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Journal of Histochemistry and Cytochemistry, Vol. 50, 779-788, June 2002, Copyright © 2002, The Histochemical Society, Inc.

ARTICLE

Endothelial Nitric Oxide Synthase and Its Negative Regulator Caveolin-1 Localize to Distinct Perinuclear Organelles

Roland Goversa, Peter van der Sluijsb, Elly van Donselaarb, Jan-Willem Slotb, and Ton J. Rabelinka
a Department of Vascular Medicine, UMC Utrecht, Utrecht, the Netherlands
b Department of Cell Biology, UMC Utrecht, Utrecht, the Netherlands

Correspondence to: Roland Govers, Garvan Inst. of Medical Research, 384 Victoria St., Darlinghurst NSW 2010, Australia. E-mail: r.govers@garvan.org.au

Caveolin-1 is a member of a subset of intracellular proteins that regulate endothelial nitric oxide synthase (eNOS) activity. In caveolae, caveolin-1 inhibits eNOS activity via a direct interaction with the enzyme. Previous work has indicated that both eNOS and caveolin-1 are also localized at the perinuclear Golgi complex. Whether caveolin-1 is involved in eNOS regulation in this cell compartment is unknown. Here we studied the localization of eNOS and caveolin-1 in the perinuclear region of primary bovine aortic endothelial cells. By immunofluorescence microscopy we show that both eNOS and caveolin-1 co-localize with Golgi markers. On treatment of the cells with the microtubule-depolymerizing drug nocodazole, the Golgi complex is scattered and caveolin-1 is found in vesicles at the periphery of the cell, while eNOS is localized at large structures near the nucleus. The nocodazole-induced redistribution of eNOS is similar to that of cis-, medial-, and trans-Golgi markers, while the caveolin-1 redistribution resembles that of sec22, a marker for the intermediate compartment. The localization of eNOS and caveolin-1 at distinct perinuclear compartments that behave differently in the presence of nocodazole indicates that eNOS activity is not regulated by caveolin-1 in the Golgi complex.

(J Histochem Cytochem 50:779–788, 2002)

Key Words: eNOS, caveolin-1, endothelium, immunolocalization


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