Silencing of casein kinase 2 inhibits PKC‑induced cell invasion by targeting MMP‑9 in MCF‑7 cells
Casein kinase 2 (CK2) is a serine/threonine protein kinase that has been considered to represent an important factor in mammary tumorigenesis. Increased expression of matrix metalloproteinase‑9 (MMP‑9) via nuclear factor‑κB (NF‑κB) activation has been demonstrated to promote breast cancer cell invas...
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| Veröffentlicht in: | Molecular medicine reports 2018-06, Vol.17 (6), p.8397-8402 |
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| container_title | Molecular medicine reports |
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| creator | Kim, Jeong-Mi Noh, Eun-Mi Song, Hyun-Kyung You, Yong-Ouk Jung, Sung Hoo Kim, Jong-Suk Kwon, Kang-Beom Lee, Young-Rae Youn, Hyun Jo |
| description | Casein kinase 2 (CK2) is a serine/threonine protein kinase that has been considered to represent an important factor in mammary tumorigenesis. Increased expression of matrix metalloproteinase‑9 (MMP‑9) via nuclear factor‑κB (NF‑κB) activation has been demonstrated to promote breast cancer cell invasion. In the present study, the involvement of CK2 in protein kinase C (PKC) induced cell invasion in MCF‑7 breast cancer cells was investigated as well as the underlying molecular mechanisms. The mRNA and protein levels of MMP‑9 in MCF‑7 cells were investigated using reverse transcription‑quantitative polymerase chain reaction, western blot analyses and a zymography assay. Cell invasiveness was investigated using a Matrigel invasion assay, and it was revealed that small interfering RNA specific for CK2 suppressed PKC induced cell invasion by regulating MMP‑9 expression via activation of the p38 kinase/c‑Jun N‑terminal kinase/NF‑κB pathway. In addition, it was demonstrated that CK2 inhibitors [apigenin (20 µM), emodin (20 µM) or 2‑dimethylamino‑4,5,6,7‑tetrabromo‑1H‑benzimidazole (2 µM)] suppressed PKC induced cell invasion and MMP‑9 expression. The results of the present study suggested that CK2 is an important factor involved in the induction of MCF‑7 breast cancer cell invasion by PKC. Therefore, CK2 may represent novel candidates for therapy intended to inhibit invasion in breast cancer. |
| doi_str_mv | 10.3892/mmr.2018.8885 |
| format | Article |
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Increased expression of matrix metalloproteinase‑9 (MMP‑9) via nuclear factor‑κB (NF‑κB) activation has been demonstrated to promote breast cancer cell invasion. In the present study, the involvement of CK2 in protein kinase C (PKC) induced cell invasion in MCF‑7 breast cancer cells was investigated as well as the underlying molecular mechanisms. The mRNA and protein levels of MMP‑9 in MCF‑7 cells were investigated using reverse transcription‑quantitative polymerase chain reaction, western blot analyses and a zymography assay. Cell invasiveness was investigated using a Matrigel invasion assay, and it was revealed that small interfering RNA specific for CK2 suppressed PKC induced cell invasion by regulating MMP‑9 expression via activation of the p38 kinase/c‑Jun N‑terminal kinase/NF‑κB pathway. In addition, it was demonstrated that CK2 inhibitors [apigenin (20 µM), emodin (20 µM) or 2‑dimethylamino‑4,5,6,7‑tetrabromo‑1H‑benzimidazole (2 µM)] suppressed PKC induced cell invasion and MMP‑9 expression. The results of the present study suggested that CK2 is an important factor involved in the induction of MCF‑7 breast cancer cell invasion by PKC. Therefore, CK2 may represent novel candidates for therapy intended to inhibit invasion in breast cancer.