Eintrag weiter verarbeiten
Autoregulation of phospholipase D activity is coupled to selective induction of phospholipase D1 expression to promote invasion of breast cancer cells
Gespeichert in:
Zeitschriftentitel: | International Journal of Cancer |
---|---|
Personen und Körperschaften: | , , , , , , |
In: | International Journal of Cancer, 128, 2011, 4, S. 805-816 |
Format: | E-Article |
Sprache: | Englisch |
veröffentlicht: |
Wiley
|
Schlagwörter: |
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 |
doi_str_mv |
10.1002/ijc.25402 |
facet_avail |
Online Free |
finc_class_facet |
Medizin |
format |
ElectronicArticle |
fullrecord |
blob:ai-49-aHR0cDovL2R4LmRvaS5vcmcvMTAuMTAwMi9pamMuMjU0MDI |
id |
ai-49-aHR0cDovL2R4LmRvaS5vcmcvMTAuMTAwMi9pamMuMjU0MDI |
institution |
DE-15 DE-Pl11 DE-Rs1 DE-105 DE-14 DE-Ch1 DE-L229 DE-D275 DE-Bn3 DE-Brt1 DE-Zwi2 DE-D161 DE-Gla1 DE-Zi4 |
imprint |
Wiley, 2011 |
imprint_str_mv |
Wiley, 2011 |
issn |
0020-7136 1097-0215 |
issn_str_mv |
0020-7136 1097-0215 |
language |
English |
mega_collection |
Wiley (CrossRef) |
match_str |
kang2011autoregulationofphospholipasedactivityiscoupledtoselectiveinductionofphospholipased1expressiontopromoteinvasionofbreastcancercells |
publishDateSort |
2011 |
publisher |
Wiley |
recordtype |
ai |
record_format |
ai |
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> |
container_issue |
4 |
container_start_page |
805 |
container_title |
International Journal of Cancer |
container_volume |
128 |
format_de105 |
Article, E-Article |
format_de14 |
Article, E-Article |
format_de15 |
Article, E-Article |
format_de520 |
Article, E-Article |
format_de540 |
Article, E-Article |
format_dech1 |
Article, E-Article |
format_ded117 |
Article, E-Article |
format_degla1 |
E-Article |
format_del152 |
Buch |
format_del189 |
Article, E-Article |
format_dezi4 |
Article |
format_dezwi2 |
Article, E-Article |
format_finc |
Article, E-Article |
format_nrw |
Article, E-Article |
_version_ |
1792343171266510848 |
geogr_code |
not assigned |
last_indexed |
2024-03-01T16:47:00.706Z |
geogr_code_person |
not assigned |
openURL |
url_ver=Z39.88-2004&ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fvufind.svn.sourceforge.net%3Agenerator&rft.title=Autoregulation+of+phospholipase+D+activity+is+coupled+to+selective+induction+of+phospholipase+D1+expression+to+promote+invasion+of+breast+cancer+cells&rft.date=2011-02-15&genre=article&issn=1097-0215&volume=128&issue=4&spage=805&epage=816&pages=805-816&jtitle=International+Journal+of+Cancer&atitle=Autoregulation+of+phospholipase+D+activity+is+coupled+to+selective+induction+of+phospholipase+D1+expression+to+promote+invasion+of+breast+cancer+cells&aulast=Min&aufirst=Do+Sik&rft_id=info%3Adoi%2F10.1002%2Fijc.25402&rft.language%5B0%5D=eng |
SOLR | |
_version_ | 1792343171266510848 |
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> |
doi_str_mv | 10.1002/ijc.25402 |
facet_avail | Online, Free |
finc_class_facet | Medizin |
format | ElectronicArticle |
format_de105 | Article, E-Article |
format_de14 | Article, E-Article |
format_de15 | Article, E-Article |
format_de520 | Article, E-Article |
format_de540 | Article, E-Article |
format_dech1 | Article, E-Article |
format_ded117 | Article, E-Article |
format_degla1 | E-Article |
format_del152 | Buch |
format_del189 | Article, E-Article |
format_dezi4 | Article |
format_dezwi2 | Article, E-Article |
format_finc | Article, E-Article |
format_nrw | Article, E-Article |
geogr_code | not assigned |
geogr_code_person | not assigned |
id | ai-49-aHR0cDovL2R4LmRvaS5vcmcvMTAuMTAwMi9pamMuMjU0MDI |
imprint | Wiley, 2011 |
imprint_str_mv | Wiley, 2011 |
institution | DE-15, DE-Pl11, DE-Rs1, DE-105, DE-14, DE-Ch1, DE-L229, DE-D275, DE-Bn3, DE-Brt1, DE-Zwi2, DE-D161, DE-Gla1, DE-Zi4 |
issn | 0020-7136, 1097-0215 |
issn_str_mv | 0020-7136, 1097-0215 |
language | English |
last_indexed | 2024-03-01T16:47:00.706Z |
match_str | kang2011autoregulationofphospholipasedactivityiscoupledtoselectiveinductionofphospholipased1expressiontopromoteinvasionofbreastcancercells |
mega_collection | Wiley (CrossRef) |
physical | 805-816 |
publishDate | 2011 |
publishDateSort | 2011 |
publisher | Wiley |
record_format | ai |
recordtype | ai |
series | International Journal of Cancer |
source_id | 49 |
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 |