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1.
Chem Phys Lipids ; 51(1): 67-71, 1989 Jul.
Artigo em Inglês | MEDLINE | ID: mdl-2766437

RESUMO

The effect of glycosaminoglycans (GAG) and divalent cations on the thermal properties of dipalmitoyl-phosphatidylcholine (DPPC)-water systems was examined in order to model some interactions taking place on low density lipoprotein (LDL) surfaces. The thermal properties of these systems were measured by differential scanning calorimetry (DSC). According to the results, all three glycosaminoglycans used (chondroitin-4-sulfate, chondroitin-6-sulfate and heparin) were effective but to a different extent. Calcium ions enhance the interaction more than magnesium ions, probably because divalent cations form bridges between the negatively charged groups of GAGs and the headgroups of lipids. It is conceivable that similar processes might occur in the case of LDL.


Assuntos
1,2-Dipalmitoilfosfatidilcolina , Cloreto de Cálcio , Glicosaminoglicanos , Magnésio , Varredura Diferencial de Calorimetria , Cátions Bivalentes , Lipoproteínas LDL/metabolismo , Cloreto de Magnésio , Modelos Teóricos , Termodinâmica
2.
J Theor Biol ; 137(2): 203-14, 1989 Mar 21.
Artigo em Inglês | MEDLINE | ID: mdl-2601346

RESUMO

A statistical mechanical model with experimentally proved facts as starting points is presented. This model explains on molecular level, the pre- and subtransitions appearing in lipid membranes. The model describes the main features of the transitions, the hysteresis of the subtransition and the mobility changes of the heads and chains at these transitions. The model was expanded for phosphatidylcholine homologues with arbitrary chain lengths, and a qualitative agreement in the case of pretransition as far as a quantitative one for the subtransition were found.


Assuntos
Bicamadas Lipídicas , Fluidez de Membrana , Modelos Biológicos , Fosfatidilcolinas , Fenômenos Químicos , Físico-Química , Modelos Estatísticos , Temperatura , Termodinâmica
3.
Membr Biochem ; 8(1): 1-10, 1989.
Artigo em Inglês | MEDLINE | ID: mdl-2478862

RESUMO

In this paper the authors present a comparative study of the actions of the antibiotics primycin and gramicidin on the erythrocyte membrane permeability. It has been found that both antibiotics have a nonlinear effect on the membrane permeability. Above a threshold antibiotic concentration, which is characteristic of the type of the antibiotic, the cation permeability of the erythrocyte membranes increases sharply. In the range of nonlinearity the transport-kinetic curves level off before achieving the equilibrium radioactive ion distribution between the extra- and intracellular spaces. A stochastic model of the cooperative and aspecific incorporation of antibiotic molecules into the membrane explains the experimental findings. The authors conclude that membrane permeability increases at the places where two or more antibiotic molecules form aggregates in the membrane.


Assuntos
Antibacterianos/sangue , Cátions/sangue , Membrana Eritrocítica/metabolismo , Gramicidina/sangue , Macrolídeos , Transporte Biológico , Radioisótopos de Césio , Fenômenos Químicos , Química , Espaço Extracelular/metabolismo , Hematócrito , Humanos , Técnicas In Vitro , Cinética , Modelos Biológicos , Radioisótopos de Potássio , Radioisótopos de Rubídio
4.
Biochimie ; 71(1): 99-104, 1989 Jan.
Artigo em Inglês | MEDLINE | ID: mdl-2470422

RESUMO

Studies for the cation permeability properties of the gramicidin A channel in erythrocyte membranes are presented. It is shown that gramicidin A interacts with the membrane in a cooperative manner, creating aggregates of the antibiotic molecules in the lipid lattice of the membrane. Cationic channels exist in these aggregates with the following order of selectivity: Rb+ greater than Cs+ greater K+ greater than Na+. The cation permeability of the channels depends on the media surrounding the membrane. This finding has been explained on the basis of Hodgkin-Keynes theory for single-file ion diffusion through extra-narrow pores.


