Platelet-derived growth factor-induced disruption of gap junctional communication and phosphorylation of connexin43 involves protein kinase C and mitogen-activated protein kinase
Previously we showed a rapid and transient inhibition of gap junctional communication (GJC) by platelet‐derived growth factor (PDGF) in T51B rat liver epithelial cells expressing wild‐type platelet‐derived growth factor β receptors (PDGFrβ). This action of PDGF correlated with the hyperphosphorylati...
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Published in | Journal of cellular physiology Vol. 176; no. 2; pp. 332 - 341 |
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Abstract | Previously we showed a rapid and transient inhibition of gap junctional communication (GJC) by platelet‐derived growth factor (PDGF) in T51B rat liver epithelial cells expressing wild‐type platelet‐derived growth factor β receptors (PDGFrβ). This action of PDGF correlated with the hyperphosphorylation of the gap junction protein connexin43 (Cx43) and required PDGFrβ tyrosine kinase activity, suggesting the participation of protein kinases and phosphatases many of which are activated by PDGF treatment. In the present study, two such kinases, namely protein kinase C (PKC) and mitogen‐activated protein kinase (MAPK), are investigated for their possible involvement in PDGF‐induced closure of junctional channels and Cx43‐phosphorylation. Down‐regulation of PKC‐isoforms by 12‐O‐tetradecanoylphorbol‐13‐acetate or pretreatment with the PKC inhibitor calphostin C, completely blocked PDGF action on GJC and Cx43. Activation of MAPK correlated with PDGF‐induced Cx43 phosphorylation, and prevention of MAPK activation by PD98059 eliminated the PDGF effects. Interestingly, elimination of GJC recovery by cycloheximide was associated with a sustained activated‐MAPK level. Based on these results we postulate that the activation of PKC and MAPK are required in PDGF‐mediated Cx43 phosphorylation and junctional closure. J. Cell. Physiol. 176:332–341, 1998. © 1998 Wiley‐Liss, Inc. |
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AbstractList | Previously we showed a rapid and transient inhibition of gap junctional communication (GJC) by platelet‐derived growth factor (PDGF) in T51B rat liver epithelial cells expressing wild‐type platelet‐derived growth factor β receptors (PDGFrβ). This action of PDGF correlated with the hyperphosphorylation of the gap junction protein connexin43 (Cx43) and required PDGFrβ tyrosine kinase activity, suggesting the participation of protein kinases and phosphatases many of which are activated by PDGF treatment. In the present study, two such kinases, namely protein kinase C (PKC) and mitogen‐activated protein kinase (MAPK), are investigated for their possible involvement in PDGF‐induced closure of junctional channels and Cx43‐phosphorylation. Down‐regulation of PKC‐isoforms by 12‐O‐tetradecanoylphorbol‐13‐acetate or pretreatment with the PKC inhibitor calphostin C, completely blocked PDGF action on GJC and Cx43. Activation of MAPK correlated with PDGF‐induced Cx43 phosphorylation, and prevention of MAPK activation by PD98059 eliminated the PDGF effects. Interestingly, elimination of GJC recovery by cycloheximide was associated with a sustained activated‐MAPK level. Based on these results we postulate that the activation of PKC and MAPK are required in PDGF‐mediated Cx43 phosphorylation and junctional closure. J. Cell. Physiol. 176:332–341, 1998. © 1998 Wiley‐Liss, Inc. Previously we showed a rapid and transient inhibition of gap junctional communication (GJC) by platelet-derived growth factor (PDGF) in T51B rat liver epithelial cells expressing wild-type platelet-derived growth factor beta receptors (PDGFrbeta). This action of PDGF correlated with the hyperphosphorylation of the gap junction protein connexin43 (Cx43) and required PDGFrbeta tyrosine kinase activity, suggesting the participation of protein kinases and phosphatases many of which are activated by PDGF treatment. In the present study, two such kinases, namely protein kinase C (PKC) and mitogen-activated protein kinase (MAPK), are investigated for their possible involvement in PDGF-induced closure of junctional channels and Cx43-phosphorylation. Down-regulation of PKC-isoforms by 12-O-tetradecanoylphorbol-13-acetate or pretreatment with the PKC inhibitor calphostin C, completely blocked PDGF action on GJC and Cx43. Activation of MAPK correlated with PDGF-induced Cx43 phosphorylation, and prevention of MAPK activation by PD98059 eliminated the PDGF effects. Interestingly, elimination of GJC recovery by cycloheximide was associated with a sustained activated-MAPK level. Based on these results we postulate that the activation of PKC and MAPK are required in PDGF-mediated Cx43 phosphorylation and junctional closure. |
Author | Hossain, Mohammad Z. Boynton, Alton L. Ao, Peng |
Author_xml | – sequence: 1 givenname: Mohammad Z. surname: Hossain fullname: Hossain, Mohammad Z. email: mhossain@nwhsea.org organization: Molecular Medicine, Northwest Hospital, Seattle, Washington – sequence: 2 givenname: Peng surname: Ao fullname: Ao, Peng organization: Molecular Medicine, Northwest Hospital, Seattle, Washington – sequence: 3 givenname: Alton L. surname: Boynton fullname: Boynton, Alton L. organization: Molecular Medicine, Northwest Hospital, Seattle, Washington |
BackLink | https://www.ncbi.nlm.nih.gov/pubmed/9648920$$D View this record in MEDLINE/PubMed |
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Snippet | Previously we showed a rapid and transient inhibition of gap junctional communication (GJC) by platelet‐derived growth factor (PDGF) in T51B rat liver... Previously we showed a rapid and transient inhibition of gap junctional communication (GJC) by platelet-derived growth factor (PDGF) in T51B rat liver... |
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SubjectTerms | Animals Calcium-Calmodulin-Dependent Protein Kinases - metabolism Carcinogens - pharmacology Cell Communication - drug effects Cell Communication - physiology Connexin 43 - metabolism Enzyme Inhibitors - pharmacology Epithelial Cells - chemistry Epithelial Cells - drug effects Epithelial Cells - enzymology Gap Junctions - drug effects Gap Junctions - physiology Liver - cytology Naphthalenes - pharmacology Phosphorylation Platelet-Derived Growth Factor - pharmacology Protein Kinase C - antagonists & inhibitors Protein Kinase C - metabolism Rats Tetradecanoylphorbol Acetate - pharmacology |
Title | Platelet-derived growth factor-induced disruption of gap junctional communication and phosphorylation of connexin43 involves protein kinase C and mitogen-activated protein kinase |
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