RÉSUMÉ
In the current literature, two distinct and opposite models are suggested to explain the consciousness disorders in schizophrenia. The first one suggests that consciousness disorders rely on a low-level processing deficit, when the second model suggests that consciousness disorders rely on disruption in the ability to consciously access information, with preserved unconscious processing. The current study aims to understand the mechanisms associated with visual consciousness disorder in order to pave the road that will settle the debate regarding these hypotheses. During a functional magnetic resonance imaging session, 19 healthy participants (HC) and 15 patients with schizophrenia (SCZ) performed a visual detection task to compare the neural substrates associated with the conscious access to the visual inputs. The visual detection threshold was significantly higher in SCZ than in HC [t(32) = 3.37, p = 0.002]. Whole-brain ANOVA demonstrated that around the visual detection threshold patients with SCZ failed to activate a large network of brain areas compared to HC. (1) During conscious vision, HC engaged more the left cuneus and the right occipital cortex than patients with SCZ, (2) during unconscious vision, HC engaged a large network that patients with SCZ failed to activate, and finally, (3) during the access to consciousness process, patients with SCZ failed to activate the anterior cingulate cortex. These results suggest that the consciousness disorders in schizophrenia rely on specific dysfunctions depending on the consciousness stage. The disorders of the conscious vision are associated with dysfunction of occipital areas while the ones associated with unconscious vision rely on a large widespread network. Finally, the conscious access to the visual inputs is impaired by a dysfunction of the anterior cingulate cortex. The current study suggests that none of the two suggested models can explain consciousness disorders in schizophrenia. We suggest that there is an alternative model supporting that the conscious access to visual inputs is due to a disengagement of the supragenual anterior cingulate during the unconscious processing of the visual inputs associated with a sensory deficit.
Sujet(s)
Conscience , Schizophrénie , Troubles de la conscience/imagerie diagnostique , Troubles de la conscience/étiologie , Humains , Imagerie par résonance magnétique , Schizophrénie/complications , Schizophrénie/imagerie diagnostique , Perception visuelleRÉSUMÉ
Paradigms of Latent Inhibition (LI) are inter-species and derived from learning theories. They are considered as tools which allow the attentional processes to be studied. The absence of LI is interpreted as difficulty in discriminating relevant and irrelevant stimuli. Abolition of LI has been shown in acute schizophrenics. The objectives of our study were partly to validate an LI paradigm, based on a contingency detection between two stimuli, in healthy subjects, and partly to analyse LI in schizophrenics. The study included 105 subjects (65 patients and 40 controls). Patients fulfilled the DSM IV diagnosis of schizophrenia. 35 in the acute phase and 30 in the chronic phase. We observed a loss of LI for acute schizophrenics, and an enhancement of LI for chronic schizophrenics. The variations in LI are interpreted from the perspective of a disturbance in the attentional processes. The LI status in acute schizophrenics appears to correlate with the clinical criteria with a prognostic value (low intensity of the negative dimension, late age at the first hospitalization). Moreover, the enhancement of LI correlates with the negative dimension of schizophrenic disease. This correlation is found in acute and chronic schizophrenics. It suggests that the variations of LI may be an indicator of adaptive strategies to a cognitive dysfunction specific to schizophrenia.
Sujet(s)
Inhibition psychologique , Psychologie des schizophrènes , Adulte , Analyse de variance , Femelle , Humains , Mâle , Tests neuropsychologiques , Analyse et exécution des tâchesRÉSUMÉ
The gene aspS encoding an aspartyl protease has been cloned from Sclerotinia sclerotiorum by screening a genomic library with a PCR-amplified fragment of the gene. The open reading frame of 1368 bp interrupted by one intron would encode a preproprotein of 435 amino acids. The catalytic aspartyl residues characteristic of aspartyl proteases are conserved; however, the active-site motif (DSG) in the N-terminal lobe is unusual in that Ser replaced Thr used in the active-site motif (DTG) of the C-terminal lobe and in all other fungal aspartyl proteases. RT-PCR revealed that aspS expression in axenic culture is not subjected to catabolite repression and demonstrated that aspS is expressed from the beginning of infection of sunflower cotyledons.
