Bilirubin inhibits protein kinase C activity and protein kinase C-mediated phosphorylation of endogenous substrates in human skin fibroblasts
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Cited by (44)
Pathophysiology of Kernicterus
2017, Fetal and Neonatal Physiology, 2-Volume SetMechanisms of Bilirubin-Induced Brain Injury
2011, Fetal and Neonatal Physiology E-Book, Fourth EditionProtein kinase A and C signaling induces bilirubin potentiation of GABA/glycinergic synaptic transmission in rat ventral cochlear nucleus neurons
2010, Brain ResearchCitation Excerpt :Thus, evaluation of the effects of bilirubin on GABA/glycinergic synaptic transmission and the related underlying mechanisms may provide new directions for exploring the pathogenesis of bilirubin-induced CNS injury. Previous reports have indicated that bilirubin inhibited protein phosphorylation, modulated by cAMP-dependent protein kinase (PKA) and protein kinase C (PKC), in several cell types (Amit and Boneh, 1993; Hansen et al., 1996; Sano et al., 1985). Protein/peptide phosphorylation has been shown to be an important regulatory mechanism for many cell processes, including neurotransmitter release (Evans and Morgan, 2003; Oleskevich and Walmsley, 2000; Walaas and Greengard, 1991).
Regulation of vulnerable plaque development by the heme oxygenase/carbon monoxide system
2010, Trends in Cardiovascular MedicineCitation Excerpt :Bilirubin is able to potently inhibit superoxide-producing nicotinamide adenine dinucleotide phosphate oxidase activation upon exposure to reactive oxygen species (Kwak et al. 1991). In addition, biliverdin has been shown to directly inhibit protein phosphorylation (Hansen et al. 1996) and protein kinase C activity (PKC) (Amit and Boneh 1993) in subcellular fractions of human skin fibroblasts, and in vitro by PKC phosphorylation of endogenous substrates (Hansen et al. 1996). The PKC activity in vitro was inhibited in a dose-dependent manner by biliverdin and reversed by increasing concentrations of lipids, in both the cytosolic and membrane fractions.
Hemoxygenase-1 in Cardiovascular Disease
2008, Journal of the American College of CardiologyCitation Excerpt :Both molecules are natural antioxidants, and high-normal serum levels of bilirubin are inversely related to the atherogenic risk, possibly by inhibitory effects against low-density lipoprotein oxidation and the scavenging of oxygen radicals (17,18). Additionally, an inhibitory effect on protein kinase C and protein phosphorylation activity has been shown, both of which lead to inhibition of proatherogenic factors (19,20). Bilirubin also provides cardioprotection against reperfusion injury, such as by the suppression of the oxidation of lipid membranes (21,22).
Association of serum bilirubin with pulsatile arterial function in asymptomatic young adults: the Bogalusa Heart Study
2008, Metabolism: Clinical and ExperimentalCitation Excerpt :The present observational study, however, cannot address the issue of causality or mechanisms by which bilirubin protects the vasculature against oxidative stress and inflammation. Based on research findings in this area [27-32], the possible mechanisms include, among others, activation of endothelial nitric oxide synthase expression and suppression of proinflammatory genes like vascular cell adhesion molecule 1, monocyte chemoattractant protein 1, and macrophage colony-stimulating factor; inhibition of superoxide producing nicotinamide adenine dinucleotide phosphate (NADPH) oxidase; protein phosphorylation; protein kinase C activity; and p38 mitogen-activated protein kinase signal transduction pathways. In this study, cigarette smoking attenuated the strength of the positive association between bilirubin and small-artery compliance and reduced the bilirubin level.