Randomised Controlled Trial on Prophylaxis of Mastitis-Metritis-Agalactia Syndrome in Swine using Caulophyllum Logoplex and Lachesis Logoplex.

Background: Mastitis-metritis-agalactia (MMA) syndrome occurs in the first days post-partum and causes piglet losses mainly due to malnutrition. One possibility for prophylaxis of MMA is via homeopathy. In this veterinary study, the effectiveness of a prophylactic administration of homeopathic remedies for the prevention of the occurrence of MMA in swine was evaluated.

Microtubule dynamic instability controls podosome patterning in osteoclasts through EB1, cortactin, and Src.

In osteoclasts (OCs) podosomes are organized in a belt, a feature critical for bone resorption. Although microtubules (MTs) promote the formation and stability of the belt, the MT and/or podosome molecules that mediate the interaction of the two systems are not identified. Because the growing "plus" ends of MTs point toward the podosome belt, plus-end tracking proteins (+TIPs) might regulate podosome patterning.

Cell-specific TLR9 trafficking in primary APCs of transgenic TLR9-GFP mice.

Recognition of nucleic acids by TLR9 requires its trafficking from the endoplasmic reticulum to endolysosomal compartments and its subsequent proteolytic processing. Both processes depend on interactions of TLR9 with the polytopic endoplasmic reticulum-resident protein UNC93B1. To examine the intracellular behavior of TLR9 in primary APCs, we generated transgenic mice expressing a TLR9-GFP fusion.

Cortactin deficiency is associated with reduced neutrophil recruitment but increased vascular permeability in vivo.

Neutrophil extravasation and the regulation of vascular permeability require dynamic actin rearrangements in the endothelium. In this study, we analyzed in vivo whether these processes require the function of the actin nucleation-promoting factor cortactin. Basal vascular permeability for high molecular weight substances was enhanced in cortactin-deficient mice.

Microtubules as platforms for assaying actin polymerization in vivo.

The actin cytoskeleton is continuously remodeled through cycles of actin filament assembly and disassembly. Filaments are born through nucleation and shaped into supramolecular structures with various essential functions. These range from contractile and protrusive assemblies in muscle and non-muscle cells to actin filament comets propelling vesicles or pathogens through the cytosol.

Cortactin promotes migration and platelet-derived growth factor-induced actin reorganization by signaling to Rho-GTPases.

Dynamic actin rearrangements are initiated and maintained by actin filament nucleators, including the Arp2/3-complex. This protein assembly is activated in vitro by distinct nucleation-promoting factors such as Wiskott-Aldrich syndrome protein/Scar family proteins or cortactin, but the relative in vivo functions of each of them remain controversial. Here, we report the conditional genetic disruption of murine cortactin, implicated previously in dynamic actin reorganizations driving lamellipodium protrusion and endocytosis.