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Journal of Histochemistry and Cytochemistry, Vol. 49, 613-622, May 2001, Copyright © 2001, The Histochemical Society, Inc.

ARTICLE

The Role of 15-lipoxygenase in Disruption of the Peroxisomal Membrane and in Programmed Degradation of Peroxisomes in Normal Rat Liver

Sadaki Yokotaa, Toshiaki Odab, and H. Dariush Fahimic
a Biology Laboratory, Yamanashi Medical University, Yamanashi, Japan
b Department of Biochemistry, Hamamatsu University School of Medicine, Hamamatsu, Japan
c Department of Anatomy and Cell Biology, University of Heidelberg, Heidelberg, Germany

Correspondence to: Sadaki Yokota, Biology Laboratory, Yamanashi Medical University, Yamanashi 409-3898, Japan. E-mail: syokota@res.yamanashi-med.ac.jp

Our earlier electron microscopic observations revealed that prolonged exposure of glutaraldehyde-fixed rat liver sections to buffer solutions induced focal membrane disruptions of peroxisomes with catalase diffusion as shown cytochemically. Recently, it was suggested that 15-lipoxygenase (15-LOX) might be involved in natural degradation of membrane-bound organelles in reticulocytes by integrating into and permeabilizing the organelle membranes, leading to the release of matrix proteins. We have now investigated the localization of 15-LOX and its role in degradation of peroxisomal membranes in rat liver. Aldehyde-fixed liver slices were incubated in a medium that conserved the 15-LOX activity, consisting of 50 mM HEPES–KOH buffer (pH 7.4), 5 mM mercaptoethanol, 1 mM MgCl2, 15 mM NaN3, and 0.2 M sucrose, in presence or absence of 0.5–0.05 mM propyl gallate or esculetin, two inhibitors of 15-LOX. The exposure of aldehyde-fixed liver sections to this medium induced focal disruptions of peroxisome membranes and catalase diffusion around some but not all peroxisomes. This was significantly reduced by both 15-LOX inhibitors, propyl gallate and esculetin, with the latter being more effective. Double immunofluorescent staining for 15-LOX and catalase revealed that 15-LOX was co-localized with catalase in some but not all peroxisomes in rat hepatocytes. By postembedding immunoelectron microscopy, gold labeling was localized on membranes of some peroxisomes. These observations suggest that 15-LOX is involved in degradation of peroxisomal membranes and might have a physiological role in programmed degradation and turnover of peroxisomes in hepatocytes. (J Histochem Cytochem 49:613–621, 2001)

Key Words: 15-lipoxygenase, membrane disruption, peroxisomes, programmed degradation


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