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@ARTICLE{vomDahl:32540,
      author       = {vom Dahl, S. and Schliess, F. and Reissmann, R. and Görg,
                      B. and Weiergräber, O. and Kocalkova, M. and Dombrowski, F.
                      and Häussinger, D.},
      title        = {{I}nvolvement of integrins in osmosensing and signaling
                      towards autophagic proteolysis in rat liver},
      journal      = {The journal of biological chemistry},
      volume       = {278},
      issn         = {0021-9258},
      address      = {Bethesda, Md.},
      publisher    = {Soc.},
      reportid     = {PreJuSER-32540},
      pages        = {27088 - 27095},
      year         = {2003},
      note         = {Record converted from VDB: 12.11.2012},
      abstract     = {Inhibition of autophagic proteolysis by hypoosmotic or
                      amino acid-induced hepatocyte swelling requires
                      osmosignaling toward p38MAPK; however, the upstream
                      osmosensing and signaling events are unknown. These were
                      studied in the intact perfused rat liver with a preserved in
                      situ environment of hepatocytes. It was found that
                      hypoosmotic hepatocyte swelling led to an activation of Src
                      (but not FAK), Erks, and p38MAPK, which was prevented by the
                      integrin inhibitory hexapeptide GRGDSP, but not its inactive
                      analogue GRGESP. Src inhibition by PP-2 prevented
                      hypoosmotic MAP kinase activation, indicating that the
                      integrin/Src system is located upstream in the osmosignaling
                      toward p38MAPK and Erks. Inhibition of the integrin/Src
                      system by the RGD motif-containing peptide or PP-2 also
                      prevented the inhibition of proteolysis and the decrease in
                      autophagic vacuole volume, which is otherwise observed in
                      response to hypoosmotic or glutamine/glycine-induced
                      hepatocyte swelling. These inhibitors, however, did not
                      affect swelling-independent proteolysis inhibition by
                      phenylalanine. In line with a role of p38MAPK in triggering
                      the volume regulatory decrease (RVD), PP-2 and the RGD
                      peptide blunted RVD in response to hypoosmotic cell
                      swelling. The data identify integrins and Src as upstream
                      events in the osmosignaling toward MAP kinases, proteolysis,
                      and RVD. They further point to a role of integrins as osmo-
                      and mechanosensors in the intact liver, which may provide a
                      link between cell volume and cell function.},
      keywords     = {Animals / Autophagy / Cell Size: drug effects / Cell Size:
                      physiology / Cells, Cultured / Hepatocytes: cytology /
                      Hepatocytes: drug effects / Hepatocytes: physiology /
                      Integrins: antagonists $\&$ inhibitors / Integrins:
                      physiology / Liver: drug effects / Liver: physiology /
                      Liver: ultrastructure / MAP Kinase Signaling System / Male /
                      Mitogen-Activated Protein Kinases: metabolism / Models,
                      Biological / Oligopeptides: pharmacology / Perfusion / Rats
                      / Rats, Wistar / Signal Transduction / Water-Electrolyte
                      Balance: physiology / p38 Mitogen-Activated Protein Kinases
                      / src-Family Kinases: antagonists $\&$ inhibitors /
                      src-Family Kinases: metabolism / Integrins (NLM Chemicals) /
                      Oligopeptides (NLM Chemicals) /
                      glycyl-arginyl-glycyl-aspartyl-seryl-proline (NLM Chemicals)
                      / arginyl-glycyl-aspartic acid (NLM Chemicals) /
                      glycyl-arginyl-glycyl-glutamyl-seryl-proline (NLM Chemicals)
                      / src-Family Kinases (NLM Chemicals) / Mitogen-Activated
                      Protein Kinases (NLM Chemicals) / p38 Mitogen-Activated
                      Protein Kinases (NLM Chemicals) / J (WoSType)},
      cin          = {IBI-2},
      ddc          = {570},
      cid          = {I:(DE-Juel1)VDB58},
      pnm          = {Neurowissenschaften},
      pid          = {G:(DE-Juel1)FUEK255},
      shelfmark    = {Biochemistry $\&$ Molecular Biology},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:12721289},
      UT           = {WOS:000184155700102},
      doi          = {10.1074/jbc.M210699200},
      url          = {https://juser.fz-juelich.de/record/32540},
}