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Immunohistochemical study of arachidonate 12-lipoxygenase in porcine tissues

T Maruyama, N Ueda, T Yoshimoto, S Yamamoto, N Komatsu and K Watanabe

Department of Biochemistry, Tokushima University School of Medicine, Japan.

12-Lipoxygenase oxygenates the 12 position of arachidonic acid and produces its 12-hydroperoxy derivative. The enzyme is found in greatest amounts in porcine leukocytes and is distributed widely in various other tissues. An anti-12-lipoxygenase antibody was raised in rabbits with the immunoaffinity-purified enzyme as an antigen and was used in immunohisto- and cytochemical studies on the enzyme, the physiological significance of which remains to be clarified. When peripheral blood cells were examined by immunoelectron microscopy, the enzyme was found in neutrophils and monocytes but was not detected in lymphocytes, platelets, and erythrocytes. In immunostained neutrophils and monocytes the enzyme was localized in the cytosol but was not clearly detected in the plasma membrane, nuclear membrane, endoplasmic reticulum, and other organelles. Several other organs known to contain considerable amounts of 12-lipoxygenase were also investigated immunohistochemically, i.e., alimentary tract (ileum and jejunum), lymphatic organs (spleen, lymph node, and thymus), ovary, lung, liver, and others. In these organs, resident mast cells and granulocytes infiltrating the interstitial tissues were positively immunostained. The enzyme was not detected in parenchymal cells of these organs under our experimental conditions.

Volume 37, Issue 7, pp. 1125-1131, 07/01/1989
Copyright © 1989 by The Histochemical Society


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