EC were collected from the brachial artery and an antecubital vein of 106 healthy adults (60 men and 46 women, age 18-77 years). Quantitative immunofluorescence was used to measure protein expression of endothelial nitric oxide synthase (eNOS), Ser-1177 phosphorylated eNOS, manganese superoxide dismutase, nitrotyrosine, xanthine oxidase and nuclear factor-kappa Tideglusib datasheet B p65. Protein expression in EC obtained from brachial artery and antecubital vein sampling was moderately to strongly related (r = 0.59-0.81, all p < 0.0001, mean r = 0.70). Moreover, differences between subgroups in the lowest and highest tertiles of protein expression
in EC obtained from arterial samples were consistently reflected in EC obtained from venous collections. These findings indicate that interindividual and group differences in expression of several proteins involved in nitric oxide production, oxidant production, antioxidant defense and inflammatory signaling in EC obtained from brachial artery sampling are consistently reflected in EC buy Temsirolimus obtained
from venous samples. Thus, EC collected from peripheral veins may provide a useful surrogate for EC obtained from arteries for measurements of EC protein expression in humans. Copyright (C) 2009 S. Karger AG, Basel”
“Background: Increasing evidence has suggested that differentiation of adventitial fibroblasts (AFs) to myofibroblasts plays an important role in arterial remodeling. The molecular mechanisms by which myofibroblast formation is regulated still remain largely unknown. This study aimed to evaluate the role of cyclic nucleotide phosphodiesterase 1A (PDE1A) in the formation of adventitial myofibroblasts induced by transforming growth factor (TGF)-beta(1). Methods and Results: AFs were
cultured by the explant method. Western blot and immunocytochemistry were applied for alpha-smooth muscle actin (SMA) or protein Etomidate kinase C (PKC) alpha protein analysis. Results showed that TGF-beta(1) upregulated PDE1A protein expression in rat aortic AFs and pharmacological inhibition of PDE1A blocked TGF-beta(1)-induced alpha-SMA expression, a marker of myofibroblast formation, suggesting that the upregulation of PDE1A may mediate TGF-beta(1)-induced AF transformation. Moreover, calphostin C (a PKC inhibitor) inhibited TGF-beta(1)-induced alpha-SMA expression, whereas phorbol-12-myristate-13-acetate (a PKC activator) induced it. Finally, the upregulation of PKC alpha expression by TGF-beta(1) was also inhibited by PDE1A inhibition. Conclusions: Taken together, our data suggest that TGF beta(1) induces alpha-SMA expression and myofibroblast formation via a PDE1A-PKC alpha dependent mechanism. Our study thus unveils a novel signaling mechanism underlying TGF-beta(1)-induced adventitial myofibroblast formation. Copyright (C) 2009 S.