% IMPORTANT: The following is UTF-8 encoded.  This means that in the presence
% of non-ASCII characters, it will not work with BibTeX 0.99 or older.
% Instead, you should use an up-to-date BibTeX implementation like “bibtex8” or
% “biber”.

@ARTICLE{Dangwal:14547,
      author       = {Dangwal, S. and Rauch, B.H. and Gensch, T. and Dai, L. and
                      Bretschneider, E. and Vogelaar, C.F. and Schrör, K. and
                      Rosenkranz, A.C.},
      title        = {{H}igh glucose enhances thrombin responses via
                      protease-activated receptor-4 in human vascular smooth
                      muscle cells},
      journal      = {Arteriosclerosis, thrombosis, and vascular biology},
      volume       = {31},
      issn         = {1079-5642},
      address      = {Philadelphia, Pa.},
      publisher    = {Lippincott, Williams $\&$ Wilkins},
      reportid     = {PreJuSER-14547},
      pages        = {624 - 633},
      year         = {2011},
      note         = {This study was supported in part by the Deutsche
                      Forschungsgemeinschaft (SFB 612, Project B11), the Anna
                      Wunderlich-Ernst Juhling Stiftung (Dusseldorf, Germany), and
                      the Forschungsgruppe Herz-Kreislauf eV (Monheim, Germany).},
      abstract     = {Diabetes is associated with vascular remodeling and
                      increased thrombin generation. Thrombin promotes vascular
                      smooth muscle cell (SMC) mitogenesis and migration via
                      protease-activated receptors (PAR)-1, PAR-3, and PAR-4. We
                      investigated the effect of high glucose on expression and
                      function of vascular thrombin receptors.In human vascular
                      SMCs, high glucose (25 versus 5.5 mmol/L) induced a rapid
                      and sustained increase in PAR-4 mRNA, protein, and cell
                      surface expression. PAR-1 and PAR-3 expression were not
                      changed. High glucose pretreatment (48 hours) enhanced
                      thrombin or PAR-4-activating peptide but not
                      PAR-1-activating peptide evoked intracellular calcium
                      mobilization, migration, and tumor necrosis factor α gene
                      expression. This enhancement of thrombin-stimulated
                      migration and gene expression by high glucose was abolished
                      by endogenous PAR-4 knockdown. PAR-4 regulation was
                      prevented by inhibition of protein kinase (PK)C-β and -δ
                      isoforms or nuclear factor (NF)κB. Nuclear translocation of
                      NFκB in high glucose-stimulated SMCs led to PKC-dependent
                      NFκB binding to the PAR-4 promoter in a chromatin
                      immunoprecipitation assay. Furthermore, in situ
                      hybridization and immunohistochemistry confirmed high
                      abundance of PAR-4 in human diabetic vessels as compared
                      with nondiabetic vessels.High glucose enhances SMC
                      responsiveness to thrombin through transcriptional
                      upregulation of PAR-4, mediated via PKC-β, -δ, and NFκB.
                      This may play an important role in the vascular
                      complications of diabetes.},
      keywords     = {Binding Sites / Calcium: metabolism / Calcium Signaling /
                      Cell Movement / Cells, Cultured / Chromatin
                      Immunoprecipitation / Diabetic Angiopathies: genetics /
                      Diabetic Angiopathies: metabolism / Glucose: metabolism /
                      Humans / Immunohistochemistry / In Situ Hybridization /
                      Muscle, Smooth, Vascular: metabolism / Myocytes, Smooth
                      Muscle: metabolism / NF-kappa B: metabolism / Promoter
                      Regions, Genetic / Protein Kinase C: antagonists $\&$
                      inhibitors / Protein Kinase C: metabolism / Protein Kinase
                      C-delta: genetics / Protein Kinase C-delta: metabolism /
                      Protein Kinase Inhibitors: pharmacology / RNA Interference /
                      RNA, Messenger: metabolism / Receptor, PAR-1: metabolism /
                      Receptors, Thrombin: genetics / Receptors, Thrombin:
                      metabolism / Thrombin: metabolism / Time Factors /
                      Transcriptional Activation / Tumor Necrosis Factor-alpha:
                      genetics / Up-Regulation / NF-kappa B (NLM Chemicals) /
                      Protein Kinase Inhibitors (NLM Chemicals) / RNA, Messenger
                      (NLM Chemicals) / Receptor, PAR-1 (NLM Chemicals) /
                      Receptors, Thrombin (NLM Chemicals) / Tumor Necrosis
                      Factor-alpha (NLM Chemicals) / protease-activated receptor 3
                      (NLM Chemicals) / protease-activated receptor 4 (NLM
                      Chemicals) / Glucose (NLM Chemicals) / Calcium (NLM
                      Chemicals) / protein kinase C beta (NLM Chemicals) / PRKCD
                      protein, human (NLM Chemicals) / Protein Kinase C (NLM
                      Chemicals) / Protein Kinase C-delta (NLM Chemicals) /
                      Thrombin (NLM Chemicals) / J (WoSType)},
      cin          = {ISB-1},
      ddc          = {610},
      cid          = {I:(DE-Juel1)VDB922},
      pnm          = {BioSoft: Makromolekulare Systeme und biologische
                      Informationsverarbeitung},
      pid          = {G:(DE-Juel1)FUEK505},
      shelfmark    = {Hematology / Peripheral Vascular Disease},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:21164077},
      UT           = {WOS:000287409900023},
      doi          = {10.1161/ATVBAHA.110.219105},
      url          = {https://juser.fz-juelich.de/record/14547},
}