author_facet Kang, Dong Woo
Park, Mi Hee
Lee, Young Jun
Kim, Hyung Sik
Lindsley, Craig W.
Alex Brown, H.
Min, Do Sik
Kang, Dong Woo
Park, Mi Hee
Lee, Young Jun
Kim, Hyung Sik
Lindsley, Craig W.
Alex Brown, H.
Min, Do Sik
author Kang, Dong Woo
Park, Mi Hee
Lee, Young Jun
Kim, Hyung Sik
Lindsley, Craig W.
Alex Brown, H.
Min, Do Sik
spellingShingle Kang, Dong Woo
Park, Mi Hee
Lee, Young Jun
Kim, Hyung Sik
Lindsley, Craig W.
Alex Brown, H.
Min, Do Sik
International Journal of Cancer
Autoregulation of phospholipase D activity is coupled to selective induction of phospholipase D1 expression to promote invasion of breast cancer cells
Cancer Research
Oncology
author_sort kang, dong woo
spelling Kang, Dong Woo Park, Mi Hee Lee, Young Jun Kim, Hyung Sik Lindsley, Craig W. Alex Brown, H. Min, Do Sik 0020-7136 1097-0215 Wiley Cancer Research Oncology http://dx.doi.org/10.1002/ijc.25402 <jats:title>Abstract</jats:title><jats:p>Phospholipase D (PLD) is an important signaling enzyme implicated in the control of many biological processes, including cell proliferation and survival. Despite the importance of the duration and amplitude of PLD signaling in carcinogenesis, mechanisms that regulate PLD expression remain poorly understood. In our study, we define the regulatory components of the machinery that specifies selective PLD1 induction <jats:italic>via</jats:italic> signals propagated through PLD activity. We demonstrate for the first time that establishment of a positive feedback loop that is dependent on enzymatic activity originating from both PLD1 and PLD2 isozymes enhances selective expression of PLD1, but not PLD2. Phosphatidic acid, the product of PLD activity, leads to an increase in the Ras‐ERK/PI3K‐NFκB signaling cascade and enhances binding of NFκB to the PLD1 promoter, consequently inducing selective PLD1 expression in SK‐BR3 breast cancer cells. Moreover, selective PLD inhibitor suppressed epidermal growth factor‐induced matrix metalloproteinase upregulation and invasion by inhibiting PLD1 expression. In conclusion, we propose that autoregulation of PLD activity might be coupled to induction of PLD1 expression, and thereby play a role in carcinogenesis.</jats:p> Autoregulation of phospholipase D activity is coupled to selective induction of phospholipase D1 expression to promote invasion of breast cancer cells International Journal of Cancer
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series International Journal of Cancer
source_id 49
title Autoregulation of phospholipase D activity is coupled to selective induction of phospholipase D1 expression to promote invasion of breast cancer cells
title_unstemmed Autoregulation of phospholipase D activity is coupled to selective induction of phospholipase D1 expression to promote invasion of breast cancer cells
title_full Autoregulation of phospholipase D activity is coupled to selective induction of phospholipase D1 expression to promote invasion of breast cancer cells
title_fullStr Autoregulation of phospholipase D activity is coupled to selective induction of phospholipase D1 expression to promote invasion of breast cancer cells
title_full_unstemmed Autoregulation of phospholipase D activity is coupled to selective induction of phospholipase D1 expression to promote invasion of breast cancer cells
title_short Autoregulation of phospholipase D activity is coupled to selective induction of phospholipase D1 expression to promote invasion of breast cancer cells
title_sort autoregulation of phospholipase d activity is coupled to selective induction of phospholipase d1 expression to promote invasion of breast cancer cells
topic Cancer Research
Oncology
url http://dx.doi.org/10.1002/ijc.25402
publishDate 2011
physical 805-816
description <jats:title>Abstract</jats:title><jats:p>Phospholipase D (PLD) is an important signaling enzyme implicated in the control of many biological processes, including cell proliferation and survival. Despite the importance of the duration and amplitude of PLD signaling in carcinogenesis, mechanisms that regulate PLD expression remain poorly understood. In our study, we define the regulatory components of the machinery that specifies selective PLD1 induction <jats:italic>via</jats:italic> signals propagated through PLD activity. We demonstrate for the first time that establishment of a positive feedback loop that is dependent on enzymatic activity originating from both PLD1 and PLD2 isozymes enhances selective expression of PLD1, but not PLD2. Phosphatidic acid, the product of PLD activity, leads to an increase in the Ras‐ERK/PI3K‐NFκB signaling cascade and enhances binding of NFκB to the PLD1 promoter, consequently inducing selective PLD1 expression in SK‐BR3 breast cancer cells. Moreover, selective PLD inhibitor suppressed epidermal growth factor‐induced matrix metalloproteinase upregulation and invasion by inhibiting PLD1 expression. In conclusion, we propose that autoregulation of PLD activity might be coupled to induction of PLD1 expression, and thereby play a role in carcinogenesis.</jats:p>