</description><identifier>ISSN: 1791-2997</identifier><identifier>EISSN: 1791-3004</identifier><identifier>DOI: 10.3892/mmr.2018.8885</identifier><identifier>PMID: 29658601</identifier><language>eng</language><publisher>Greece: Spandidos Publications</publisher><subject>Apoptosis ; Benzimidazoles ; Breast cancer ; c-Jun protein ; Cancer invasiveness ; Cancer research ; Casein ; Casein kinase II ; Cell cycle ; Cell division ; Development and progression ; Emodin ; Gelatinase B ; Health aspects ; Immunoglobulins ; Invasiveness ; JNK protein ; Kinases ; Matrix metalloproteinase ; Medical prognosis ; Metalloproteinase ; Metastasis ; Molecular modelling ; NF-κB protein ; Physiological aspects ; Polymerase chain reaction ; Proteases ; Protein expression ; Protein kinase C ; Protein kinases ; Protein-serine/threonine kinase ; Proteins ; Reverse transcription ; siRNA ; Studies ; Transcription factors ; Tumorigenesis</subject><ispartof>Molecular medicine reports, 2018-06, Vol.17 (6), p.8397-8402</ispartof><rights>COPYRIGHT 2018 Spandidos Publications</rights><rights>Copyright Spandidos Publications UK Ltd. 2018</rights><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c427t-47cd37b44836e5b85b829c5d5fd3c4e77c0ca791298152962a425f3b3acfa6bb3</citedby><cites>FETCH-LOGICAL-c427t-47cd37b44836e5b85b829c5d5fd3c4e77c0ca791298152962a425f3b3acfa6bb3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/29658601$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kim, Jeong-Mi</creatorcontrib><creatorcontrib>Noh, Eun-Mi</creatorcontrib><creatorcontrib>Song, Hyun-Kyung</creatorcontrib><creatorcontrib>You, Yong-Ouk</creatorcontrib><creatorcontrib>Jung, Sung Hoo</creatorcontrib><creatorcontrib>Kim, Jong-Suk</creatorcontrib><creatorcontrib>Kwon, Kang-Beom</creatorcontrib><creatorcontrib>Lee, Young-Rae</creatorcontrib><creatorcontrib>Youn, Hyun Jo</creatorcontrib><title>Silencing of casein kinase 2 inhibits PKC‑induced cell invasion by targeting MMP‑9 in MCF‑7 cells</title><title>Molecular medicine reports</title><addtitle>Mol Med Rep</addtitle><description>Casein kinase 2 (CK2) is a serine/threonine protein kinase that has been considered to represent an important factor in mammary tumorigenesis. Increased expression of matrix metalloproteinase‑9 (MMP‑9) via nuclear factor‑κB (NF‑κB) activation has been demonstrated to promote breast cancer cell invasion. In the present study, the involvement of CK2 in protein kinase C (PKC) induced cell invasion in MCF‑7 breast cancer cells was investigated as well as the underlying molecular mechanisms. The mRNA and protein levels of MMP‑9 in MCF‑7 cells were investigated using reverse transcription‑quantitative polymerase chain reaction, western blot analyses and a zymography assay. Cell invasiveness was investigated using a Matrigel invasion assay, and it was revealed that small interfering RNA specific for CK2 suppressed PKC induced cell invasion by regulating MMP‑9 expression via activation of the p38 kinase/c‑Jun N‑terminal kinase/NF‑κB pathway. In addition, it was demonstrated that CK2 inhibitors [apigenin (20 µM), emodin (20 µM) or 2‑dimethylamino‑4,5,6,7‑tetrabromo‑1H‑benzimidazole (2 µM)] suppressed PKC induced cell invasion and MMP‑9 expression. The results of the present study suggested that CK2 is an important factor involved in the induction of MCF‑7 breast cancer cell invasion by PKC. Therefore, CK2 may represent novel candidates for therapy intended to inhibit invasion in breast cancer.