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Patrick M Mcdonough - One of the best experts on this subject based on the ideXlab platform.

  • Phorbol Myristate acetate induced hypertrophy of neonatal rat cardiac myocytes is associated with decreased sarcoplasmic reticulum ca2 atpase serca2 gene expression and calcium reuptake
    Journal of Molecular and Cellular Cardiology, 1996
    Co-Authors: Ron Hartong, Francisco Villarreal, Frank Giordano, Randa Hilaldandan, Patrick M Mcdonough
    Abstract:

    The decreased expression of the sarcoplasmic reticulum Ca2+-ATPase associated with cardiac hypertrophy was investigated in cultured neonatal rat cardiac myocytes. Northern blot analysis indicated a significant 55–60% decrease in Ca2+-ATPase mRNA levels and after 12 and 24 h of treatment with the Phorbol ester Phorbol Myristate acetate (PMA). Myocytes treated with the Phorbol ester for 80 h showed a significant 34% decrease (relative to vehicle-treated control cells) in the levels of Ca2+-ATPase protein, and a significant 38% increase in the levels ofα-sarcomeric actin, as assessed by Western blot analysis using specific antibodies. Immunocytochemistry of myocytes treated for 72 h with the Phorbol ester revealed a hypertrophied cell morphology, and showed a marked decrease in Ca2+-ATPase staining intensity. Contractile calcium transients were evaluated through the use of indo-1. It was found that thet1/2for the decline of calcium transient was significantly prolonged by PMA treatment (0.51±0.15) when compared to controls (0.38±0.17,P<0.001). Treatment of myocytes with endothelin-1 also led to a 35% decrease in sarcoplasmic reticulum Ca2+-ATPase mRNA levels. It is concluded that Phorbol ester treatment of neonatal rat cardiac myocytes induces similar changes in Ca2+-ATPase gene expression as observedin vivoin the hypertrophied and failing heart. The observed prolongation int1/2for [Ca2+]idecline might be due to the observed depressed levels for sarcoplasmic reticulum Ca2+-ATPase in PMA treated cells.

  • Phorbol Myristate acetate induced hypertrophy of neonatal rat cardiac myocytes is associated with decreased sarcoplasmic reticulum ca2 atpase serca2 gene expression and calcium reuptake
    Journal of Molecular and Cellular Cardiology, 1996
    Co-Authors: Ron Hartong, Francisco Villarreal, Frank Giordano, Randa Hilaldandan, Patrick M Mcdonough, Wolfgang H Dillmann
    Abstract:

    The decreased expression of the sarcoplasmic reticulum Ca(2+)-ATPase associated with cardiac hypertrophy was investigated in cultured neonatal rat cardiac myocytes. Northern blot analysis indicated a significant 55-60% decrease in Ca(2+)-ATPase mRNA levels and after 12 and 24 h of treatment with the Phorbol ester Phorbol Myristate acetate (PMA). Myocytes treated with the Phorbol ester for 80 h showed a significant 34% decrease (relative to vehicle-treated control cells) in the levels of Ca(2+)-ATPase protein, and a significant 38% increase in the levels of alpha-sarcomeric actin, as assessed by Western blot analysis using specific antibodies. Immunocytochemistry of myocytes treated for 72 h with the Phorbol ester revealed a hypertrophied cell morphology, and showed a marked decrease in Ca(2+)-ATPase staining intensity. Contractile calcium transients were evaluated through the use of indo-1. It was found that the t1/2 for the decline of calcium transient was significantly prolonged by PMA treatment (0.51 +/- 0.15) when compared to controls (0.38 +/- 0.17, P < 0.001). Treatment of myocytes with endothelin-1 also led to a 35% decrease in sarcoplasmic reticulum Ca(2+)-ATPase mRNA levels. It is concluded that Phorbol ester treatment of neonatal rat cardiac myocytes induces similar changes in Ca(2+)-ATPase mRNA levels. It is concluded that Phorbol ester treatment of neonatal rat cardiac myocytes induces similar changes in Ca(2+)-ATPase gene expression as observed in vivo in the hypertrophied and failing heart. The observed prolongation in t1/2 for [Ca2+]i decline might be due to the observed depressed levels for sarcoplasmic reticulum Ca(2+)-ATPase in PMA treated cells.

