Comparación de la estructura y rendimientos ganaderos en sistemas de producción tradicional y ecológico de bovino en Extremadura. Comparison of the structure and livestock yields in traditional production systems and ecological bovine Extremadura

The paper analyzes the structure and performance of beef cattle farms in Extremadura: Conventional (n = 50), Organic with no sales of organic products (n = 37) and Organic farms with sales of organic products (n = 11). Regarding stocking rate levels, no significant differences were observed among groups. By contrast, significant differences among the three types of farms regarding racial structure (p <0.05). Similarly, significant differences were found (p <0.1) in relation to farm's area, cattle's reproductive management and performance. The study highlights the similarity between conventional and organic cattle production in Extremadura. This fact could allow a smooth transition of conventional farms to the organic production model

Gem Associates with Ezrin and Acts via the Rho-GAP Protein Gmip to Down-Regulate the Rho Pathway

Gem is a protein of the Ras superfamily that plays a role in regulating voltage-gated Ca(2+) channels and cytoskeletal reorganization. We now report that GTP-bound Gem interacts with the membrane–cytoskeleton linker protein Ezrin in its active state, and that Gem binds to active Ezrin in cells. The coexpression of Gem and Ezrin induces cell elongation accompanied by the disappearance of actin stress fibers and collapse of most focal adhesions. The same morphological effect is elicited when cells expressing Gem alone are stimulated with serum and requires the expression of ERM proteins. We show that endogenous Gem down-regulates the level of active RhoA and actin stress fibers. The effects of Gem downstream of Rho, i.e., ERM phosphorylation as well as disappearance of actin stress fibers and most focal adhesions, require the Rho-GAP partner of Gem, Gmip, a protein that is enriched in membranes under conditions in which Gem induced cell elongation. Our results suggest that Gem binds active Ezrin at the plasma membrane–cytoskeleton interface and acts via the Rho-GAP protein Gmip to down-regulate the processes dependent on the Rho pathway

c-Met recruits ICAM-1 as a coreceptor to compensate for the loss of CD44 in Cd44 null mice

CD44v6 acts as a coreceptor for the receptor tyrosine kinases c-Met and VEGFR-2. It is shown that ICAM-1 can act as a new coreceptor in CD44v6-negative tumor cells. Furthermore, ICAM-1 can substitute for CD44v6 as a coreceptor for c-Met in primary hepatocytes and in liver regeneration in Cd44 null mice

The postsynaptic density 95/disc-large/zona occludens protein syntenin directly interacts with frizzled 7 and supports noncanonical Wnt signaling.

Wnt signaling pathways are essential for embryonic patterning, and they are disturbed in a wide spectrum of diseases, including cancer. An unresolved question is how the different Wnt pathways are supported and regulated. We previously established that the postsynaptic density 95/disc-large/zona occludens (PDZ) protein syntenin binds to syndecans, Wnt coreceptors, and known stimulators of protein kinase C (PKC)alpha and CDC42 activity. Here, we show that syntenin also interacts with the C-terminal PDZ binding motif of several Frizzled Wnt receptors, without compromising the recruitment of Dishevelled, a key downstream Wnt-signaling component. Syntenin is coexpressed with cognate Frizzled during early development in Xenopus. Overexpression and down-regulation of syntenin disrupt convergent extension movements, supporting a role for syntenin in noncanonical Wnt signaling. Syntenin stimulates c-jun phosphorylation and modulates Frizzled 7 signaling, in particular the PKCalpha/CDC42 noncanonical Wnt signaling cascade. The syntenin-Frizzled 7 binding mode indicates syntenin can accommodate Frizzled 7-syndecan complexes. We propose that syntenin is a novel component of the Wnt signal transduction cascade and that it might function as a direct intracellular link between Frizzled and syndecans.Journal ArticleResearch Support, Non-U.S. Gov'tinfo:eu-repo/semantics/publishe