Anticonvulsant effects of aerial parts of Passiflora incarnata extract in mice: involvement of benzodiazepine and opioid receptors

<p>Abstract</p> <p>Background</p> <p>Passion flower (<it>Passiflora incarnata</it>) is used in traditional medicine of Europe and South America to treat anxiety, insomnia and seizure. Recently, it has shown antianxiety and sedative effects in human.</p> <p>Methods</p> <p>In this study, anticonvulsant effects of hydro- alcoholic extract of Passiflora, Pasipay, were examined by using pentylentetrazole model (PTZ) on mice. Pasipay, diazepam, and normal saline were injected intraperitoneally at the doses 0.4–0.05 mg/kg, 0.5–1 mg/kg and 10 ml/kg respectively 30 minutes before PTZ (90 mg/kg, i.p). The time taken before the onset of clonic convulsions, the duration of colonic convulsions, and the percentage of seizure and mortality protection were recorded. For investigating the mechanism of Pasipay, flumazenil (2 mg/kg, i.p) and naloxone (5 mg/kg, i.p) were also injected 5 minutes before Pasipay.</p> <p>Results</p> <p>An ED₅₀value of Pasipay in the PTZ model was 0.23 mg/kg (%95 CL: 0.156, 0.342). Pasipay at the dose of 0.4 mg/kg prolonged the onset time of seizure and decreased the duration of seizures compared to saline group (p < 0.001). At the dose of 0.4 mg/kg, seizure and mortality protection percent were 100%. Flumazenil and naloxone could suppress anticonvulsant effects of Pasipay.</p> <p>Conclusion</p> <p>It seems that Pasipay could be useful for treatment absence seizure and these effects may be related to effect of it on GABAergic and opioid systems. More studies are needed in order to investigate its exact mechanism.</p

Structure and non-structure of centrosomal proteins

Here we perform a large-scale study of the structural properties and the expression of proteins that constitute the human Centrosome. Centrosomal proteins tend to be larger than generic human proteins (control set), since their genes contain in average more exons (20.3 versus 14.6). They are rich in predicted disordered regions, which cover 57% of their length, compared to 39% in the general human proteome. They also contain several regions that are dually predicted to be disordered and coiled-coil at the same time: 55 proteins (15%) contain disordered and coiled-coil fragments that cover more than 20% of their length. Helices prevail over strands in regions homologous to known structures (47% predicted helical residues against 17% predicted as strands), and even more in the whole centrosomal proteome (52% against 7%), while for control human proteins 34.5% of the residues are predicted as helical and 12.8% are predicted as strands. This difference is mainly due to residues predicted as disordered and helical (30% in centrosomal and 9.4% in control proteins), which may correspond to alpha-helix forming molecular recognition features (α-MoRFs). We performed expression assays for 120 full-length centrosomal proteins and 72 domain constructs that we have predicted to be globular. These full-length proteins are often insoluble: Only 39 out of 120 expressed proteins (32%) and 19 out of 72 domains (26%) were soluble. We built or retrieved structural models for 277 out of 361 human proteins whose centrosomal localization has been experimentally verified. We could not find any suitable structural template with more than 20% sequence identity for 84 centrosomal proteins (23%), for which around 74% of the residues are predicted to be disordered or coiled-coils. The three-dimensional models that we built are available at http://ub.cbm.uam.es/centrosome/models/index.php

Agaritine content of 53 Agaricus species collected from nature

International audienceAbstract Fifty-three different species of the genus Agaricus were collected in the Czech Republic during the period 1998-2001 and identified by an experienced mycologist. The samples were analysed for agaritine (N2-(Γ-L-glutamyl)-4-hydroxymethylphenyl¬hydrazine) content, a precursor to a suspected rodent carcinogen. There was a huge variation in agaritine content between species, less variation between samples of a species. Whereas the cultivated mushroom Agaricus bisporus commonly contain 200-500 mg agaritine/kg fresh weight, no less than 24 of the 53 species contained agaritine levels above 1000 mg/kg fresh weight. The highest level was found in A. elvensis containing up to 10,000 mg/kg fresh weight. Seventeen species contained intermediate levels (125-1000 mg/kg), and twelve species below 125 mg/kg. Some of the species producing low levels of agaritine might be candidates for future strain-development of Agaricus mushrooms for cultivation. No correlation could be observed between the agaritine content and size of the mushroom, week of the year when collected, year of collection, or site of collection. Besides occurring in the genus Agaricus, some species of the genera Leucoagaricus and Macrolepiota were also shown to contain agaritine