Ron Hartong - One of the best experts on this subject based on the ideXlab platform.

  • Phorbol Myristate acetate induced hypertrophy of neonatal rat cardiac myocytes is associated with decreased sarcoplasmic reticulum ca2 atpase serca2 gene expression and calcium reuptake
    Journal of Molecular and Cellular Cardiology, 1996
    Co-Authors: Ron Hartong, Francisco Villarreal, Frank Giordano, Randa Hilaldandan, Patrick M Mcdonough
    Abstract:

    The decreased expression of the sarcoplasmic reticulum Ca2+-ATPase associated with cardiac hypertrophy was investigated in cultured neonatal rat cardiac myocytes. Northern blot analysis indicated a significant 55–60% decrease in Ca2+-ATPase mRNA levels and after 12 and 24 h of treatment with the Phorbol ester Phorbol Myristate acetate (PMA). Myocytes treated with the Phorbol ester for 80 h showed a significant 34% decrease (relative to vehicle-treated control cells) in the levels of Ca2+-ATPase protein, and a significant 38% increase in the levels ofα-sarcomeric actin, as assessed by Western blot analysis using specific antibodies. Immunocytochemistry of myocytes treated for 72 h with the Phorbol ester revealed a hypertrophied cell morphology, and showed a marked decrease in Ca2+-ATPase staining intensity. Contractile calcium transients were evaluated through the use of indo-1. It was found that thet1/2for the decline of calcium transient was significantly prolonged by PMA treatment (0.51±0.15) when compared to controls (0.38±0.17,P<0.001). Treatment of myocytes with endothelin-1 also led to a 35% decrease in sarcoplasmic reticulum Ca2+-ATPase mRNA levels. It is concluded that Phorbol ester treatment of neonatal rat cardiac myocytes induces similar changes in Ca2+-ATPase gene expression as observedin vivoin the hypertrophied and failing heart. The observed prolongation int1/2for [Ca2+]idecline might be due to the observed depressed levels for sarcoplasmic reticulum Ca2+-ATPase in PMA treated cells.

  • Phorbol Myristate acetate induced hypertrophy of neonatal rat cardiac myocytes is associated with decreased sarcoplasmic reticulum ca2 atpase serca2 gene expression and calcium reuptake
    Journal of Molecular and Cellular Cardiology, 1996
    Co-Authors: Ron Hartong, Francisco Villarreal, Frank Giordano, Randa Hilaldandan, Patrick M Mcdonough, Wolfgang H Dillmann
    Abstract:

    The decreased expression of the sarcoplasmic reticulum Ca(2+)-ATPase associated with cardiac hypertrophy was investigated in cultured neonatal rat cardiac myocytes. Northern blot analysis indicated a significant 55-60% decrease in Ca(2+)-ATPase mRNA levels and after 12 and 24 h of treatment with the Phorbol ester Phorbol Myristate acetate (PMA). Myocytes treated with the Phorbol ester for 80 h showed a significant 34% decrease (relative to vehicle-treated control cells) in the levels of Ca(2+)-ATPase protein, and a significant 38% increase in the levels of alpha-sarcomeric actin, as assessed by Western blot analysis using specific antibodies. Immunocytochemistry of myocytes treated for 72 h with the Phorbol ester revealed a hypertrophied cell morphology, and showed a marked decrease in Ca(2+)-ATPase staining intensity. Contractile calcium transients were evaluated through the use of indo-1. It was found that the t1/2 for the decline of calcium transient was significantly prolonged by PMA treatment (0.51 +/- 0.15) when compared to controls (0.38 +/- 0.17, P < 0.001). Treatment of myocytes with endothelin-1 also led to a 35% decrease in sarcoplasmic reticulum Ca(2+)-ATPase mRNA levels. It is concluded that Phorbol ester treatment of neonatal rat cardiac myocytes induces similar changes in Ca(2+)-ATPase mRNA levels. It is concluded that Phorbol ester treatment of neonatal rat cardiac myocytes induces similar changes in Ca(2+)-ATPase gene expression as observed in vivo in the hypertrophied and failing heart. The observed prolongation in t1/2 for [Ca2+]i decline might be due to the observed depressed levels for sarcoplasmic reticulum Ca(2+)-ATPase in PMA treated cells.