Sujet(s)
Ascomycota/enzymologie , Ascomycota/pathogénicité , Aspartic acid endopeptidases/génétique , Aspartic acid endopeptidases/métabolisme , Helianthus/microbiologie , Séquence d'acides aminés , Ascomycota/génétique , Ascomycota/croissance et développement , Aspartic acid endopeptidases/composition chimique , Séquence nucléotidique , Milieux de culture , Protéines fongiques , Régulation de l'expression des gènes fongiques , Données de séquences moléculaires , Maladies des plantes/microbiologie , Analyse de séquence d'ADN , VirulenceSujet(s)
Troubles anxieux , Schizophrénie/complications , Adulte , Troubles anxieux/complications , Troubles anxieux/diagnostic , Troubles anxieux/épidémiologie , Troubles anxieux/psychologie , Comorbidité , Femelle , Humains , Mâle , Surveillance de la population , Échelles d'évaluation en psychiatrie , Schizophrénie/épidémiologieRÉSUMÉ
A cDNA fragment encoding the A catalytic domain of the Neocallimastix frontalis endoxylanase XYN3 was amplified and cloned by the polymerase chain reaction technique. The xyn3A DNA fragment was inserted between the Saccharomyces cerevisiae phosphoglycerate kinase gene promoter and terminator sequences on a multicopy episomal plasmid for Kluyveromyces lactis. The XYN3A domain was successfully expressed in K. lactis and functional endoxylanase was secreted by the yeast cells with the K. lactis killer toxin secretion signal. The XYN3A domain was also expressed in a strain of Penicillium roqueforti as a fusion protein (ShBLE::XYN3A) of the phleomycin-resistance gene product and the endoxylanase. Active endoxylanase was efficiently secreted from the fungal cells with the Trichoderma viride cellobiohydrolase (CBH1) secretion signal and processed by a related KEX2 endoprotease of the secretion pathway. Several differently glycosylated forms of the recombinant enzymes were secreted by the yeast and the filamentous fungus.
Sujet(s)
Gènes fongiques , Kluyveromyces/génétique , Neocallimastix/génétique , Penicillium/génétique , Protéines recombinantes/biosynthèse , Xylosidases/biosynthèse , Séquence d'acides aminés , Séquence nucléotidique , Domaine catalytique/génétique , Endo-1,4-beta xylanases , Données de séquences moléculaires , Neocallimastix/enzymologie , Fragments peptidiques/biosynthèse , Fragments peptidiques/génétique , Phosphoglycerate kinase/génétique , Régions promotrices (génétique) , Régions terminatrices (génétique) , Trichoderma/génétique , Xylosidases/génétiqueRÉSUMÉ
Agitation is one of the diagnostic features of catatonia in the DSM IV classification, but permanent forms of agitated catatonia have occasionally been described. We report the case of a 43-year-old man who had already suffered from undifferentiated schizophrenia for 7 years, and in whom we diagnosed agitated catatonia. While our patient was being treated with a neuroleptic during a second episode of paranoia, a state of agitation was observed which persisted for a further 8 months. During this period, he was treated with several different neuroleptics and benzodiazepines, either alone or in association, without any improvement. No organic cause was found. He was then transferred to our electroconvulsive therapy (ECT) unit, with a diagnosis of schizophrenic agitation resistant to drug therapy. ECT was begun, and he was only given droperidol in case of agitation and alimemazine for insomnia, neither of which had any effect. In view of his persistent agitation without any purpose, echolalia and echopraxia, stereotyped movements with mannerisms and marked mimicking and grimacing, we diagnosed him as having agitated catatonia. After the fourth session of ECT, we decided to stop all treatment and gave him lorazepam at a dose of 12.5 mg daily. Twenty-four hours later, all symptoms of agitation had disappeared. In our opinion, permanent catatonic agitation is not rare. In our case, the neuroleptic treatment maintained and may even have worsened the symptomatology. Lorazepam can be used as a therapeutic test for this type of agitation, especially if it does not respond to neuroleptics. This also allows the patient to be sedated rapidly and effectively, thus preventing him from injuring himself further.
Sujet(s)
Catatonie/psychologie , Agitation psychomotrice/psychologie , Adulte , Catatonie/traitement médicamenteux , Électroconvulsivothérapie , Humains , Mâle , Échelles d'évaluation en psychiatrie , Agitation psychomotrice/traitement médicamenteux , Schizophrénie/complications , Psychologie des schizophrènesRÉSUMÉ
BACKGROUND: Neuroleptic malignant syndrome (NMS) is a potentially lethal adverse effect to neuroleptic drugs. METHODS: We report on 2 cases where NMS dramatically improved with carbamazepine. Incidental removal and reapplication of carbamazepine attests to its effectiveness for this condition. RESULTS: A 34-year-old woman treated for a major depressive disorder experienced NMS with a phenothiazine. Her condition dramatically improved in 8 hours after she was administered carbamazepine. Since carbamazepine was discontinued, NMS recurred in 10 hours and remitted anew within less than 24 hours after reintroduction. A 31-year-old woman experiencing a schizoaffective disorder displayed NMS with aphenothiazine and a butyrophenone. NMS completely resolved within 8 hours after she was administered carbamazepine. NMS recurred within 12 hours after carbamazepine discontinuation. CONCLUSIONS: These data thus account for a cause-effect relationship between carbamazepine administration and NMS relief, and argue against the neuroleptic withdrawal to be responsible by itself for NMS relief.