Assuntos
Membrana Eritrocítica/metabolismo , Gramicidina/metabolismo , Cátions , Permeabilidade da Membrana Celular , Canais Iônicos , Radioisótopos de Potássio , Radioisótopos de Rubídio , Radioisótopos de Sódio
5.
Acta Physiol Hung ; 70(1): 133-47, 1987.
Artigo em Inglês | MEDLINE | ID: mdl-3425328

RESUMO

Earlier the autophosphorylation of myosin and the labile phosphate (P) content of rabbit skeletal muscle was reported [6, 7, 9]. The present paper describes that the endogeneous preformed P level in fresh preparation of exercised muscle is higher than that of untrained control one. It was revealed that the presence of a significant amount of mitochondrial myosin (with much higher P content) in the well-trained human muscle preparations falsified the appreciation of myofibrillar myosin. Therefore, a reliable myofibrillar preparation with correct P content from exercised subjects was obtained only after the separation of mitochondrial fraction. The P content of fresh preparations can be increased by phosphorylation even in the exercised muscle myosins up to the most higher level in human samples. The phosphoryl group incorporation from [gamma-32P]ATP into the rabbit and hare myosins was checked by radioactive tracer technique, and confirmed by total P content determination performed parallel with molybdate test. It was stated that under present circumstances the labelled 32P incorporation was lower even at an optimal substrate concentration than that of P value obtained directly with molybdate method; because the total P content of preparations had not exchanged during 2 min incubation. So it has been concluded from [gamma-23P] phosphoryl group assayments that much higher amount of P was incorporated into P-Arg, N pi-P-His and fraction 2 as compared with unappreciated labelled P level of the inorganic P (P-Ser, P-Thr), P-Lys, N tau-P-His and minor fractions. From these observations it has been considered that the P-Arg, N pi-P-His and fraction 2 take part in the contraction mechanism and in the course of physical training.


Assuntos
Músculos/enzimologia , Miosinas/metabolismo , Trifosfato de Adenosina/metabolismo , Animais , Fosfatos/análise , Fosforilação , Coelhos
6.
Gen Physiol Biophys ; 5(6): 625-36, 1986 Dec.
Artigo em Inglês | MEDLINE | ID: mdl-2435616

RESUMO

Data are presented on the interaction of gramicidin, primycin and valinomycin with red blood cell membranes and compared with those obtained for artificial lipid bilayer membranes. The channel forming antibiotics gramicidin and primycin show specific kinetic behaviour in living cell membranes. It could be shown that the penetration of these antibiotics into the red blood cell membrane is a cooperative process resulting in the occurrence of aggregates in the lipid lattice of the membrane.


Assuntos
Antibacterianos/farmacologia , Membrana Eritrocítica/efeitos dos fármacos , Gramicidina/farmacologia , Macrolídeos , Valinomicina/farmacologia , Antibacterianos/metabolismo , Membrana Eritrocítica/metabolismo , Gramicidina/metabolismo , Humanos , Canais Iônicos/metabolismo , Cinética , Lactonas/metabolismo , Lactonas/farmacologia , Bicamadas Lipídicas , Modelos Biológicos , Valinomicina/metabolismo
7.
Acta Biochim Biophys Acad Sci Hung ; 19(3-4): 289-98, 1984.
Artigo em Inglês | MEDLINE | ID: mdl-6085854

RESUMO

A comparative study of the actions of antibiotics primycin and gramicidin on tracer exchange of red blood cells at steady state salt distribution was carried out. The equilibrium radioactive ion distribution was not achieved at definite concentrations of either antibiotics. A development of Adam's statistical mechanical model for cooperative transitions in membranes are presented to explain the results obtained.


Assuntos
Antibacterianos/farmacologia , Eritrócitos/metabolismo , Gramicidina/farmacologia , Macrolídeos , Transporte Biológico Ativo/efeitos dos fármacos , Cátions , Césio/sangue , Eritrócitos/efeitos dos fármacos , Humanos , Cinética , Lactonas/farmacologia , Matemática , Modelos Biológicos , Potássio/sangue , Rubídio/sangue
9.
Acta Biol Med Ger ; 40(4-5): 465-9, 1981.
Artigo em Inglês | MEDLINE | ID: mdl-7315092

RESUMO

The effects of the antibiotic primycin on alkali cation transport of human erythrocytes were investigated. Primycin selectively increases the permeability of erythrocytes to alkali-cations according to the sequence: Cs+ greater than Rb+ approximately K+ greater than Na+. The time course of the cation effluxes depends on the antibiotic concentration and can be altered by negatively charged SDS. Some evidence is given for the mechanism of primycin-membrane interaction.


