Transcriptome profiling of hippocampal CA1 after early-life seizure-induced preconditioning may elucidate new genetic therapies for epilepsy.

Injury of the CA1 subregion induced by a single injection of kainic acid (1 × KA) in juvenile animals (P20) is attenuated in animals with two prior sustained neonatal seizures on P6 and P9. To identify gene candidates involved in the spatially protective effects produced by early-life conditioning seizures we profiled and compared the transcriptomes of CA1 subregions from control, 1 × KA- and 3 × KA-treated animals. More genes were regulated following 3 × KA (9.6%) than after 1 × KA (7.1%). Following 1 × KA, genes supporting oxidative stress, growth, development, inflammation and neurotransmission were upregulated (e.g. Cacng1, Nadsyn1, Kcng1, Aven, S100a4, GFAP, Vim, Hrsp12 and Grik1). After 3 × KA, protective genes were differentially over-expressed [e.g. Cat, Gpx7, Gad1, Hspa12A, Foxn1, adenosine A1 receptor, Ca(2+) adaptor and homeostasis proteins, Cacnb4, Atp2b2, anti-apoptotic Bcl-2 gene members, intracellular trafficking protein, Grasp and suppressor of cytokine signaling (Socs3)]. Distinct anti-inflammatory interleukins (ILs) not observed in adult tissues [e.g. IL-6 transducer, IL-23 and IL-33 or their receptors (IL-F2 )] were also over-expressed. Several transcripts were validated by real-time polymerase chain reaction (QPCR) and immunohistochemistry. QPCR showed that casp 6 was increased after 1 × KA but reduced after 3 × KA; the pro-inflammatory gene Cox1 was either upregulated or unchanged after 1 × KA but reduced by ~70% after 3 × KA. Enhanced GFAP immunostaining following 1 × KA was selectively attenuated in the CA1 subregion after 3 × KA. The observed differential transcriptional responses may contribute to early-life seizure-induced pre-conditioning and neuroprotection by reducing glutamate receptor-mediated Ca(2+) permeability of the hippocampus and redirecting inflammatory and apoptotic pathways. These changes could lead to new genetic therapies for epilepsy.

Characteristics of chicken-seal salami.

Mechanically separated seal meat (MSSM) at 10% (SM-10) and 20% (SM-20) or seal protein hydrolysate (SPH) at 1% (SPH-1) and 2% (SPH-2) prepared from MSSM were used to replace mechanically separated chicken meat (MSCM) in salami formulations. Cured products containing 10 or 20% MSSM had a deeper red colour than those of the controls as noted by Hunter L and a values. Samples containing 20% MSSM had a softer texture as determined by sensory and Kramer shear-compression test studies, which was supported by scanning electron micrographs. All samples were equally acceptable as determined by sensory evaluation, except for SM-20 salamis which were less favoured.

[Renin secreting tumor and severe hypertension. Apropos of a new case]. / Tumeur à rénine et hypertension artérielle sévère. A propos d'un nouveau cas.

A renin-secreting tumour has been observed in a 32-year-old female with severe hypertension known for 17 years. The excision of the tumour lead to the complete normalisation of the blood pressure. Histological examination showed that the tumour was benign, contained secretion granules at different stages of maturation, and derived from the juxta-glomerular apparatus. After reviewing the 40 cases previously reported in the literature we discuss the clinical presentation of this type of tumour and the approach to their diagnosis.

Solubilization and purification of a membrane-associated 3,3',5-tri-iodo-L-thyronine-binding protein from rat erythrocytes.

3,3',5-Tri-iodo-L-thyronine (L-T3) binding sites from rat erythrocyte membranes were solubilized in an active form by using the zwitterionic detergent CHAPS or the anionic detergent lauroylsarcosine. The binding protein was successively purified by Sephadex G-200 and affinity chromatography. The purified material retained its binding activity and exhibited high affinity and specificity compared with those displayed in the original membrane. Yield was about 10% of the starting activity. The specific binding activity was enriched by approx. 100-fold, which represents a purity of only 0.1%. Analysis of the purified preparation on SDS/PAGE showed two major protein bands (Mr 64,000 and Mr 50,000), but these could not represent the binding protein since the purity obtained was low. However, affinity-labelling experiments with N-bromoacetyl-L-[125I]T3 in intact membranes showed that two proteins (also with Mr values of 64,000 and 50,000) bound the hormone specifically, suggesting a co-migration of hormone receptors and contaminants on gel electrophoresis.

High affinity L-triiodothyronine binding to right-side-out and inside-out vesicles from rat and human erythrocyte membrane.

