos
Cianobactérias/genética , Ferroquelatase/genética , Genes Bacterianos , Sequência de Aminoácidos , Sequência de Bases , Clonagem Molecular , Cianobactérias/metabolismo , Heme/metabolismo , Dados de Sequência Molecular , Alinhamento de Sequência
11.
Microbiology (Reading) ; 141 ( Pt 1): 163-9, 1995 Jan.
Artigo em Inglês | MEDLINE | ID: mdl-7894708

RESUMO

The murF gene encodes UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-meso-2, 6-diaminopimeloyl-D-Ala-D-Ala synthetase (EC 6.3.2.15), which catalyses the final step in the synthesis of UDP-N-acetylmuramoyl-pentapeptide, the precursor of murein. An open reading frame identified as the murF gene was found in the genome of the cyanobacterium Synechocystis sp. PCC 6803. The murF gene encodes a polypeptide of 454 amino acid residues with a predicted molecular mass of 48 kDa. The murF gene is present as a single-copy gene in the genome of Synechocystis sp. PCC 6803. The amino acid sequence deduced from the murF gene is 39% identical to that of the product of the murF gene of Escherichia coli. The cyanobacterial murF gene complemented a temperature-sensitive mutation in a murF-deficient strain of E. coli, restoring the mutant's ability to synthesize a cell wall and to survive at high sublethal temperatures.


Assuntos
Cianobactérias/enzimologia , Cianobactérias/genética , Genes Bacterianos , Peptídeo Sintases/genética , Sequência de Aminoácidos , Sequência de Bases , Clonagem Molecular , DNA Bacteriano/química , DNA Bacteriano/metabolismo , Escherichia coli/enzimologia , Escherichia coli/genética , Teste de Complementação Genética , Dados de Sequência Molecular , Mutagênese , Fases de Leitura Aberta , Peptídeo Sintases/biossíntese , Plasmídeos , Biossíntese de Proteínas , Proteínas Recombinantes/biossíntese , Proteínas Recombinantes/isolamento & purificação , Homologia de Sequência de Aminoácidos
12.
Plant Mol Biol ; 21(5): 913-8, 1993 Mar.
Artigo em Inglês | MEDLINE | ID: mdl-8467083

RESUMO

The rplI gene encoding the ribosomal protein L9 was found 4 kbp downstream from the desA gene, but on the opposite strand, in the genome of the cyanobacterium Synechocystis PCC6803. The deduced amino acid sequence is homologous to the sequences of the L9 proteins from Escherichia coli and chloroplasts of Arabidopsis and pea. The gene is present as a single copy in the chromosome and is transcribed as a mRNA of 0.64 kb. An open reading frame of unknown function (ORF291) was found in the upstream region of the rplI gene.


Assuntos
Cianobactérias/genética , Proteínas Ribossômicas/genética , Sequência de Aminoácidos , Sequência de Bases , Mapeamento Cromossômico , Clonagem Molecular , Escherichia coli , Dados de Sequência Molecular , Homologia de Sequência de Aminoácidos
SELEÇÃO DE REFERÊNCIAS
DETALHE DA PESQUISA