Francisco Villarreal - One of the best experts on this subject based on the ideXlab platform.

  • Phorbol Myristate acetate induced hypertrophy of neonatal rat cardiac myocytes is associated with decreased sarcoplasmic reticulum ca2 atpase serca2 gene expression and calcium reuptake
    Journal of Molecular and Cellular Cardiology, 1996
    Co-Authors: Ron Hartong, Francisco Villarreal, Frank Giordano, Randa Hilaldandan, Patrick M Mcdonough
    Abstract:

    The decreased expression of the sarcoplasmic reticulum Ca2+-ATPase associated with cardiac hypertrophy was investigated in cultured neonatal rat cardiac myocytes. Northern blot analysis indicated a significant 55–60% decrease in Ca2+-ATPase mRNA levels and after 12 and 24 h of treatment with the Phorbol ester Phorbol Myristate acetate (PMA). Myocytes treated with the Phorbol ester for 80 h showed a significant 34% decrease (relative to vehicle-treated control cells) in the levels of Ca2+-ATPase protein, and a significant 38% increase in the levels ofα-sarcomeric actin, as assessed by Western blot analysis using specific antibodies. Immunocytochemistry of myocytes treated for 72 h with the Phorbol ester revealed a hypertrophied cell morphology, and showed a marked decrease in Ca2+-ATPase staining intensity. Contractile calcium transients were evaluated through the use of indo-1. It was found that thet1/2for the decline of calcium transient was significantly prolonged by PMA treatment (0.51±0.15) when compared to controls (0.38±0.17,P<0.001). Treatment of myocytes with endothelin-1 also led to a 35% decrease in sarcoplasmic reticulum Ca2+-ATPase mRNA levels. It is concluded that Phorbol ester treatment of neonatal rat cardiac myocytes induces similar changes in Ca2+-ATPase gene expression as observedin vivoin the hypertrophied and failing heart. The observed prolongation int1/2for [Ca2+]idecline might be due to the observed depressed levels for sarcoplasmic reticulum Ca2+-ATPase in PMA treated cells.

  • Phorbol Myristate acetate induced hypertrophy of neonatal rat cardiac myocytes is associated with decreased sarcoplasmic reticulum ca2 atpase serca2 gene expression and calcium reuptake
    Journal of Molecular and Cellular Cardiology, 1996
    Co-Authors: Ron Hartong, Francisco Villarreal, Frank Giordano, Randa Hilaldandan, Patrick M Mcdonough, Wolfgang H Dillmann
    Abstract:

    The decreased expression of the sarcoplasmic reticulum Ca(2+)-ATPase associated with cardiac hypertrophy was investigated in cultured neonatal rat cardiac myocytes. Northern blot analysis indicated a significant 55-60% decrease in Ca(2+)-ATPase mRNA levels and after 12 and 24 h of treatment with the Phorbol ester Phorbol Myristate acetate (PMA). Myocytes treated with the Phorbol ester for 80 h showed a significant 34% decrease (relative to vehicle-treated control cells) in the levels of Ca(2+)-ATPase protein, and a significant 38% increase in the levels of alpha-sarcomeric actin, as assessed by Western blot analysis using specific antibodies. Immunocytochemistry of myocytes treated for 72 h with the Phorbol ester revealed a hypertrophied cell morphology, and showed a marked decrease in Ca(2+)-ATPase staining intensity. Contractile calcium transients were evaluated through the use of indo-1. It was found that the t1/2 for the decline of calcium transient was significantly prolonged by PMA treatment (0.51 +/- 0.15) when compared to controls (0.38 +/- 0.17, P < 0.001). Treatment of myocytes with endothelin-1 also led to a 35% decrease in sarcoplasmic reticulum Ca(2+)-ATPase mRNA levels. It is concluded that Phorbol ester treatment of neonatal rat cardiac myocytes induces similar changes in Ca(2+)-ATPase mRNA levels. It is concluded that Phorbol ester treatment of neonatal rat cardiac myocytes induces similar changes in Ca(2+)-ATPase gene expression as observed in vivo in the hypertrophied and failing heart. The observed prolongation in t1/2 for [Ca2+]i decline might be due to the observed depressed levels for sarcoplasmic reticulum Ca(2+)-ATPase in PMA treated cells.