3,5,3'-Triiodo-L-thyronine (L-T3)-binding sites from rat and human red cells were characterized as to their distribution between the two surfaces of the membrane. Analysis of L-T3 binding to sealed right-side-out and inside-out vesicles from erythrocyte membrane revealed that high affinity L-T3-binding sites are located on the external side in rat erythrocytes and on the internal side in human red cells. These results were further confirmed by preincubation of intact red cells with p-chloromercuribenzoate, a slowly permeant reagent that interacts reversibly with SH groups of proteins. Following this treatment only the SH groups of L-T3 sites from rat erythrocytes were found to be blocked. Scatchard analysis of the binding data for rat right-side-out and human inside-out vesicles showed high affinity sites with Kd values of 0.2 x 10(-10) and 2 x 10(-10) M, respectively. The results suggest that the orientation of L-T3-binding sites in the erythrocyte membrane is species-dependent.

Modification of L-triiodothyronine binding sites from rat erythrocyte membrane by heating and by proteinase treatments.

The number of binding sites for L-triiodothyronine in rat erythrocyte membranes was increased 2-fold by incubation at 37 degrees C for 60 min. An increase of approximately 3-fold was found when the incubation was carried out at 50 degrees C. The proteinase inhibitor phenylmethylsulfonyl fluoride abolished the effect. Similar increments in the number of binding sites were obtained by treatment of the membranes with proteinases. The Kd values (0.09 X 10(-10) M and 3.6 X 10(-10) M for the high-affinity and the low-affinity binding sites, respectively) remained unchanged after the treatment, as did the free-SH group requirements, storage stability and stereospecificity. Our results suggest that endogenous proteolytic activity could be involved in the increase of the number of membrane latent sites for L-triiodothyronine.

[Stenosis of the posterior cerebral artery (P1) discovered at the time of a meningeal hemorrhage and simulating an arterial aneurysm]. / Sténose de l'artère cérébrale postérieure (P1) découverte à l'occasion d'une hémorragie méningée et simulant un anévrysme artériel.

A case is reported, in which a patient 54 years old, was admitted after a SAH. The CT Scan (D1) demonstrated blood in the peri-peduncular cisterns. A first angiogram through femoral route was performed at D1. There was no vascular malformation on both carotid territories. An arterial ectasia was demonstrated on the basilar artery, arising at the origin of the left superior cerebellar artery. The left posterior cerebral artery was supplied only by the left carotid artery through a dilated posterior communicating artery. A second left vertebral angiogram was performed at D8, to make sure whether this ectasia was an aneurysm or a non aneurysmal dysplasia, but failed to provide certainty. The patient was operated upon at D17, with the diagnosis of possible aneurysm at the origin of the left superior cerebellar artery. Through a pterional route the posterior communicating artery was approached, no blood was found in the area of the upper basilar artery; there was an abnormal posterior circle of Willis, the superior cerebellar artery arising with a common trunk from the upper basilar artery; distal to this common trunk, the P1 segment was normal on the first three fourths of its course; the last fourth of the P1 segment was highly narrowed, the outer diameter of the narrowed P1 segment was approximately one third of the normal P1 segment, and was located at the junction with the complex posterior communicating artery-P2 segment. This narrowed part of the P1 segment showed evidence of an atheromatous plaque on its wall. No aneurysm was found in this area.(ABSTRACT TRUNCATED AT 250 WORDS)

Solubilization of L-triiodothyronine binding site from human erythrocyte membrane.

A thyroid binding peripheral membrane protein(s) has been characterized in human red cell. Two classes of affinity sites for triiodothyronine have been demonstrated. The high affinity, low capacity site showed values for dissociation constant of 2 X 10(-10)M. The binding activity depended on the presence of free -SH group and showed a high stereospecificity for L-triiodothyronine, L-thyroxine was less potent (about 1,000-fold) than L-triiodothyronine in competing for this site. The results are discussed with respect to their cellular significance.

High affinity L-triiodothyronine binding sites on washed rat erythrocyte membranes.

Two orders of saturable binding sites for L-triiodothyronine were found on washed rat erythrocyte membranes. The high affinity, low capacity site showed values of Kd 0.19 X 10(-10) M. This value was in the range of concentration of free L-triiodothyronine found in the plasma and was several orders of magnitude higher than the Kd values previously reported for other L-triiodothyronine membrane-binding systems. The binding site also showed a high stereospecificity for L-triiodothyronine. D-3,5,3'-triiodothyronine and L-thyroxine were less potent (about 1000-fold) than L-triiodothyronine in competing for these sites. L-3,3,5'-triiodothyronine and triiodothyroacetic acid were inactive. The physiological relevance of this site is considered.