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Biomedical subjects

F Penin

Publications and source records attributed to F Penin.

At least 55 records · Page 3Linked to original sources
PubMed1990

Blood activity of Cu/Zn superoxide dismutase, glutathione peroxidase and catalase in Alzheimer's disease: a case-control study.

Cu/Zn superoxide dismutase (Cu/Zn SOD), glutathione peroxidase (GPx) and catalase, which are the three main enzymes involved in cellular protection against damage due to oxygen-derived free radicals have been assayed in plasma and erythrocytes obtained from subjects with dementia of the Alzheimer type (DAT) and from controls. Blood samples were obtained from 25 patients with DAT and from age-matched subjects without diagnoses of neurological disease (non-DAT), as well as from younger individuals (reference group). Using appropriate statistical procedures, the three enzyme activities measured in blood of the elderly were decreased if compared to the younger reference group. Moreover, a significant increase in erythrocyte Cu/Zn SOD and catalase activities of DAT patients was observed compared to the non-DAT group. These results are discussed taking the free radical theory of aging into consideration.

Aged↗
PubMed1990

[Cerebrospinal fluid amino acids in Alzheimer's disease].

Twenty-two amino acids are measured in cerebrospinal fluid of fourty patients with senile dementia of the Alzheimer type (SDAT) and of ten age matched healthy control subjects. There is no significant difference between these two groups.

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PubMed1989

Lipid peroxidation and free radical scavengers in Alzheimer's disease.

Lipid peroxidation products and defenses against free radical damage were determined in serum of 55 patients with senile dementia of the Alzheimer type (SDAT) and compared with values in 24 age-matched healthy control subjects. The following parameters were evaluated: lipid-conjugated dienes and trienes, malondialdehyde, superoxide dismutase (SOD) and glutathione peroxidase (GSH-Px) activity in erythrocytes, vitamins E, C and A, zinc, selenium and copper, ceruloplasmin, transferrin and albumin. The results showed a statistically significant decrease in the levels of GSH-Px, vitamins E, C and A, zinc, transferrin and albumin in the SDAT group. On the other hand, most of the deficiencies concern the malnourished subgroup of the SDAT population (SOD, GSH-Px, vitamins E and C, selenium, zinc, transferrin and albumin). Such an alteration of free radical scavengers in the malnourished subgroup of the SDAT population could combine the radical and nutritional hypothesis advanced by some authors.

Aged↗
PubMed1988

Fate of nucleotides bound to reconstituted Fo-F1 during adenosine 5'-triphosphate synthesis activation or hydrolysis: role of protein inhibitor and hysteretic inhibition.

The protein ATPase inhibitor entraps about five nucleotides in pig heart mitochondrial F1, one at least being a triphosphate [Di Pietro, A., Penin, F., Julliard, J.H., Godinot, C., & Gautheron, D.C. (1988) Biochem. Biophys. Res. Commun. 152, 1319-1325]. The fate of these nucleotides was studied during ATP synthesis driven by NADH oxidation in reconstituted inverted submitochondrial particles. Iodinated F1, containing 0.7 mol of endogenous nucleotides/mol, was first loaded with tritiated adenine nucleotides in the presence or absence of the protein inhibitor and then reassociated with F1-depleted submitochondrial particles (ASU particles) to reconstitute an efficient NADH-driven ATP synthesis. In the absence of the protein inhibitor, 1.7 mol of labeled nucleotides remained bound per mole of reassociated F1, 0.8-0.9 mol being rapidly exchangeable against medium ADP or ATP, as measured after rapid filtration through nitrocellulose filters. In the presence of the protein inhibitor, as many as 3.25 mol of labeled nucleotides remained bound per mole of reassociated F1. Under hydrolysis conditions where ATPase activity was highly inhibited, no release of tritiated nucleotide occurred. In contrast, under ATP synthesis conditions where the protonmotive force was generated by NADH oxidation, the progressive reversal of inhibition by the protein inhibitor was correlated to a concomitant release of tritiated nucleotide. When ATP synthesis became fully active, about one nucleotide was completely exchanged whereas more than three nucleotides remained tightly bound and did not appear to be directly involved in ATP synthesis.(ABSTRACT TRUNCATED AT 250 WORDS)

Adenosine Diphosphate↗
PubMed1988

IF1 inhibition of mitochondrial F1-ATPase is correlated to entrapment of four adenine- or guanine-nucleotides including at least one triphosphate.

