s and the cytotoxic effects of atheromatous “gruel”. It is however worth highlighting that SR-AI inhibition, by chemical or immunological means, did not entirely block CPP uptake or CPP-induced pro-inflammatory cytokine expression. Indeed, in the study by Herrmann et al, CPP uptake was only reduced by,50% in macrophage derived from SR-AI/DCC-2618 chemical information IIdeficient mice. Thus other clearance pathways may play a role in CPP metabolism, particularly in disease states and when SRAI/II pathways become saturated. Clinical Significance In the context of uraemia, elevated CPP levels may represent a response to mineral stress, but may also directly contribute to the pathogenesis of vascular calcification. Inflammatory factors like TNF-a and IL-1b have been shown to induce the de-differentiation of contractile VSMC to a synthetic mineralizing phenotype, which is considered a key event in the development of arterial calcification. Chronic elevation of inflammatory cytokines has also been shown to drive skeletal osteolysis, potentially increasing the efflux of mineral from bone, theoretically, increasing the production of CPP. Thus the induction and elaboration of pro-inflammatory signals from macrophages that we have observed with high levels of CPP, in vitro, may be expected to exacerbate vascular calcification and bone demineralization. Whether failure to remove CPP from the circulation 15120495 leads to the initiation or seeding of vascular mineralization, or whether CPP at levels encountered in vivo can potentiate these effects, has yet to be demonstrated. Animal models are now needed to translate these findings to the in vivo situation, and to test ways in which to harness this data therapeutically. ~~ ~~ Bacterial cell division is essential to bacterial survival, and must be tightly controlled and regulated to ensure the successful generation of two identical daughter cells. This process involves the polymerization of a tubulin-like protein into a ring at midcell, which then acts as a scaffold for the recruitment of other cell division proteins. These proteins form a complex known as the divisome, which carries out the synthesis and subsequent splitting of the septal cell wall. The division process must be precisely spatially and temporally regulated to ensure the equal partitioning of DNA into the resulting daughter cells. The essential nature of cell division makes it an attractive target for novel antibiotic development, and several inhibitors of FtsZ are currently under development for this purpose. Many of the known divisome components have been identified via screens of genetic mutants in the model 
bacteria Escherichia coli and Bacillus subtilis. FtsZ, and many other members of the divisome complex, were identified from temperature sensitive mutations, which result in the formation of filaments at the non-permissive temperature. Several of these genes are conserved, to varying 11121575 degrees, and have subsequently been identified in a wide range of bacteria via gene homology. However, less is known about the regulation of cell division in time and space. Two well known spatial regulators of division site placement, are nucleoid occlusion and the Min system. Nucleoid occlusion prevents Z rings forming over the nucleoid or chromosome, while the Min system inhibits the assembly of Z-rings at the cell poles; as the replicated chromosomes segregate, nucleoid occlusion is relieved at midcell allowing formation of a Z ring at this site. But these proteins alone cannot so