Abstract. Segmental aplasia of the uterine body was diagnosed in a 5-year-old, mixed breed bitch. Abdominal radiography and transabdominal ultrasonography revealed marked dilation of fluid-filled uterine horns with no evidence of a uterine body. Sex hormone assays did not detect the presence of estradiol-17 ␤; however, progesterone (2 ng/ml) was found in the serum, indicating anestrus. On gross examination of the reproductive tract, the uterine body was absent, apparently never formed. In its place, a cord-like piece of tissue was identified as an aplastic/dysplastic remnant, connecting the cervix and right uterine horn. The tip of the cord-like piece branched into 5 string-like pieces of tissue, 1 of which was connected to the region dividing the left and right uterine horns. Both the uterine horns were dilated markedly revealing hydrometra. Histologically, uterine body remnant tissues from the endometrium, myometrium, and perimetrium were detected in proximal and distal parts of the uterine body. The string-like piece of tissue connecting the uterine body remnant and the uterine horn consisted of a round cluster of smooth muscle cells surrounding a central core of adipose tissue with blood vessels. It was concluded that the hydrometra observed in both uterine horns was induced by an obstruction resulting from segmental aplasia in the uterine body. This is the first known report of segmental aplasia in the uterine body of a bitch.

Zinc is trace element essential for diverse metabolic and cellular signaling pathways for the growth, development, and maintenance. Zinc deficiency is involved in bone malformations and oral disease. Mice deficient in zinc transporter Zip13 show connective tissue and skeletal disorders, abnormal incisor teeth, and reduced root dentin formation in the molar teeth and share a morphologically similar phenotype to nuclear factor I-C (NFI-C)-deficient mice. However, the precise function of zinc in NFI-C signaling-mediated odontoblast differentiation and dentin formation remains unclear. Here, we show that zinc stimulated the expression of metal transcription factor-1, but decreased NFI-C expression in odontoblastic MDPC-23 cells. Zinc also enhanced the phosphorylation of Smad2/3 (p-Smad2/3) and increased the binding efficiency of NFI-C and p-Smad2/3 in the cytoplasm. In contrast, zinc deficiency resulted in the accumulation of NFI-C into nucleus. Consequently, NFI-C had the biologic properties of a transcription factor, including DNA binding affinity for metallothionein-1 and the dentin sialophosphoprotein (DSPP) promoter, and transcriptional activation of the DSPP gene. Furthermore, zinc deficiency condition promoted DSPP expression in odontoblasts and dentin mineralization, while zinc sufficiency condition decreased DSPP expression and slightly delayed dentin mineralization. These data suggest that zinc equilibrium is required for odontoblast differentiation and dentin formation during dentinogenesis through the nuclear accumulation and modulation of NFI-C.

Serum proteins are believed to trigger a sudden failure of lung function, but to date the mechanism remains elusive. Most studies have focused on the transport of the proteins from the subphase to the lung surfactant interface, although the opposite direction of transport, i.e., from air-to-interface, could be equally important. Here, we report that physiological concentrations of serum droplets can rapidly form a film upon exposure to air, and the entire film can be transferred to the lung surfactant interface upon coalescence, displacing it. This film was mechanically stable and remains intact even for multiple biaxial compression/expansion cycles. Our findings provide a mechanism of lung surfactant replacement by serum proteins that is fundamentally different from the subphase-to-interface transport and demonstrate that it is nearly impossible to remove the film from the interface where the lung surfactant should be, thus impairing the lung in a permanent way.