Bilateral hydrosalpinx in a mare - a case report

During a research visit for tissue collection at an abattoir located in Pelotas, Brazil, one female genital tract showed both enlarged oviducts. The reproductive tract was collected and analyzed. Occluded uterine tubes and an increase in the organ volume due to the large amount of fluid in the organ lumen were the macroscopic findings. Three samples, corresponding to isthmus, ampulla and infundibulum from each uterine tube and one sample from the endometrium were collected. Samples were fixed in Bouin's solution and processed in light microscopy. Microscopically a decrease in the number of folds and also an increase in the lumen of the organ were observed, mainly in the ampulla and infundibulum. The epithelial lining of the uterine tubes ranged from ciliated to simple squamous. Inflammatory cells were observed between the epithelial cells and in the lamina propria. Hydrosalpinx is difficult to diagnose and can be a cause of infertility in the mare

etramps, a New Plasmodium falciparum Gene Family Coding for Developmentally Regulated and Highly Charged Membrane Proteins Located at the Parasite–Host Cell Interface

After invasion of erythrocytes, the human malaria parasite Plasmodium falciparum resides within a parasitophorous vacuole and develops from morphologically and metabolically distinct ring to trophozoite stages. During these developmental phases, major structural changes occur within the erythrocyte, but neither the molecular events governing this development nor the molecular composition of the parasitophorous vacuole membrane (PVM) is well known. Herein, we describe a new family of highly cationic proteins from P. falciparum termed early transcribed membrane proteins (ETRAMPs). Thirteen members were identified sharing a conserved structure, of which six were found only during ring stages as judged from Northern and Western analysis. Other members showed different stage-specific expression patterns. Furthermore, ETRAMPs were associated with the membrane fractions in Western blots, and colocalization and selective permeabilization studies demonstrated that ETRAMPs were located in the PVM. This was confirmed by immunoelectron microscopy where the PVM and tubovesicular extensions of the PVM were labeled. Early expressed ETRAMPs clearly defined separate PVM domains compared with the negatively charged integral PVM protein EXP-1, suggesting functionally different domains in the PVM with an oppositely charged surface coat. We also show that the dynamic change of ETRAMP composition in the PVM coincides with the morphological changes during development. The P. falciparum PVM is an important structure for parasite survival, and its analysis might provide better understanding of the requirements of intracellular parasites