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DOI: 10.1369/jhc.4A6307.2004
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Journal of Histochemistry and Cytochemistry
Volume 52 (10): 1277-1285, 2004
Copyright ©The Histochemical Society, Inc.

Colocalization of eNOS and the Catalytic Subunit of PKA in Endothelial Cell Junctions : A Clue for Regulated NO Production

Harry F.G. Heijnen, Sandra Waaijenborg, James D. Crapo, Russell P. Bowler, Jan-Willem N. Akkerman and Jan W. Slot

Thrombosis and Haemostasis Laboratory (HFGH,SW,J-WNA), and Department of Cell Biology, (HFGH,SW,JWS), University Medical Center Utrecht, Utrecht, The Netherlands; Institute for Biomembranes (HFGH,SW,J-WNA,JWS), Utrecht, The Netherlands; and National Jewish Medical Center (JDC,RPB), Denver, Colorado

Correspondence to: Dr. Harry F.G. Heijnen, Thrombosis and Haemostasis Laboratory, University Medical Center Utrecht, Heidelberglaan 100, 3584 CX Utrecht, The Netherlands. E-mail: h.f.g.heijnen{at}azu.nl

Localization and coordinate phosphorylation/dephosphorylation of endothelial nitric oxide synthase (eNOS) are critical determinants for the basal and stimulated production of nitric oxide. Several phosphorylation sites in eNOS have been identified as targets of the cAMP-dependent protein kinase A (PKA). Basal eNOS activity is also regulated by interaction with caveolin-1, the major coat protein of caveolae. In the present study we have examined in rat aorta endothelium the subcellular steady-state distribution of eNOS, the catalytic subunit of PKA (PKA-c), and caveolin-1. Basal eNOS expression was found in two distinct locations, the endothelial cell surface and the Golgi complex. Cell surface eNOS was equally distributed over caveolar and non-caveolar membranes but was 2.5-fold enriched on luminal lamellipodia located at endothelial cell contacts. PKA-c colocalized with eNOS in the lamellipodia, whereas caveolin-1 was absent from these membrane domains. PKA-c was also found associated with cell surface caveolae and with tubulovesicular membranes of Golgi complex and endosomes. The topological proximity of eNOS with the catalytic subunit of PKA in restricted intracellular locations may provide mechanisms for differential PKA-mediated eNOS regulation. (J Histochem Cytochem 52:1277–1285, 2004)

Key Words: eNOS • PKA • caveolin-1 • NO production


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