Search PubMed⌕ Search

Biomedical subjects

E Glaser

Publications and source records attributed to E Glaser.

At least 55 records · Page 3Linked to original sources
PubMed1994

Short-coupled variant of torsade de pointes. A new electrocardiographic entity in the spectrum of idiopathic ventricular tachyarrhythmias.

BACKGROUND: Torsade de pointes is characterized not only by its particular ECG pattern but by its context of congenital or acquired long QT syndrome and the long coupling interval of the initial premature beat. METHODS AND RESULTS: We observed 14 patients aged 34.6 +/- 10 years (mean +/- SD) with no structural heart disease who presented with syncope related to a typical ECG aspect of torsade de pointes. However, there was no evidence of long QT syndrome, and the torsade had the unusual particularity of an extremely short coupling interval of the first beat or of the isolated premature beats (245 +/- 28 milliseconds). In 10 cases they deteriorated into ventricular fibrillation. Four patients had a familial history of sudden death. Only 2 patients had a tachyarrhythmia inducible by programmed stimulation. At Holter recordings the heart rate variability was globally and significantly depressed, the vagal limb of the autonomic nervous system being predominantly affected. During a mean follow-up of 7 years there were 5 deaths (4 sudden). Nine patients are alive, 3 with implanted defibrillators and 6 treated with verapamil alone. Unlike the other types of antiarrhythmic agents including beta-blockers and amiodarone, verapamil is in our experience the only drug apparently active on the arrhythmias; however, it does not prevent sudden death. CONCLUSIONS: The short-coupled variant of torsade de pointes should be identified because of their ECG pattern and the risk of sudden death in young adults with no structural heart disease.

Adult↗
PubMed1994

[Design of heterologous mitochondria: import of cattle cytochrome P-450SCC precursors in plant mitochondria].

It has been shown that pre-P-450scc of bovine adrenal cortex mitochondria synthesized in a rabbit reticulocyte lysate cell-free system, is translocated into isolated soybean cotyledon mitochondria, thereby taking the mature form size. This finding is suggestive of the occurrence of a specific receptor and maturase for pre-P-450scc in plant mitochondria. Thus, plant mitochondria can be used as recipients for the mammalian cholesterol hydroxylase system in an attempt to study the mechanism of its formation and preservation.

Adrenal Cortex↗
PubMed1993

[Torsades de pointes with short coupling interval].

The authors describe a ventricular arrhythmia observed in 14 patients between 1972 and 1991, and 9 cases in the literature. The patients were hospitalised for investigations of syncope related to torsades de pointes. They were characterised by the very short coupling interval to the initiating extrasystole (average: 245 ms), by the young age of the patients (average: 34.6 years) and by the absence of overt cardiac disease. The resting electrocardiogrammes were normal, especially ventricular repolarisation. Some recordings showed isolated ventricular extrasystoles with short coupling intervals. Quite often, a family history of sudden death was obtained. These episodes of ventricular arrhythmia may degenerate to ventricular fibrillation. Pharmacological and electrophysiological investigations did not show any consistent characteristic electrophysiological behaviour. Investigations of autonomic nervous system function showed a decrease in global sinus rhythm variability and an increased sympathetic over parasympathetic activity. The clinical outcome of these patients is unpredictable with present methods. From a therapeutic point of view, Class I antiarrhythmics, betablockers and amiodarone were ineffective. Verapamil showed an electrocardiographic improvement by increasing the coupling interval of the extrasystoles and decreasing or even suppressing some repetitive forms, but without preventing recurrences. The indications for an implantable automatic defibrillator should be considered in this group of patients. These patients have clinical and electrocardiographic abnormalities which are sufficiently coherent for them to constitute a new pathological entity which the authors suggest calling "torsades de pointes with a short coupling interval".

Defibrillators, Implantable↗
PubMed1992

Plant mitochondrial F0F1 ATP synthase. Identification of the individual subunits and properties of the purified spinach leaf mitochondrial ATP synthase.

