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Bronchoalveolar Lavage Exosomes in Lipopolysaccharide-induced Septic Lung Injury
Published on: May 21, 2018
Biochemical and immunohistochemical evidence for selective expression of novel epithelial lipoxygenases
V R Shannon1, J R Hansbrough, Y Takahashi
1Department of Medicine, Washington University School of Medicine, St. Louis, Missouri 63110.
Human tracheal epithelial cells contain an arachidonate 15-lipoxygenase, while the same cells from animals (including bovine, ovine, canine, porcine) cells express a 12-lipoxygenase. The epithelial 12-lipoxygenase is antigenically related to the leukocyte 12-lipoxygenase but is biochemically distinct from platelet and leukocyte forms of the enzyme, in that it is more efficient at metabolizing a wider array of fatty acid substrates. We have suggested that this lipoxygenase heterogeneity may provide a basis for different functional roles for the enzyme in different cell types. In addition, animal epithelial 12-lipoxygenase and human epithelial 15-lipoxygenase are antigenically related and have similar but distinct distributions in the lung. Our findings might suggest that the species diversity for epithelial lipoxygenases represents molecular divergence within a family of closely related genes with perhaps closely related functions.
Human tracheal epithelial cells contain an arachidonate 15-lipoxygenase, while the same cells from animals (including bovine, ovine, canine, porcine) cells express a 12-lipoxygenase. The epithelial 12-lipoxygenase is antigenically related to the leukocyte 12-lipoxygenase but is biochemically distinct from platelet and leukocyte forms of the enzyme, in that it is more efficient at metabolizing a wider array of fatty acid substrates. We have suggested that this lipoxygenase heterogeneity may provide a basis for different functional roles for the enzyme in different cell types. In addition, animal epithelial 12-lipoxygenase and human epithelial 15-lipoxygenase are antigenically related and have similar but distinct distributions in the lung. Our findings might suggest that the species diversity for epithelial lipoxygenases represents molecular divergence within a family of closely related genes with perhaps closely related functions.

