No abstract

No abstract

No abstract

A leiomyosarcoma that occurred in the right kidney of a dog (7-year-old female Labrador retriever) was studied pathologically. On histological examination, tumour cells were spindle-shaped, the cell density was high, and complex fasciculated tumour cells showing longitudinal and transverse cross-sections were observed. Both ends of the nuclei were rounded, the nucleoli were clear and many images of nuclear division were observed. Immunohistochemically, tumour cells reacted intensely with anti-vimentin antibody and anti-actin smooth muscle antibody, and mildly with anti-desmin antibody. On electron microscopy, the nuclei of tumour cells were rounded at both ends and elongated elliptically, and a large number of microfibrils with focal density and dense patches were observed in the cytoplasm. This is a case report of a very rare leiomyosarcoma of the dog kidney.

Thraustochytrids are heterotrophic marine protists that are considered as important decomposers in the marine ecosystem; however, how they digest and uptake lipid nutrients from the environment is largely unknown. Genomic clustering analysis using thraustochytrid draft genome databases revealed that novel proteins with a Lipase_3 domain are commonly present in thraustochytrids, including Aurantiochytrium limacinum. After heterologous expression and His tag-based purification, protein ID: 145138 was identified as lipase/phospholipase capable of hydrolyzing triacylglycerol (TG) and phosphatidylcholine (PC). 145138 was secreted into the medium, and deletion of the 145138 gene in A. limacinum reduced the degradation of extracellular lipids. Fatty acids generated by 145138 were reused for the biosynthesis of PC and TG, and 145138 allowed A. limacinum to survive in the medium containing TG as a sole carbon source. 145138 hydrolyzed all the acyl-ester linkages of TG; however, the enzyme showed strict positional specificity toward phospholipids, generating 2-acyl lysophospholipids. The 2-acyl lysophospholipids showed stronger antimicrobial activity compared with 1-acyl lysophospholipids. These results suggested that 145138 is a bifunctional enzyme that contributes to the acquisition of lipid nutrients from the environment, as well as to generate antimicrobial lysophospholipids that are beneficial for competition with bacteria over lipid nutrients in the marine environment.