Spinach leaf mitochondrial F0F1 ATPase has been purified and is shown to consist of twelve polypeptides. Five of the polypeptides constitute the F1 part of the enzyme. The remaining polypeptides, with molecular masses of 28 kDa, 23 kDa, 18.5 kDa, 15 kDa, 10.5 kDa, 9.5 kDa and 8.5 kDa, belong to the F0 part of the enzyme. This is the first report concerning identification of the subunits of the plant mitochondrial F0. The identification of the components is achieved on the basis of the N-terminal amino acid sequence analysis and Western blot technique using monospecific antibodies against proteins characterized in other sources. The 28-kDa protein crossreacts with antibodies against the subunit of bovine heart ATPase with N-terminal Pro-Val-Pro- which corresponds to subunit F0b of Escherichia coli F0F1. Sequence analysis of the N-terminal 32 amino acids of the 23-kDa protein reveals that this protein is similar to mammalian oligomycin-sensitivity-conferring protein and corresponds to the F1 delta subunit of the chloroplast and E. coli ATPases. The 18.5-kDa protein crossreacts with antibodies against subunit 6 of the beef heart F0 and its N-terminal sequence of 14 amino acids shows a high degree of sequence similarity to the conserved regions at N-terminus of the ATPase subunits 6 from different sources. ATPase subunit 6 corresponds to subunit F0a of the E. coli enzyme. The 15-kDa protein and the 10.5-kDa protein crossreact with antibodies against F6 and the endogenous ATPase inhibitor protein of beef heart F0F1-ATPase, respectively. The 9.5-kDa protein is an N,N'-dicyclohexylcarbodiimide-binding protein corresponding to subunit F0c of the E. coli enzyme. The 8.5-kDa protein is of unknown identity. The isolated spinach mitochondrial F0F1 ATPase catalyzes oligomycin-sensitive ATPase activity of 3.5 mumol.mg-1.min-1. The enzyme catalyzes also hydrolysis of GTP (7.5 mumol.mg-1.min-1) and ITP (4.4 mumol.mg-1.min-1). Hydrolysis of ATP was stimulated fivefold in the presence of amphiphilic detergents, however the hydrolysis of other nucleotides could not be stimulated by these agents. These results show that the plant mitochondrial F0F1 ATPase complex differs in composition from the other mitochondrial, chloroplast and bacterial ATPases. The enzyme is, however, more closely related to the yeast mitochondrial ATPase and to the animal mitochondrial ATPase than to the chloroplast enzyme. The plant mitochondrial enzyme, however, exhibits catalytic properties which are characteristic for the chloroplast enzyme.

Amino Acid Sequence↗
PubMed1992

Prompt diagnosis of 'acute groin' conditions in infants.

Urgent sonographic examination of the groin was performed in 58 patients under the age of two years. Accurate diagnosis was done in conditions such as: incarcerated inguinal hernia, twisted undescended testis, incarcerated ovary in inguinal hernia and others. Ultrasonography facilitated decision-making and differentiation between surgical and non-surgical conditions.

Abdomen, Acute↗
PubMed1991

Specificity of leaf mitochondrial and chloroplast processing systems for nuclear-encoded precursor proteins.

The specificity of the mitochondrial and chloroplast processing enzymes for the nuclear-encoded precursor proteins was investigated. Mitochondrial precursor proteins of the Nicotiana plumbaginifolia and the Neurospora crassa beta subunits of F1-ATPase and the Neurospora Rieske FeS precursor protein were processed to the correct mature size by matrix extracts isolated from spinach leaves, yeast, rat liver and beef heart. The mitochondrial extracts failed to process chloroplast precursor proteins of the stromal small subunit of ribulose 1,5-bisphosphate carboxylase and the thylakoid 33 kDa protein of the oxygen-evolving complex. Both mitochondrial F1 beta precursors were specifically processed by a soluble stromal extract from chloroplasts. However, no processing of the Rieske FeS precursor protein was observed under the same conditions with the chloroplast extract. The cleavage of the mitochondrial F1 beta precursors by the chloroplast extract was shown to be sensitive to the metal chelators EDTA and ortho-phenanthroline. The cleavage site of the mitochondrial F1 beta precursor by the chloroplast soluble extract appears to be located at the N-terminus.

