A function for lipoxygenase in programmed organelle degradation Journal Article


Authors: Van Leyen, K.; Duvoisin, R. M.; Engelhardt, H.; Wiedmann, M.
Article Title: A function for lipoxygenase in programmed organelle degradation
Abstract: Membrane-enclosed organelles, a defining characteristic of eukaryotic cells, are lost during differentiation of specific cell types such as reticulocytes (an intermediate in differentiation of erythrocytes), central fibre cells of the eye lens, and keratinocytes. The degradation of these organelles must be tightly regulated with respect to both the time of activation and the specificity of membrane degradation. The expression of 15- lipoxygenase (15-LOX) peaks in reticulocytes immediately before organelle degradation. Here we show that 15-LOX integrates into the membranes of various organelles, allowing release of proteins from the organelle lumen and access of proteases to both lumenal and integral membrane proteins. In addition, by sparing the plasma membrane, 15-LOX shows the required specificity for organellar membranes. Thus, the action of 15-LOX provides a mechanism by which the natural degradation process can be explained. This conclusion is supported by our finding that lipoxygenase expression in the eye lens is restricted to the region at which organelle degradation occurs.
Keywords: controlled study; nonhuman; animal cell; mouse; animals; mice; animal tissue; membrane proteins; enzyme activity; animalia; endoplasmic reticulum; enzyme inhibitors; eukaryota; membrane protein; carboxyfluorescein; lens; lens, crystalline; cell organelle; liposome; liposomes; membrane lipid; organelles; solubility; degradation; permeability; rabbits; membrane lipids; intracellular membranes; rabbit; lipoxygenase inhibitor; oryctolagus cuniculus; reticulocyte; reticulocytes; priority journal; article; arachidonate 15 lipoxygenase; arachidonate 15-lipoxygenase; gallic acid propyl ester; icosatetraynoic acid; propyl gallate
Journal Title: Nature
Volume: 395
Issue: 6700
ISSN: 0028-0836
Publisher: Nature Publishing Group  
Date Published: 1998-09-24
Start Page: 392
End Page: 395
Language: English
DOI: 10.1038/26500
PUBMED: 9759730
PROVIDER: scopus
DOI/URL:
Notes: Article -- Export Date: 12 December 2016 -- Source: Scopus
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