Randa Hilaldandan - One of the best experts on this subject based on the ideXlab platform.

  • Phorbol Myristate acetate induced hypertrophy of neonatal rat cardiac myocytes is associated with decreased sarcoplasmic reticulum ca2 atpase serca2 gene expression and calcium reuptake
    Journal of Molecular and Cellular Cardiology, 1996
    Co-Authors: Ron Hartong, Francisco Villarreal, Frank Giordano, Randa Hilaldandan, Patrick M Mcdonough
    Abstract:

    The decreased expression of the sarcoplasmic reticulum Ca2+-ATPase associated with cardiac hypertrophy was investigated in cultured neonatal rat cardiac myocytes. Northern blot analysis indicated a significant 55–60% decrease in Ca2+-ATPase mRNA levels and after 12 and 24 h of treatment with the Phorbol ester Phorbol Myristate acetate (PMA). Myocytes treated with the Phorbol ester for 80 h showed a significant 34% decrease (relative to vehicle-treated control cells) in the levels of Ca2+-ATPase protein, and a significant 38% increase in the levels ofα-sarcomeric actin, as assessed by Western blot analysis using specific antibodies. Immunocytochemistry of myocytes treated for 72 h with the Phorbol ester revealed a hypertrophied cell morphology, and showed a marked decrease in Ca2+-ATPase staining intensity. Contractile calcium transients were evaluated through the use of indo-1. It was found that thet1/2for the decline of calcium transient was significantly prolonged by PMA treatment (0.51±0.15) when compared to controls (0.38±0.17,P<0.001). Treatment of myocytes with endothelin-1 also led to a 35% decrease in sarcoplasmic reticulum Ca2+-ATPase mRNA levels. It is concluded that Phorbol ester treatment of neonatal rat cardiac myocytes induces similar changes in Ca2+-ATPase gene expression as observedin vivoin the hypertrophied and failing heart. The observed prolongation int1/2for [Ca2+]idecline might be due to the observed depressed levels for sarcoplasmic reticulum Ca2+-ATPase in PMA treated cells.

  • Phorbol Myristate acetate induced hypertrophy of neonatal rat cardiac myocytes is associated with decreased sarcoplasmic reticulum ca2 atpase serca2 gene expression and calcium reuptake
    Journal of Molecular and Cellular Cardiology, 1996
    Co-Authors: Ron Hartong, Francisco Villarreal, Frank Giordano, Randa Hilaldandan, Patrick M Mcdonough, Wolfgang H Dillmann
    Abstract:

    The decreased expression of the sarcoplasmic reticulum Ca(2+)-ATPase associated with cardiac hypertrophy was investigated in cultured neonatal rat cardiac myocytes. Northern blot analysis indicated a significant 55-60% decrease in Ca(2+)-ATPase mRNA levels and after 12 and 24 h of treatment with the Phorbol ester Phorbol Myristate acetate (PMA). Myocytes treated with the Phorbol ester for 80 h showed a significant 34% decrease (relative to vehicle-treated control cells) in the levels of Ca(2+)-ATPase protein, and a significant 38% increase in the levels of alpha-sarcomeric actin, as assessed by Western blot analysis using specific antibodies. Immunocytochemistry of myocytes treated for 72 h with the Phorbol ester revealed a hypertrophied cell morphology, and showed a marked decrease in Ca(2+)-ATPase staining intensity. Contractile calcium transients were evaluated through the use of indo-1. It was found that the t1/2 for the decline of calcium transient was significantly prolonged by PMA treatment (0.51 +/- 0.15) when compared to controls (0.38 +/- 0.17, P < 0.001). Treatment of myocytes with endothelin-1 also led to a 35% decrease in sarcoplasmic reticulum Ca(2+)-ATPase mRNA levels. It is concluded that Phorbol ester treatment of neonatal rat cardiac myocytes induces similar changes in Ca(2+)-ATPase mRNA levels. It is concluded that Phorbol ester treatment of neonatal rat cardiac myocytes induces similar changes in Ca(2+)-ATPase gene expression as observed in vivo in the hypertrophied and failing heart. The observed prolongation in t1/2 for [Ca2+]i decline might be due to the observed depressed levels for sarcoplasmic reticulum Ca(2+)-ATPase in PMA treated cells.