This paper demonstrates that the inhibition of F1 ATPase activity by the natural inhibitor protein IF1 is correlated to triphosphate nucleotide entrapment in F1. The complete balance of nucleotides bound after preincubation with Mg-[alpha-32P]GTP or Mg-[alpha-32P]ATP, used to promote IF1 inhibition, has been established on purified F1 containing 0.7 mol of non-exchangeable endogenous nucleotides. As many as 4 mol of labelled guanine- or adenine- nucleotides are trapped in F1; at least one of these nucleotides is a triphosphate. On the contrary, in the absence of IF1, no triphosphate nucleotide is significantly retained and the diphosphate nucleotides bound are mainly exchangeable.

Adenine Nucleotides↗
PubMed1986

Efficient reconstitution of mitochondrial energy-transfer reactions from depleted membranes and F1-ATPase as a function of the amount of bound oligomycin sensitivity-conferring protein (OSCP).

Pig heart mitochondrial membranes depleted of F1 and OSCP by various treatments were analyzed for their content in alpha and beta subunits of F1 and in OSCP using monoclonal antibodies. Membrane treatments and conditions of rebinding of F1 and OSCP were optimized to reconstitute efficient NADH- and ATP-dependent proton fluxes, ATP synthesis and oligomycin-sensitive ATPase activity. F1 and OSCP can be rebound independently to depleted membranes but to avoid unspecific binding of F1 to depleted membranes (ASUA) which is not efficient for ATP synthesis, F1 must be rebound before the addition of OSCP. The rebinding of OSCP to depleted membranes reconstituted with F1 inhibits the ATPase activity of rebound F1, while it restores the ATP-driven proton flux measured by the quenching of ACMA fluorescence. The rebinding of OSCP also renders the ATPase activity of bound F1 sensitive to uncouplers. The rebinding of OSCP alone or F1 alone, does not modify the NADH-dependent proton flux, while the rebinding of both F1 and OSCP controls this flux, inducing an inhibition of the rate of NADH oxidation. Similarly, oligomycin, which seals the F0 channel even in the absence of F1 and OSCP, inhibits the rate of NADH oxidation. OSCP is required to adjust the fitting of F1 to F0 for a correct channelling of protons efficient for ATP synthesis. All reconstituted energy-transfer reactions reach their optimal value for the same amount of OSCP. This amount is consistent with a stoichiometry of two OSCP per F1 in the F0-F1 complex.

Adenosine Triphosphatases↗
PubMed1985

Stoichiometry of the oligomycin-sensitivity-conferring protein (OSCP) in the mitochondrial F0F1-ATPase determined by an immunoelectrotransfer blot technique.

The ratio between the amount of oligomycin-sensitivity-conferring protein (OSCP) and the amount of the alpha and beta subunits of F1-ATPase in the mitochondria has been determined by a method combining electrophoresis, electrotransfer and immunotitration with monoclonal antibodies. The peptides separated in SDS-polyacrylamide gel electrophoresis were blotted to nitrocellulose sheets by electrotransfer. The nitrocellulose sheets were incubated with 125I-labelled purified monoclonal antibodies specific to various peptides. The 125I-labelled immune complexes were located by immunodecoration using peroxidase-conjugated second antibodies and the blotted peptides were revealed with H2O2 and alpha-naphthol. The amount of immune complex present on the nitrocellulose was determined by counting the radioactivity present on the spots. The amount of peptide blotted is directly proportional to the amount of protein loaded on the electrophoresis. By comparing standard curves made with the isolated proteins to the values obtained in the presence of various amounts of the membrane-protein complex, one can calculate the content of this peptide in the membrane. It was found that the mitochondrial membrane contains 2 mol of OSCP per mol of F1.

Adenosine Triphosphatases↗
PubMed1984

Two-dimensional gel electrophoresis of membrane proteins using anionic and cationic detergents. Application to the study of mitochondrial F0-F1-ATPase.