Sujet(s)
Anticonvulsivants/usage thérapeutique , Carbamazépine/usage thérapeutique , Syndrome malin des neuroleptiques/traitement médicamenteux , Adulte , Neuroleptiques/effets indésirables , Neuroleptiques/usage thérapeutique , Trouble dépressif/complications , Trouble dépressif/traitement médicamenteux , Femelle , Halopéridol/effets indésirables , Halopéridol/usage thérapeutique , Humains , Phénothiazines/effets indésirables , Phénothiazines/usage thérapeutiqueSujet(s)
Catatonie/diagnostic , Hypnotiques et sédatifs , Pyridines , Administration par voie orale , Adulte , Alprazolam/usage thérapeutique , Catatonie/sang , Catatonie/traitement médicamenteux , Femelle , Humains , Hypnotiques et sédatifs/sang , Hypnotiques et sédatifs/usage thérapeutique , Pyridines/sang , Pyridines/usage thérapeutique , ZolpidemRÉSUMÉ
The rumen anaerobic fungus Neocallimastix frontalis was biolistically transformed using plasmids containing the bacterial beta-glucuronidase gene (GUS) fused to the promoter sequences of the enolase gene from N. frontalis. Multiple copies of the plasmids were precipitated onto tungsten particles and delivered into zoosporangia and a mycelial mat by a helium-driven biolistic device. Transformants were detected by histochemical assay for beta-glucuronidase. It was found that the enolase promoter sequences tested were responsible for the transient expression of the beta-glucuronidase gene. This is the first study presenting results on the transformation of an anaerobic fungus.
Sujet(s)
Champignons/génétique , Régulation de l'expression des gènes codant pour des enzymes , Régulation de l'expression des gènes fongiques , Glucuronidase/génétique , Transformation génétique , Anaérobiose , Animaux , Biolistique , Clonage moléculaire , ADN fongique/génétique , Électrophorèse sur gel d'agar , Gènes bactériens , Glucuronidase/métabolisme , Enolase/génétique , Plasmides , Réaction de polymérisation en chaîne , Régions promotrices (génétique) , Rumen/microbiologie , Spores fongiques/génétiqueRÉSUMÉ
Different cDNAs designated xyn3 and xyn4 were isolated from an expression library of the anaerobic rumen fungus Neocallimastix frontalis. Xyn3 was further characterized and was shown to contain a single open reading frame of 1821 bp coding for a protein, XYN3, of 607 amino acids (Mr 66 000). The predicted primary structure of XYN3 consisted of two large reiterated regions of 223 amino acids with a high degree of identity (88.3%). Each domain of XYN3, XYN3A and XYN3B, showed significant homology with fungal and bacterial xylanases belonging to the endoxylanase family 11. XYN3 and XYN3A were cloned in a bacterial expression plasmid harbouring a 6 His-C terminal tag and the recombinant proteins XYN3 and XYN3A were purified from Escherichia coli. The recombinant proteins had Mr of 66 800 and 34 000 respectively and hydrolysed xylan to xylo-oligosaccharides. Analysis of truncated forms of XYN3 confirmed that the full-length protein contained two catalytic domains displaying similar substrate specificity. Western-blot analysis using antiserum raised against XYN3A showed that the N. frontalis xylanase was not submitted to post-translational maturation. XYN3A antiserum recognized similar polypeptides in the culture medium of two other rumen fungi, Piromyces rhizinflata and Caecomyces communis.