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author Kang, Dong Woo, Park, Mi Hee, Lee, Young Jun, Kim, Hyung Sik, Lindsley, Craig W., Alex Brown, H., Min, Do Sik
author_facet Kang, Dong Woo, Park, Mi Hee, Lee, Young Jun, Kim, Hyung Sik, Lindsley, Craig W., Alex Brown, H., Min, Do Sik, Kang, Dong Woo, Park, Mi Hee, Lee, Young Jun, Kim, Hyung Sik, Lindsley, Craig W., Alex Brown, H., Min, Do Sik
author_sort kang, dong woo
container_issue 4
container_start_page 805
container_title International Journal of Cancer
container_volume 128
description <jats:title>Abstract</jats:title><jats:p>Phospholipase D (PLD) is an important signaling enzyme implicated in the control of many biological processes, including cell proliferation and survival. Despite the importance of the duration and amplitude of PLD signaling in carcinogenesis, mechanisms that regulate PLD expression remain poorly understood. In our study, we define the regulatory components of the machinery that specifies selective PLD1 induction <jats:italic>via</jats:italic> signals propagated through PLD activity. We demonstrate for the first time that establishment of a positive feedback loop that is dependent on enzymatic activity originating from both PLD1 and PLD2 isozymes enhances selective expression of PLD1, but not PLD2. Phosphatidic acid, the product of PLD activity, leads to an increase in the Ras‐ERK/PI3K‐NFκB signaling cascade and enhances binding of NFκB to the PLD1 promoter, consequently inducing selective PLD1 expression in SK‐BR3 breast cancer cells. Moreover, selective PLD inhibitor suppressed epidermal growth factor‐induced matrix metalloproteinase upregulation and invasion by inhibiting PLD1 expression. In conclusion, we propose that autoregulation of PLD activity might be coupled to induction of PLD1 expression, and thereby play a role in carcinogenesis.</jats:p>
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spelling Kang, Dong Woo Park, Mi Hee Lee, Young Jun Kim, Hyung Sik Lindsley, Craig W. Alex Brown, H. Min, Do Sik 0020-7136 1097-0215 Wiley Cancer Research Oncology http://dx.doi.org/10.1002/ijc.25402 <jats:title>Abstract</jats:title><jats:p>Phospholipase D (PLD) is an important signaling enzyme implicated in the control of many biological processes, including cell proliferation and survival. Despite the importance of the duration and amplitude of PLD signaling in carcinogenesis, mechanisms that regulate PLD expression remain poorly understood. In our study, we define the regulatory components of the machinery that specifies selective PLD1 induction <jats:italic>via</jats:italic> signals propagated through PLD activity. We demonstrate for the first time that establishment of a positive feedback loop that is dependent on enzymatic activity originating from both PLD1 and PLD2 isozymes enhances selective expression of PLD1, but not PLD2. Phosphatidic acid, the product of PLD activity, leads to an increase in the Ras‐ERK/PI3K‐NFκB signaling cascade and enhances binding of NFκB to the PLD1 promoter, consequently inducing selective PLD1 expression in SK‐BR3 breast cancer cells. Moreover, selective PLD inhibitor suppressed epidermal growth factor‐induced matrix metalloproteinase upregulation and invasion by inhibiting PLD1 expression. In conclusion, we propose that autoregulation of PLD activity might be coupled to induction of PLD1 expression, and thereby play a role in carcinogenesis.</jats:p> Autoregulation of phospholipase D activity is coupled to selective induction of phospholipase D1 expression to promote invasion of breast cancer cells International Journal of Cancer
spellingShingle Kang, Dong Woo, Park, Mi Hee, Lee, Young Jun, Kim, Hyung Sik, Lindsley, Craig W., Alex Brown, H., Min, Do Sik, International Journal of Cancer, Autoregulation of phospholipase D activity is coupled to selective induction of phospholipase D1 expression to promote invasion of breast cancer cells, Cancer Research, Oncology
title Autoregulation of phospholipase D activity is coupled to selective induction of phospholipase D1 expression to promote invasion of breast cancer cells
title_full Autoregulation of phospholipase D activity is coupled to selective induction of phospholipase D1 expression to promote invasion of breast cancer cells
title_fullStr Autoregulation of phospholipase D activity is coupled to selective induction of phospholipase D1 expression to promote invasion of breast cancer cells
title_full_unstemmed Autoregulation of phospholipase D activity is coupled to selective induction of phospholipase D1 expression to promote invasion of breast cancer cells
title_short Autoregulation of phospholipase D activity is coupled to selective induction of phospholipase D1 expression to promote invasion of breast cancer cells
title_sort autoregulation of phospholipase d activity is coupled to selective induction of phospholipase d1 expression to promote invasion of breast cancer cells
title_unstemmed Autoregulation of phospholipase D activity is coupled to selective induction of phospholipase D1 expression to promote invasion of breast cancer cells
topic Cancer Research, Oncology
url http://dx.doi.org/10.1002/ijc.25402