Polyacrylamide gel electrophoresis in the presence of a cationic detergent, tetradecyltrimethylammonium bromide (TDAB) has been compared to electrophoresis in the presence of an anionic detergent, sodium dodecyl sulfate (SDS). Although, in both systems, the peptides generally migrated as a function of their molecular weight, the TDAB electrophoresis permitted us to obtain a much better resolution of several peptides of the mitochondrial F0-F1-ATPase, especially for the alpha and beta subunits and for the oligomycin sensitivity conferring protein (OSCP). The differences between the two electrophoretic profiles have been used to devise a new technique of two-dimensional electrophoresis using successively anionic and cationic detergents. This method could be very useful in the case of membrane proteins, which are generally soluble only in the presence of powerful ionic detergents. It has been particularly successful in resolving the small peptides of the F0-F1-ATPase which were difficult to differentiate by other techniques in one- or two-dimensional polyacrylamide gel electrophoresis.

Adenosine Triphosphatases↗
PubMed1984

[Aortic dissection and Horton's disease. 2 cases].

The authors report two cases of temporal arteritis complicated with dissecting aneurysm of the aorta. The first one is discovered on systematical physical examination, the second is revealed by a thoracic pain. Clinical course is favourable under steroid therapy in both cases. Eleven cases of such complication with pathological control are reported in literature. Physiopathological mechanisms are discussed and active inflammatory involvement of aortic wall seem to be the main cause.

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PubMed1983

Correlations between ATP hydrolysis, ATP synthesis, generation and utilization of delta pH in mitochondrial ATPase-ATP synthase.

Using fluorescence quenching of 9-amino-6-chloro-2- methoxyacridine induced either by ATP hydrolysis in the ATPase-ATP synthase complex or by succinate oxidation in inverted submitochondrial particles, correlation have been established between ATP hydrolysis, ATP synthesis and the generation and utilization of delta pH. The results obtained are best explained in terms of local circuits of protons.

ATP Synthetase Complexes↗
PubMed1983

[The future of the aged patient at the end of an acute disease].

Elderly patients play an important role in the inpatient structure of departments of Internal Medicine. Although they pose many difficult problems during their admission due to multiple system disease, the problems often increase at the end of the therapeutic period when discharge from hospital is decided upon. Over half the cases are able to be sent home but the liaison with the domiciliary services is often poor, leading to reiterative hospital admission. A period in a medium-stay unit may provide a solution, but, due to insufficient numbers and uneven distribution, their function does not always meet the required demand: rehabilitation of the patient to his previous life style. Long-stay departments may be justified when there is a loss of autonomy and when regular medical care is needed. The exact place of these medicalised long-stay units within the hospital structure is still a matter of heated argument. What must be avoided is the creation of circuits of transfer of patients from one establishment to another. The present situation could be improved upon by the development of pre-hospital services, a better appreciation of the functional needs of the individual during hospitalisation, and a better liaison between the hospital and domiciliary services, by the creation of a range of options which do not favourise one or the other solution in too theoretical a manner.

Acute Disease↗
PubMed1982

Vesicular preparation of a highly coupled ATPase-ATP synthase complex from pig heart mitochondria.

1. A method is described to prepare an ATPase-ATP synthase complex from pig heart mitochondria exhibiting a very high ATP-32Pi exchange activity (1.6 mumol/min per mag protein in optimal conditions). 2. The preparation is virtually devoid of nucleoside diphosphokinase and adenylate kinase activities. 3. Freeze-fracture studies show that the ATPase-ATP synthase complex is integrated in lipid vesicles of 400-600 A in diameter. 4. It contains the endogenous natural proteic inhibitor which seems to behave as a coupling factor. 5. The rate of ATP hydrolysis catalyzed by the ATPase-ATP synthase complex is competitively inhibited by ADP, while the presence of ADP increases the initial rate of 32Pi incorporation into ATP. 6. The 32Pi incorporation into ATP can occur at a rate almost equal to that of nucleoside triphosphate (NTP) hydrolysis provided that the rate of NTP hydrolysis is kept low and that the ADP concentration is high enough. In these conditions, a very high coupling between NTP hydrolysis and ATP synthesis can be demonstrated.

ATP Synthetase Complexes↗