Assuntos
Antibacterianos/farmacologia , Transporte Biológico Ativo/efeitos dos fármacos , Membrana Eritrocítica/metabolismo , Eritrócitos/metabolismo , Macrolídeos , Cátions Monovalentes , Permeabilidade da Membrana Celular/efeitos dos fármacos , Césio/sangue , Membrana Eritrocítica/efeitos dos fármacos , Humanos , Cinética , Lactonas/farmacologia , Potássio/sangue , Rubídio/sangue , Sódio/sangue , Dodecilsulfato de Sódio/farmacologia
10.
J Antibiot (Tokyo) ; 32(4): 408-13, 1979 Apr.
Artigo em Inglês | MEDLINE | ID: mdl-468726

RESUMO

The effects of primycin were investigated on the alkali-cation transport of human erythrocytes and on the electric conduction of bimolecular lipid membranes. In the concentration range of 3.10(-6) approximately 10(-5) M primycin increased the permeability of erythrocytes to alkali-cations according to the sequences Cs+ greater than Rb+ approximately K+ greater than Na+, while the conductance of the negatively charged phosphatidylserine bimolecular lipid membrane increased by 2 approximately 3 orders of magnitude. The resistance-lowering effect of primycin strongly depended on the cationic species applied and a selectivity order Na+ greater than K+ greater than Rb+ greater than Cs+ was found. A possible mechanism of the primycin-membrane interaction is suggested on the basis of experimental data.


Assuntos
Antibacterianos/farmacologia , Membrana Eritrocítica/metabolismo , Eritrócitos/metabolismo , Membranas Artificiais , Cátions/metabolismo , Permeabilidade da Membrana Celular/efeitos dos fármacos , Humanos , Técnicas In Vitro , Lactonas/farmacologia , Lipídeos , Fatores de Tempo
11.
Acta Med Acad Sci Hung ; 36(4): 381-94, 1979.
Artigo em Inglês | MEDLINE | ID: mdl-233400

RESUMO

The responses of serum concentrations of TSH, thyroxine (T4), triiodothyronine (T3) and of reverse triiodothyronine (rT3) to i. v. administration of 0.4 mg THR were examined prior to (and after) i. m. administration of ACTH (2 mg Synacthen Depot) in 7 euthyroid women using estrogen-containing oral contraceptives and in 8 controls, with the following results: (1) an increase in endogenous glucocorticoid secretion is associated with a depression of the TSH response to TRH; (2) TSH formed in decreased amounts is still capable of stimulating thyroid secretion; (3) the increased serum corticoid levels fail to affect the secretory response of the thyroid to TSH; (4) control of the pituitary-thyroid axis remains normal in the presence of increased serum thyroxine-binding globulin (TBG) levels. In a further series the serum levels of TBG, T4, T3, rT3 and cortisol under the effect of ACTH-induced endogenous glucocorticoid hypersecretion were studied in 6 normal untreated controls, in 6 normal women using oral contraceptives and in 10 untreated hyperthyroid patients. During four days subsequent to treatment the serum TBG levels decreased, maximum decrease being found in the users of oral contraceptives, minimum decrease in the controls. Serum T4 was found to decrease during 2 to 4 days, serum T3 parallel with an increase in serum rT3, for 1 to 2 days, subsequent for ACTH loading. In the euthyroid cases also the serum TSH levels showed a transitory decline. It is concluded that in case of endogenous hyperproduction of glucocorticoids (1) T4 leads to T3 monodeiodination decreases and T4 leads to rT3 conversion increases parallel with the changes in the serum cortisol levels; (2) TBG synthesis is inhibited by endogenous glucocorticoids; (3) the changes in serum TBG levels are accompanied by a decrease in the serum T4 concentrations.


Assuntos
Hormônio Adrenocorticotrópico/farmacologia , Hipertireoidismo/sangue , Hormônios Tireóideos/sangue , Hormônio Liberador de Tireotropina/farmacologia , Tireotropina/sangue , Proteínas de Ligação a Tiroxina/sangue , Adulto , Cosintropina/farmacologia , Feminino , Humanos , Hidrocortisona/sangue , Tiroxina/sangue , Tri-Iodotironina/sangue , Tri-Iodotironina Reversa/sangue , Zinco/farmacologia
15.
Acta Biochim Biophys Acad Sci Hung ; 10(1-2): 57-61, 1975.
Artigo em Inglês | MEDLINE | ID: mdl-1146493

RESUMO

The effect of alkali cations on the rate of citrate uptake of rat-liver mitochondria and on the citrate adsorption has been studied. In each set of results, as in a series of comparative respiratory studies, Cs+ is more stimulatory than the other ions. This effect might be the consequence of different electrostatic interactions between the membrane and ions in solution in the case of different cations.


Assuntos
Césio/farmacologia , Citratos/metabolismo , Lítio/farmacologia , Mitocôndrias Hepáticas/metabolismo , Potássio/farmacologia , Rubídio/farmacologia , Sódio/farmacologia , Animais , Cinética , Mitocôndrias Hepáticas/efeitos dos fármacos , Ratos , Temperatura , Fatores de Tempo
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