Adenosine Triphosphatases↗
PubMed1990

F0F1-ATPase of plant mitochondria: isolation and polypeptide composition.

A simple and high yield purification procedure for the isolation of F0F1-ATPase from spinach leaf mitochondria has been developed. This is the first report concerning purification and composition of the plant mitochondrial F0F1-ATPase. The enzyme is selectively extracted from inner membrane vesicles with the zwitterionic detergent, 3-[(3-cholamidopropyl) dimethyl ammonio]-1- propane sulfonate (CHAPS). The purified enzyme exhibits a high oligomycin-sensitive ATPase activity (3,6 mumol.min-1.mg-1). SDS-PAGE of the purified F0F1-ATPase complex reveals protein bands of molecular masses of 54 kDa (F1 alpha,beta), 33 kDa (F1 gamma), 28 kDa, 23 kDa, 21 kDa (F1 delta), 18.5 kDa, 15 kDa, 10.5 kDa, 9.5 kDa (F1 epsilon) and 8.5 kDa. All polypeptides migrate as one complex in a polyacrylamide gradient gel under non-denaturing conditions in the presence of 0.1% Triton X-100. Five polypeptides could be identified as subunits of F1. Polypeptides of molecular masses 28 kDa, 23 kDa, 18.5 kDa, 15 kDa, 10.5 kDa, 9.5 kDa and 8.5 kDa constitute the F0 part of the complex. Our results show that polypeptide composition of the plant mitochondrial F0 differs from other eukaryotic F0 of yeast, mammals and chloroplasts.

Electrophoresis, Polyacrylamide Gel↗
PubMed1990

Evidence for an endogenous ATPase inhibitor protein in plant mitochondria. Purification and characterization.

An endogenous ATPase inhibitor protein has been identified and isolated for the first time from plant mitochondria. The inhibitor protein was isolated from potato (Solanum tuberosum) tuber mitochondria and purified to homogeneity. The isolated inhibitor is a heat-stable, trypsin-sensitive, basic protein, with a molecular mass approximately 8.3 kDa. Amino acid analysis reveals a high content of glutamic acid, lysine and arginine and the absence of proline; threonine and leucine. The interaction of the inhibitor with F1-ATPase requires the presence of Mg2(+)-ATP in the incubation medium. The ATPase activity of isolated F1 is inhibited to 50% in the presence of 14 micrograms inhibitor/mg F1. A stoichiometry of 1.3 mol inhibitor/mol F1 for complete inhibition can be calculated from this value. The potato ATPase inhibitor is also a potent inhibitor of the ATPase activity of the isolated yeast F1. The inhibitor resembles the ATPase inhibitors of yeast and mammalian mitochondria, and does not seem to be related to the inhibitory peptide, epsilon subunit, of chloroplast ATPase.

Adenosine Triphosphate↗
PubMed1990

Sorting of precursor proteins between isolated spinach leaf mitochondria and chloroplasts.

The precursors of the F1-ATPase beta-subunits from Nicotiana plumbaginifolia and Neurospora crassa were imported into isolated spinach (Spinacia oleracea L.) leaf mitochondria. Both F1 beta precursors were imported and processed to mature size products. No import of the mitochondrial precursor proteins into isolated intact spinach chloroplasts was seen. Moreover, the precursor of the 33 kDa protein of photosynthetic water-splitting enzyme was not imported into the leaf mitochondria. This study provides the first experimental report of in vitro import of precursor proteins into plant mitochondria isolated from photosynthetic tissue and enables studies of protein sorting between mitochondria and chloroplasts in a system which is homologous with respect to organelles. The results suggest a high organellar specificity in the plant cell for the cytoplasmically synthesized precursor proteins.

