PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 19717728-1 2009 Previously, we have demonstrated that cGMP-dependent protein kinase (PKG) activity is downregulated in vessels from diabetic animals or in vascular smooth muscle cells (VSMCs) exposed to high-glucose conditions, contributing to diabetes-associated vessel dysfunction. Glucose 192-199 protein kinase cGMP-dependent 1 Homo sapiens 69-72 32848770-6 2020 However, most data indicate that B2R induces increased glucose oxidation, instead of storage, via activation of a broad signaling cascade involving Nitric Oxide (NO) and cyclic-GMP dependent protein kinase (PKG). Glucose 55-62 protein kinase cGMP-dependent 1 Homo sapiens 207-210 22837307-4 2012 We observed that platelet exposure to 25 mmol/L d-glucose, but not to iso-osmolar mannitol, 1) reduced the ability of L-ASA to inhibit platelet responses to agonists; 2) did not modify the L-ASA-induced inhibition of thromboxane synthesis; and 3) prevented the L-ASA-induced activation of the NO/cGMP/PKG pathway. Glucose 48-57 protein kinase cGMP-dependent 1 Homo sapiens 301-304 22837307-6 2012 Thus, high glucose acutely reduces the antiaggregating effect of aspirin, does not modify the aspirin-induced inhibition of thromboxane synthesis, and inhibits the aspirin-induced activation of the NO/cGMP/PKG pathway. Glucose 11-18 protein kinase cGMP-dependent 1 Homo sapiens 206-209 31269778-5 2019 High glucose concentrations lead to a loss of mitochondrial networks, increased reactive oxygen species (ROS), endothelial nitric oxide synthase (eNOS) activation and a reduction in cGMP production related to protein kinase G (PKG) activity. Glucose 5-12 protein kinase cGMP-dependent 1 Homo sapiens 209-225 31269778-5 2019 High glucose concentrations lead to a loss of mitochondrial networks, increased reactive oxygen species (ROS), endothelial nitric oxide synthase (eNOS) activation and a reduction in cGMP production related to protein kinase G (PKG) activity. Glucose 5-12 protein kinase cGMP-dependent 1 Homo sapiens 227-230 25863494-3 2015 The present study was undertaken to investigate how high glucose concentrations regulate PKG expression in cytotrophoblast cells (CTBs). Glucose 57-64 protein kinase cGMP-dependent 1 Homo sapiens 89-92 25863494-9 2015 Exposure of CTBs to excess glucose down-regulates cGMP and cGMP-dependent PKG, contributing to the development of vascular complications in diabetic mothers during pregnancy. Glucose 27-34 protein kinase cGMP-dependent 1 Homo sapiens 74-77 19717728-3 2009 In this report, high-glucose-mediated decreased PKG activity in VSMCs was restored by transfection of cells with expression vector for the catalytic domain of PKG-I (PKG-CD, constitutive active PKG). Glucose 21-28 protein kinase cGMP-dependent 1 Homo sapiens 48-51 19717728-3 2009 In this report, high-glucose-mediated decreased PKG activity in VSMCs was restored by transfection of cells with expression vector for the catalytic domain of PKG-I (PKG-CD, constitutive active PKG). Glucose 21-28 protein kinase cGMP-dependent 1 Homo sapiens 159-162 19717728-3 2009 In this report, high-glucose-mediated decreased PKG activity in VSMCs was restored by transfection of cells with expression vector for the catalytic domain of PKG-I (PKG-CD, constitutive active PKG). Glucose 21-28 protein kinase cGMP-dependent 1 Homo sapiens 159-162 19717728-3 2009 In this report, high-glucose-mediated decreased PKG activity in VSMCs was restored by transfection of cells with expression vector for the catalytic domain of PKG-I (PKG-CD, constitutive active PKG). Glucose 21-28 protein kinase cGMP-dependent 1 Homo sapiens 159-162 19717728-5 2009 Our data demonstrated that high glucose exposure stimulated VSMC proliferation and G1 to S phase progression of the cell cycle, which was inhibited by restoration of PKG activity. Glucose 32-39 protein kinase cGMP-dependent 1 Homo sapiens 166-169 19717728-6 2009 Expression of constitutively active PKG inhibited G1 phase exit in VSMCs under high glucose conditions, which was accompanied by an inhibition of retinoblastoma protein (Rb) phosphorylation (a key switch for G1 to S phase cell cycle progression). Glucose 84-91 protein kinase cGMP-dependent 1 Homo sapiens 36-39 19717728-7 2009 Glucose-induced cyclin E expression and cyclin E-cyclin-dependent kinase 2 activity was also reduced by expression of PKG-CD in VSMCs. Glucose 0-7 protein kinase cGMP-dependent 1 Homo sapiens 118-121 19717728-8 2009 Moreover, expression of PKG-CD suppressed glucose-induced p27 degradation. Glucose 42-49 protein kinase cGMP-dependent 1 Homo sapiens 24-27 19717728-9 2009 These data demonstrate that restoring the high-glucose-mediated decrease in PKG activity in VSMCs inhibits glucose-induced abnormal VSMC proliferation occurring upstream of Rb phosphorylation. Glucose 47-54 protein kinase cGMP-dependent 1 Homo sapiens 76-79 19717728-9 2009 These data demonstrate that restoring the high-glucose-mediated decrease in PKG activity in VSMCs inhibits glucose-induced abnormal VSMC proliferation occurring upstream of Rb phosphorylation. Glucose 107-114 protein kinase cGMP-dependent 1 Homo sapiens 76-79 19717728-10 2009 Our work provides the first direct evidence linking decreased PKG activity to high glucose-induced proliferation and cell cycle progression in VSMCs, suggesting that strategies to increase PKG activity might be useful in preventing abnormal VSMC proliferation in diabetic patients and might provide treatments for diabetes-associated proliferative vascular diseases. Glucose 83-90 protein kinase cGMP-dependent 1 Homo sapiens 62-65 19717728-10 2009 Our work provides the first direct evidence linking decreased PKG activity to high glucose-induced proliferation and cell cycle progression in VSMCs, suggesting that strategies to increase PKG activity might be useful in preventing abnormal VSMC proliferation in diabetic patients and might provide treatments for diabetes-associated proliferative vascular diseases. Glucose 83-90 protein kinase cGMP-dependent 1 Homo sapiens 189-192 15184388-2 2004 We previously showed that inducible expression of the catalytic domain of cGMP-dependent protein kinase (PKG) inhibits glucose-regulated TSP1 transcription and transforming growth factor (TGF)-beta activity in stably transfected rat mesangial cells (RMCs(tr/cd)). Glucose 119-126 protein kinase cGMP-dependent 1 Homo sapiens 105-108 15184388-3 2004 However, the molecular mechanisms by which PKG represses glucose-regulated TSP1 transcription are unknown. Glucose 57-64 protein kinase cGMP-dependent 1 Homo sapiens 43-46 15184388-6 2004 Moreover, binding is significantly enhanced by high glucose treatment and is reduced by increased PKG activity. Glucose 52-59 protein kinase cGMP-dependent 1 Homo sapiens 98-101 15184388-10 2004 Increased PKG activity down-regulates USF2 protein levels and its DNA binding activity under high glucose conditions, resulting in inhibition of glucose-induced TSP1 transcription and TGF-beta activity. Glucose 98-105 protein kinase cGMP-dependent 1 Homo sapiens 10-13 15184388-10 2004 Increased PKG activity down-regulates USF2 protein levels and its DNA binding activity under high glucose conditions, resulting in inhibition of glucose-induced TSP1 transcription and TGF-beta activity. Glucose 145-152 protein kinase cGMP-dependent 1 Homo sapiens 10-13 15184388-11 2004 Overexpression of USF2 reversed the inhibitory effect of PKG on glucose-induced TSP1 gene transcription and TGF-beta activity. Glucose 64-71 protein kinase cGMP-dependent 1 Homo sapiens 57-60 12621526-5 2003 The effect of D-glucose was blocked by the PKC inhibitor calphostin C, the MAP kinase kinase 1/2 (MEK1/2) inhibitor PD-98059, the eNOS inhibitor L-NAME, the protein kinase G (PKG) inhibitor KT-5823 and the protein kinase A (PKA) inhibitor KT-5720. Glucose 14-23 protein kinase cGMP-dependent 1 Homo sapiens 157-173 12621526-5 2003 The effect of D-glucose was blocked by the PKC inhibitor calphostin C, the MAP kinase kinase 1/2 (MEK1/2) inhibitor PD-98059, the eNOS inhibitor L-NAME, the protein kinase G (PKG) inhibitor KT-5823 and the protein kinase A (PKA) inhibitor KT-5720. Glucose 14-23 protein kinase cGMP-dependent 1 Homo sapiens 175-178