We are analyzing https://link.springer.com/article/10.1007/s00125-005-1857-5.

Title:
Endothelial nitric oxide synthase dysfunction in diabetic mice: importance of tetrahydrobiopterin in eNOS dimerisation | Diabetologia
Description:
Aims/hypothesis Impaired nitric oxide (NO) bioactivity and increased superoxide (SO) production are characteristics of vascular endothelial dysfunction in diabetes. The underlying mechanisms remain unknown. In this regard, we investigated the role of tetrahydrobiopterin (BH4) bioavailability in regulating endothelial nitric oxide synthase (eNOS) activity, dimerisation and SO production in streptozotocin-induced diabetic mice. Methods Mouse aortas were used for assays of the following: (1) aortic function by isometric tension; (2) NO by electronic paramagnetic resonance; (3) SO by lucigenin-enhanced chemiluminescence and dihydroethidine fluorescence; (4) total biopterin and BH4 by high-performance liquid chromatography; and (5) eNOS protein expression and dimerisation by immunoblotting. Results In diabetic mouse aortas, relaxations to acetylcholine and NO levels were significantly decreased, but SO production was increased, in association with reductions in total biopterins and BH4. Although total eNOS levels were increased in diabetes, the protein mainly existed in monomeric form. Conversely, specifically augmented BH4 in diabetic endothelium preserved eNOS dimerisation, but the expression remained unchanged. Conclusions/interpretation Our results demonstrate that BH4 plays an important role in regulating eNOS activity and its functional protein structure, suggesting that increasing endothelial BH4 and/or protecting it from oxidation may be a rational therapeutic strategy to restore eNOS function in diabetes.
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Keywords {🔍}

enos, diabetic, endothelial, google, scholar, diabetes, mice, nitric, oxide, synthase, production, tetrahydrobiopterin, dimerisation, protein, mouse, aorta, vascular, aortic, function, mmoll, increased, dysfunction, aortas, expression, vessel, balbc, activity, levels, fig, superoxide, role, bioavailability, gchtg, buffer, biol, results, oxidation, gtpch, cbl, min, relaxation, total, endothelium, peroxynitrite, study, cells, moll, nondiabetic, nitricoxide, chem,

Topics {✒️}

ice-cold krebs-hepes buffer nitro-l-arginine methyl ester nitric-oxide synthase types endothelial nitric-oxide synthase neuronal nitric-oxide synthase targeted transgenic gtp-cyclohydrolase diabetic wild-type mice warmed krebs-hepes buffer warmed krebs–hepes buffer receptor-mediated enos agonist fresh krebs-hepes buffer evaluate endothelium-independent relaxation x-band epr spectrometer bio-rad protein assay high-performance liquid chromatography results endothelial-dependent relaxation nitric-oxide synthases 350 μl krebs-hepes buffer stz-induced diabetic mice diabetic gch-tg mice low-temperature sds-page diabetic gch-tg mouse streptozotocin-induced diabetic mice impaired vasomotor function stz-induced diabetic aorta nitric oxide generation wild-type littermates [22] krebs-hepes buffer endothelial-dependent relaxation privacy choices/manage cookies related subjects endothelium-dependent relaxation human endothelial cells augmenting intracellular bh4 6-pyruvol-tetrahydropterin synthase endothelial-independent relaxation aortic endothelial cells impaired vessel relaxation health image software endothelium-independent relaxation unstable enos homodimerisation stz-induced diabetes regulating enos activity enos enzymatic activity diabetic endothelial dysfunction 90 μl protein-free supernatant endothelium-dependent contractions vascular endothelial dysfunction smooth muscle cells apoe-deficient mice

Questions {❓}

Katusic ZS (2001) Vascular endothelial dysfunction: does tetrahydrobiopterin play a role?

Schema {🗺️}

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         description:Impaired nitric oxide (NO) bioactivity and increased superoxide (SO) production are characteristics of vascular endothelial dysfunction in diabetes. The underlying mechanisms remain unknown. In this regard, we investigated the role of tetrahydrobiopterin (BH4) bioavailability in regulating endothelial nitric oxide synthase (eNOS) activity, dimerisation and SO production in streptozotocin-induced diabetic mice. Mouse aortas were used for assays of the following: (1) aortic function by isometric tension; (2) NO by electronic paramagnetic resonance; (3) SO by lucigenin-enhanced chemiluminescence and dihydroethidine fluorescence; (4) total biopterin and BH4 by high-performance liquid chromatography; and (5) eNOS protein expression and dimerisation by immunoblotting. In diabetic mouse aortas, relaxations to acetylcholine and NO levels were significantly decreased, but SO production was increased, in association with reductions in total biopterins and BH4. Although total eNOS levels were increased in diabetes, the protein mainly existed in monomeric form. Conversely, specifically augmented BH4 in diabetic endothelium preserved eNOS dimerisation, but the expression remained unchanged. Our results demonstrate that BH4 plays an important role in regulating eNOS activity and its functional protein structure, suggesting that increasing endothelial BH4 and/or protecting it from oxidation may be a rational therapeutic strategy to restore eNOS function in diabetes.
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