Biological Transport, Active↗
PubMed1988

On the presence of a nicotinamide nucleotide transhydrogenase in mitochondria from potato tuber.

Mitochondria isolated from potato (Solanum tuberosum L.) tuber were investigated for the presence of a nicotinamide nucleotide transhydrogenase activity. Submitochondrial particles derived from these mitochondria by sonication catalyzed a reduction of NAD(+) or 3-acetylpyridine-NAD(+) by NADPH, which showed a maximum of about 50 to 150 nanomoles/minute.milligram protein at pH 5 to 6. The K(m) values for 3-acetylpyridine-NAD(+) and NADPH were about 24 and 55 micromolar, respectively. Intact mitochondria showed a negligible activity in the absence of detergents. However, in the presence of detergents the specific activity approached about 30% of that seen with submitochondrial particles. The potato mitochondria transhydrogenase activity was sensitive to trypsin and phenylarsine oxide, both agents that are known to inhibit the mammalian transhydrogenase. Antibodies raised against rat liver transhydrogenase crossreacted with two peptides in potato tuber mitochondrial membranes with a molecular mass of 100 to 115 kilodaltons. The observed transhydrogenase activities may be due to an unspecific activity of dehydrogenases and/or to a genuine transhydrogenase. The activity contributions by NADH dehydrogenases and transhydrogenase to the total transhydrogenase activity were investigated by determining their relative sensitivities to trypsin. It is concluded that, at high or neutral pH, the observed transhydrogenase activity in potato tuber submitochondrial particles is due to the presence of a genuine and specific high molecular weight transhydrogenase. At low pH an unspecific reaction of an NADH dehydrogenase with NADPH contributes to the total trans-hydrogenase activity.

Journal Article↗
PubMed1988

Inhibition of the mitochondrial F1-ATPase by rose bengal mediated photooxidation. Interaction of the Fe2+ chelate of bathophenanthroline with the sensitizer.

Rose Bengal mediated photooxidation of mitochondrial F1-ATPase and its beta-subunit resulted in inactivation and loss of about 50 and 60% of their histidine residues, respectively. The beta-subunit was not cleaved upon photooxidation. Photooxidation of histidine probably results in changes in the conformational stability of F1-ATPase leading to its inactivation. The participation of singlet molecular oxygen during the photooxidation process is suggested by the selective loss of histidine residues, while other amino acids, also sensitive to singlet oxygen attack, were not affected. Photochemical damage of F1-ATPase was prevented by various phenanthroline compounds, the order of efficiency being bathophenanthroline-Fe chelate greater than bathophenanthroline greater than orthophenanthroline-Fe chelate greater than bathophenanthroline-sulfonate-Fe chelate. The prevention by bathophenanthroline-Fe chelate of photochemical damage is interpreted on the basis of its interaction with the photosensitizer, Rose Bengal, probably implying a chemical reaction which decreases the actual concentration of the sensitizer and, thereby, the extent of photoinactivation.

Amino Acids↗
PubMed1987

Cross-reconstitution of isolated F1-ATPase from potato tuber mitochondria with F1-depleted beef heart and yeast submitochondrial particles.

Cross-reconstitution of isolated potato mitochondrial F1-ATPase with F1-depleted beef heart and yeast submitochondrial particles is reported. Potato F1 binds to the heterologous membrane and confers oligomycin sensitivity on the ATPase activity of the reconstituted system. Binding of F1 is promoted by the presence of Mg2+ with the maximal stimulatory effect at 20 mM. Mg2+ increase the sensitivity to oligomycin of the reconstituted system consisting of potato F1 and yeast membranes, however, they do not influence oligomycin sensitivity of potato F1 and beef heart membranes.

Animals↗