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July 1, 1995Journal of Biological ChemistryOpen Access

The Golgi Association of Endothelial Nitric Oxide Synthase Is Necessary for the Efficient Synthesis of Nitric Oxide

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Population

Cultured endothelial cells, intact blood vessels, and HEK 293 cells

Comparison

Expression of wild-type myristoylated and… vs Expression of mutant, non-acylated eNOS

Design

Preclinical

Authors

WSWilliam C. SessaVascular MedicineGGGuillermo Garca-CardeaAddenbrooke's HospitalJLJianwei LiuHandan College

Discussion

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Implication

Acylation-dependent eNOS localization may enhance NO output; leaves open relevance to vascular disease and requires in vivo confirmation.

Key Points

  • To determine whether endothelial nitric oxide synthase localizes to the Golgi apparatus and if this specific compartmentalization is required for cellular nitric oxide synthesis.
  • Examined endogenous eNOS localization in cultured endothelial cells and intact blood vessels.
  • Expressed wild-type acylated (myristoylated and palmitoylated) eNOS and mutant non-acylated eNOS in a heterologous HEK 293 cell model.
  • Measured and compared nitric oxide production levels between HEK 293 cells expressing wild-type eNOS and those expressing non-acylated mutant eNOS.
  • Endothelial nitric oxide synthase was identified as a Golgi-associated protein in both cultured endothelial cells and intact vascular tissue.
  • Wild-type myristoylated and palmitoylated eNOS targeted to the Golgi apparatus, whereas the mutant non-acylated enzyme failed to compartmentalize to the Golgi.
  • HEK 293 cells expressing wild-type eNOS released substantially greater amounts of nitric oxide compared to cells expressing the mutant non-acylated enzyme.

Structured PICO

P
Population
Cultured endothelial cells, intact blood vessels, and HEK 293 cells
I
Intervention
Expression of wild-type myristoylated and palmitoylated eNOS
C
Comparator
Expression of mutant, non-acylated eNOS
O
Outcome
Golgi targeting and nitric oxide (NO) releasesurrogate

Golgi compartmentalization of eNOS is necessary for efficient nitric oxide synthesis in response to intracellular signals.

Cite This Study

Sessa et al. (1995) studied this question.

synapsesocial.com/papers/6a7d0910ff1a536db837cc38https://doi.org/10.1074/jbc.270.30.17641
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Also Consider

Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context:

  1. 1Agonist-modulated Palmitoylation of Endothelial Nitric Oxide Synthase1995 · 221 citations
  2. 2Subcellular localization and characterization of nitric oxide synthase(s) in endothelial cells: physiological implications1994 · 136 citations
  3. 3Flow-induced calcium transients in single endothelial cells: spatial and temporal analysis1992 · 184 citations
  4. 4Palmitoylation of multiple Src-family kinases at a homologous N-terminal motif1994 · 184 citations
  5. 5Topology of mannosidase II in rat liver Golgi membranes and release of the catalytic domain by selective proteolysis.1986 · 44 citations