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Immunohistochemical study on arachidonate 5-lipoxygenase in porcine leukocytes and other tissues

N Komatsu, K Natsui, N Ueda, K Watanabe and S Yamamoto

Department of Pathology, Tokai University School of Medicine, Isehara, Japan.

Arachidonate 5-lipoxygenase is an enzyme that catalyzes the oxygenation of arachidonic acid, producing 5-hydroperoxy acid. This enzymatic reaction initiates the biosynthesis of various bioactive leukotrienes. An antiserum was raised in a rabbit against the purified 5-lipoxygenase of porcine leukocytes, and various types of porcine leukocytes were immunostained by use of the antibody. As examined by light and electron microscopy, neutrophils and eosinophils were positively stained. The 5- lipoxygenase was localized in the cytoplasm but not in the plasma membrane and subcellular organelles of the positively stained cells. In contrast, lymphocytes were unstained. In porcine ileum, the majority of 5-lipoxygenase-positive cells were eosinophils and mast cells resident in the lamina propria mucosae, whereas parenchymal cells were not stained. In porcine lung, certain bronchiolar or bronchial epithelial cells were clearly immunostained, in addition to eosinophils and mast cells found in the interstitium.

Volume 39, Issue 5, pp. 655-662, 05/01/1991
Copyright © 1991 by The Histochemical Society


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