Sujet(s)
Champignons/génétique , Famille multigénique , Xylosidases/génétique , Séquence d'acides aminés , Animaux , Clonage moléculaire , ADN complémentaire , ADN fongique , Endo-1,4-beta xylanases , Escherichia coli , Champignons/classification , Champignons/enzymologie , Génome fongique , Hydrolyse , Données de séquences moléculaires , Phylogenèse , ARN messager/génétique , Protéines recombinantes , Rumen/microbiologie , Similitude de séquences d'acides aminés , Ovis , Xylanes/métabolismeRÉSUMÉ
OBJECTIVE: To provide researchers with a description of the method of dealing with out-of-hospital cardiac arrests, and the results thereof, using the Utstein style. DESIGN: a series of out-of-hospital cardiac arrests between 1 October 1991 and 31 September 1992. SETTING: a French 'departement' (administrative subdivision). POPULATION: 570,000 inhabitants; area: 2600 km2; emergency medical system consisting of two levels of response: the Emergency and Resuscitation Mobile Unit and the Fire Service. PATIENTS: a sample of 380 patients found to have neither palpable pulse nor independent respiration. RESULTS: of the 234 (61%) patients in whom resuscitation was attempted, 41 (17%) were hospitalised and 12 (5%) discharged were still alive at 1 year follow-up. Of the patients who showed signs of cardiac arrest of cardiac aetiology, classified as having initial ventricular fibrillation (VF) rhythms: 62% of the cases (5/8) were alive at 1 year if the cardiac arrest occurred in the presence of emergency medical personnel; 6% of the cases (2/31) were alive at 1 year if the cardiac arrest occurred in the presence of non-specialised bystanders.
Sujet(s)
Réanimation cardiopulmonaire , Services des urgences médicales , Arrêt cardiaque/épidémiologie , Ambulances , Réanimation cardiopulmonaire/statistiques et données numériques , Femelle , Premiers secours , Études de suivi , France/épidémiologie , Arrêt cardiaque/thérapie , Humains , Mâle , Adulte d'âge moyen , Facteurs temps , Résultat thérapeutiqueRÉSUMÉ
A DNA clone containing a putative enolase gene was isolated from a genomic DNA library of the anaerobic fungus Neocallimastix frontalis. It was deduced from sequence comparisons that the enolase gene was interrupted by a large 331 bp intron. The enolase gene, termed enol, has an ORF of 1308 bp and encodes a predicted 436 amino acid protein. The deduced amino acid sequence shows high identity (71.5-71%) to those of enolases from the yeasts Saccharomyces cerevisiae and Candida albicans. The G+C content of the enolase coding sequence (43.8 mol%) is considerably higher than the G+C content of the intervening sequence (14.2 mol%) or the 5' and 3' non-translated flanking sequences (15.2 and 4.7 mol%, respectively). The codon usage of the N. frontalis enolase gene was very biased as has been found for the highly expressed genes of yeast and filamentous fungi. The gene has all the canonical features (polyadenylation signal, intron splicing boundaries) of genes isolated from aerobic filamentous fungi. Only one enolase gene could be detected in N. frontalis genomic DNA by Southern analysis with a homologous probe. RNA analysis detected a single enolase transcript of about 1.6 kb. When mycelium was grown on glucose, levels of enolase mRNA were markedly increased by comparison with enolase mRNA levels in mycelium grown on cellulose, suggesting that expression of the N. frontalis enolase gene was transcriptionally regulated by the carbon source.
Sujet(s)
Chytridiomycota/génétique , Protéines fongiques/génétique , Gènes fongiques , Introns , Enolase/génétique , Séquence nucléotidique , Chytridiomycota/enzymologie , Clonage moléculaire , Codon/génétique , Séquence consensus , ADN fongique/génétique , Régulation de l'expression des gènes fongiques/effets des médicaments et des substances chimiques , Glucose/pharmacologie , Données de séquences moléculaires , Cadres ouverts de lecture , ARN fongique/biosynthèse , ARN messager/biosynthèse , Alignement de séquences , Similitude de séquences d'acides aminés , Spécificité d'espèce , Levures/génétiqueRÉSUMÉ
The phytopathogenic fungus Sclerotinia sclerotiorum produces a number of extra-cellular pectin-degrading enzymes. We have cloned and determined the complete sequence of a gene (pg1) encoding an endopolygalacturonase (PG1). The coding region consists of a non-interrupted 1143-bp open reading frame. S. sclerotiorum pg1 was compared to other fungal PG-encoding genes. Basic transcription control sequences were identified in the 5' non-coding region. The deduced amino acid (aa) sequence (380 aa) of the enzyme is compared to seven fungal PG sequences and shows a high level of identity (41.5 to 59.8%). Predicted secondary structures were compared, revealing a similar protein organization most probably in antiparallel beta sheets. Hybridization analysis using a pg1 0.65-kb BamHI fragment as a probe allowed the identification of seven different recombinant phages from a genomic library. Analysis of the hybridizing restriction fragments suggests that PG-encoding genes are organized as a family.