The authors thank Inovio Pharmaceuticals for supplying the electroporation equipment. This work was supported

by Cancer Research UK no. C1238/A3849 (Vittes, G. E. and Stevenson, F. K.) and Leukaemia and Lymphoma Research UK no. 08025 (Harden, E. L. and Rice, J.). Conflict of interest: The authors declare no financial or commercial conflict of interest. “
“Citation Wu M-H, Huang M-F, Chang F-M, Tsai S-J. Leptin on peritoneal macrophages of patients with endometriosis. Am J Reprod Immunol 2010; 63: 214–221 Problem  The expression of cyclooxygenase (COX)-2 is considered as a marker of macrophage activation and has been implicated in the development of endometriosis. Leptin is an immunomodulator, which may also affect the development

this website of endometriosis. However, how leptin contributes to these pathological processes has not been completely understood. The aim of this study was to investigate the effects of leptin on peritoneal macrophages and its relationship with endometriosis. Methods of study  Peritoneal fluid from 60 women of reproductive age was obtained while they underwent laparoscopy. Forty patients had endometriosis and 20 patients did not have endometriosis. The concentration of leptin in the peritoneal fluid and prostaglandin F2α levels was measured by ELISA, and the other protein expression using Western blot when peritoneal macrophages were stimulated with leptin. Results  Concentration selleck kinase inhibitor of leptin in peritoneal fluid was increased in patients with endometriosis compared with disease-free

normal control. Functional leptin receptor was ADAMTS5 present in peritoneal macrophages. Treatment of peritoneal macrophages with leptin induced COX-2 expression. Production of prostaglandin F2α by peritoneal macrophages was increased after leptin stimulation in women with endometriosis. Conclusion  Elevated concentration of leptin in peritoneal fluid may contribute to the pathological process of endometriosis through activation of peritoneal macrophages. “
“An emerging theme among vacuole-adapted bacterial pathogens is the ability to hijack ubiquitin machinery to modulate host cellular processes and secure pathogen survival. Mono- and polyubiquitination differentially dictate the subcellular localization, activity, and fate of protein substrates. Monoubiquitination directs membrane traffic from the plasma membrane to the endosome and has been shown to promote autophagy. Anaplasma phagocytophilum is an obligate intracellular bacterium that replicates within a host cell-derived vacuole that co-opts membrane traffic and numerous other host cell processes. Here, we show that monoubiquitinated proteins decorate the A. phagocytophilum-occupied vacuolar membrane (AVM) during infection of promyelocytic HL-60 cell, endothelial RF/6A cells, and to a lesser extent, embryonic tick ISE6 cells.