BACKGROUND Ventriculo-pleural (VPL) shunts are used infrequently in the management of hydrocephalus. The main complication associated with these shunts is pleural effusion. CASE DESCRIPTION This is a 28 years old male with a history of congenital hydrocephalus in whom a VPL shunt was inserted. Two years later, he noticed a soft bulging in the surgical scar area of the chest, suggestive of fluid accumulation. In the next days, the scar opened up spontaneously exposing the distal catheter which extruded through the opening. Chest radiographs and CT scan showed an important pleural effusion on the same side. The VPL shunt was removed and a contralateral shunt was inserted. CONCLUSIONS To the authors' knowledge, spontaneous extrusion of the distal catheter of the VPL shunt has not been previously reported in the literature. Physicians treating patients with hydrocephalus must be aware of this potential complication when a VPL is inserted. OBJECTIVE Middle meningeal artery (MMA) embolization may be an effective means of inhibiting neovascularization of the subdural capsular membrane and preventing hematoma maintenance. We sought to better understand how the MMA may affect subdural hematoma physiology and how this process may be modified by embolization. METHODS A retrospective review was done. We studied 27 patients with 29 SDHs who underwent MMA embolization from July 2018 to May 2019. Eight of these patients had post-embolization DynaCT imaging and were included. RESULTS Average patient age was 75 years old. Baseline non-contrast head CT showed the presence of a hematoma membrane in all 8 patients.  https://www.selleckchem.com/products/AdipoRon.html  Post-embolization DynaCTs in all patients demonstrated enhancement of all four components (dura, capsular membrane, septations, and subdural hematoma fluid). All patients had a minimum 60-day imaging and clinical follow-up. There was an average 87% decrease in SDH volume at last follow-up compared to baseline. There was a significant difference between the average baseline and average last follow-up SDH volume (paired t-test, p less then 0.0001) in all patients. Average last follow-up scan was 89 days (range 61-122 days) from the date of procedure. No patient experienced post-embolization complications, subsequent SDH drainage, or mortality. CONCLUSIONS Our data lends support to the theory of contiguous vascular networks between the MMA and SDH membranes. Targeting these leaky vascular networks may remove the source of hematoma accumulation. This adds to the pathophysiological understanding of the disease and suggests potential insight into the mechanism of action of MMA embolization. Histidine-rich Glycoprotein (HRG) is the most abundant protein in mussel haemolymph plasma. In this study, we determined by qRT-PCR and FISH analysis the tissues involved in HRG synthesis in Mytilus galloprovincialis. The relative HRG mRNA abundance in haemocytes, digestive gland, gills, gonads, posterior adductor muscle, and mantle edge was evaluated. Immunofluorescence analysis of HRG protein distribution in the whole mussel body was performed by a specific antibody. Our data showed the highest gene expression level of HRG in the mantle edge. In particular the outer fold of the mantle edge was shown to be the site that produced the highest amount of the protein. These data indicate a possible role of this Ca2++-binding protein in shell growth. HRG was also found in many other tissues and cells in contact with the haemolymph. This may be related to the immuno-responsive role of this protein. The presence of HRG in tissues related to the feeding pathways and mucous production could indicate the potential significance of this protein into mucus associated antimicrobial action. Overall, the results demonstrate that numerous mussel tissues are involved in HRG production, some of which can release the protein into the haemolymph and others into the extrapallial fluid. These data indicate that extrapallial (EP) protein and HRG are the same protein. An annual cycle survey showed a maximum HRG mRNA as well HRG protein production in mussel tissues in summer, a season in which the animals show the greatest growth, but are more likely to be exposed to microbial pathogens. In any vertebrate group, tooth shape is known to fit with a biological function related to diet. However, little is known about the relationships between diet and tooth microstructure and composition in teleost fishes. In this work, we describe the external morphology, internal microstructure and elemental composition of the oral teeth of three representative species of the family Serrasalmidae having different feeding habits (herbivorous vs. omnivorous vs. carnivorous). We used backscattered-electron imaging and low vacuum environmental scanning electron microscope to compare the organization and mineralization of tooth layers as well as energy dispersive X-ray microanalysis and Raman microspectrometry to investigate the elemental composition, Ca/P ratio and mineralogy of the most superficial layers. Oral teeth of each serrasalmid species have the same internal organization based on five distinctive layers (i.e. pulp, dentine, inner enameloid, outer enameloid and cuticle) but the general tooth morphology is different according to diet. Microstructural and compositional variation of the cuticle and iron-enrichment of superficial layers were highlighted between herbivorous and carnivorous species. Iron is more concentrated in teeth of the herbivorous species where it is associated with a thicker cuticle explaining the more intense red-pigmentation of the cutting edges of oral teeth. The iron-enrichment is interpreted as a substitution of Ca by Fe in the hydroxyapatite. These traits are discussed in the light of the evolutionary history of the family. Further considerations and hypotheses about the formation and origin of the mineralized tooth layers and especially the iron-rich superficial layers in teleost fishes are suggested. The mutated nickase Nt.BspD6I E418A has been obtained by site-directed mutagenesis. The purified protein has been crystallized, and its spatial structure has been determined at 2.45 Å resolution. An analysis of the crystal structures of the wild-type and mutated nickase have shown that the elimination of a carboxyl group due to the E418A mutation initiates marked conformational changes in both the N-terminal recognition domain and the C-terminal catalytic domain of nickase and insignificantly affects its linker domain. This is supported by changes in the functional properties of mutated nickase an increase in the oligomerization capacity in the presence of a substrate, a reduction in the capacity to bind a substrate, and complete loss of catalytic activity.