Frank Giordano - One of the best experts on this subject based on the ideXlab platform.

  • Phorbol Myristate acetate induced hypertrophy of neonatal rat cardiac myocytes is associated with decreased sarcoplasmic reticulum ca2 atpase serca2 gene expression and calcium reuptake
    Journal of Molecular and Cellular Cardiology, 1996
    Co-Authors: Ron Hartong, Francisco Villarreal, Frank Giordano, Randa Hilaldandan, Patrick M Mcdonough
    Abstract:

    The decreased expression of the sarcoplasmic reticulum Ca2+-ATPase associated with cardiac hypertrophy was investigated in cultured neonatal rat cardiac myocytes. Northern blot analysis indicated a significant 55–60% decrease in Ca2+-ATPase mRNA levels and after 12 and 24 h of treatment with the Phorbol ester Phorbol Myristate acetate (PMA). Myocytes treated with the Phorbol ester for 80 h showed a significant 34% decrease (relative to vehicle-treated control cells) in the levels of Ca2+-ATPase protein, and a significant 38% increase in the levels ofα-sarcomeric actin, as assessed by Western blot analysis using specific antibodies. Immunocytochemistry of myocytes treated for 72 h with the Phorbol ester revealed a hypertrophied cell morphology, and showed a marked decrease in Ca2+-ATPase staining intensity. Contractile calcium transients were evaluated through the use of indo-1. It was found that thet1/2for the decline of calcium transient was significantly prolonged by PMA treatment (0.51±0.15) when compared to controls (0.38±0.17,P<0.001). Treatment of myocytes with endothelin-1 also led to a 35% decrease in sarcoplasmic reticulum Ca2+-ATPase mRNA levels. It is concluded that Phorbol ester treatment of neonatal rat cardiac myocytes induces similar changes in Ca2+-ATPase gene expression as observedin vivoin the hypertrophied and failing heart. The observed prolongation int1/2for [Ca2+]idecline might be due to the observed depressed levels for sarcoplasmic reticulum Ca2+-ATPase in PMA treated cells.

  • Phorbol Myristate acetate induced hypertrophy of neonatal rat cardiac myocytes is associated with decreased sarcoplasmic reticulum ca2 atpase serca2 gene expression and calcium reuptake
    Journal of Molecular and Cellular Cardiology, 1996
    Co-Authors: Ron Hartong, Francisco Villarreal, Frank Giordano, Randa Hilaldandan, Patrick M Mcdonough, Wolfgang H Dillmann
    Abstract:

    The decreased expression of the sarcoplasmic reticulum Ca(2+)-ATPase associated with cardiac hypertrophy was investigated in cultured neonatal rat cardiac myocytes. Northern blot analysis indicated a significant 55-60% decrease in Ca(2+)-ATPase mRNA levels and after 12 and 24 h of treatment with the Phorbol ester Phorbol Myristate acetate (PMA). Myocytes treated with the Phorbol ester for 80 h showed a significant 34% decrease (relative to vehicle-treated control cells) in the levels of Ca(2+)-ATPase protein, and a significant 38% increase in the levels of alpha-sarcomeric actin, as assessed by Western blot analysis using specific antibodies. Immunocytochemistry of myocytes treated for 72 h with the Phorbol ester revealed a hypertrophied cell morphology, and showed a marked decrease in Ca(2+)-ATPase staining intensity. Contractile calcium transients were evaluated through the use of indo-1. It was found that the t1/2 for the decline of calcium transient was significantly prolonged by PMA treatment (0.51 +/- 0.15) when compared to controls (0.38 +/- 0.17, P < 0.001). Treatment of myocytes with endothelin-1 also led to a 35% decrease in sarcoplasmic reticulum Ca(2+)-ATPase mRNA levels. It is concluded that Phorbol ester treatment of neonatal rat cardiac myocytes induces similar changes in Ca(2+)-ATPase mRNA levels. It is concluded that Phorbol ester treatment of neonatal rat cardiac myocytes induces similar changes in Ca(2+)-ATPase gene expression as observed in vivo in the hypertrophied and failing heart. The observed prolongation in t1/2 for [Ca2+]i decline might be due to the observed depressed levels for sarcoplasmic reticulum Ca(2+)-ATPase in PMA treated cells.