</description><subject>Apoptosis</subject><subject>Benzimidazoles</subject><subject>Breast cancer</subject><subject>c-Jun protein</subject><subject>Cancer invasiveness</subject><subject>Cancer research</subject><subject>Casein</subject><subject>Casein kinase II</subject><subject>Cell cycle</subject><subject>Cell division</subject><subject>Development and progression</subject><subject>Emodin</subject><subject>Gelatinase B</subject><subject>Health aspects</subject><subject>Immunoglobulins</subject><subject>Invasiveness</subject><subject>JNK protein</subject><subject>Kinases</subject><subject>Matrix metalloproteinase</subject><subject>Medical prognosis</subject><subject>Metalloproteinase</subject><subject>Metastasis</subject><subject>Molecular modelling</subject><subject>NF-κB protein</subject><subject>Physiological aspects</subject><subject>Polymerase chain reaction</subject><subject>Proteases</subject><subject>Protein expression</subject><subject>Protein kinase C</subject><subject>Protein kinases</subject><subject>Protein-serine/threonine kinase</subject><subject>Proteins</subject><subject>Reverse transcription</subject><subject>siRNA</subject><subject>Studies</subject><subject>Transcription factors</subject><subject>Tumorigenesis</subject><issn>1791-2997</issn><issn>1791-3004</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2018</creationdate><recordtype>article</recordtype><sourceid>BENPR</sourceid><recordid>eNptkc9u1DAQxi1ExZbCkSuyxIVLtv4Tx_axWtEWsatWAs6W4ziLl8QpdoK0N16hr9gnYUKXIqrKI3mk-c2nmfkQekPJkivNTvs-LRmhaqmUEs_QMZWaFpyQ8vkhZ1rLBXqZ846QSjChX6AF05VQFaHHaPs5dD66ELd4aLGz2YeIv4cICWY4xG-hDmPG159Wd79uQ2wm5xvsfNdB7afNYYi43uPRpq0fZ5HN5hpADVW8WZ1DKv_Q-RU6am2X_evDf4K-nn_4sros1lcXH1dn68KVTI5FKV3DZV2Wilde1AqCaSca0TbclV5KR5yFrZhWVMAWzJZMtLzm1rW2qmt-gt7f696k4cfk82j6kOcJbPTDlA0jTCjCBa8AffcI3Q1TijAdUFwJoalk_6it7bwJsR3GZN0sas5ESaWs4MpALZ-g4DW-D26IvoUz_99Q3De4NOScfGtuUuht2htKzGysAWPNbKyZjQX-7WHYqe5980D_dZL_BoeCnbY</recordid><startdate>20180601</startdate><enddate>20180601</enddate><creator>Kim, Jeong-Mi</creator><creator>Noh, Eun-Mi</creator><creator>Song, Hyun-Kyung</creator><creator>You, Yong-Ouk</creator><creator>Jung, Sung Hoo</creator><creator>Kim, Jong-Suk</creator><creator>Kwon, Kang-Beom</creator><creator>Lee, Young-Rae</creator><creator>Youn, Hyun Jo</creator><general>Spandidos Publications</general><general>Spandidos Publications UK Ltd</general><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8AO</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AN0</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M7P</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>7X8</scope></search><sort><creationdate>20180601</creationdate><title>Silencing of casein kinase 2 inhibits PKC‑induced cell invasion by targeting MMP‑9 in MCF‑7 cells</title><author>Kim, Jeong-Mi ; Noh, Eun-Mi ; Song, Hyun-Kyung ; You, Yong-Ouk ; Jung, Sung Hoo ; Kim, Jong-Suk ; Kwon, Kang-Beom ; Lee, Young-Rae ; Youn, Hyun Jo</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c427t-47cd37b44836e5b85b829c5d5fd3c4e77c0ca791298152962a425f3b3acfa6bb3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2018</creationdate><topic>Apoptosis</topic><topic>Benzimidazoles</topic><topic>Breast cancer</topic><topic>c-Jun protein</topic><topic>Cancer invasiveness</topic><topic>Cancer research</topic><topic>Casein</topic><topic>Casein kinase II</topic><topic>Cell cycle</topic><topic>Cell division</topic><topic>Development and progression</topic><topic>Emodin</topic><topic>Gelatinase B</topic><topic>Health aspects</topic><topic>Immunoglobulins</topic><topic>Invasiveness</topic><topic>JNK protein</topic><topic>Kinases</topic><topic>Matrix metalloproteinase</topic><topic>Medical prognosis</topic><topic>Metalloproteinase</topic><topic>Metastasis</topic><topic>Molecular modelling</topic><topic>NF-κB protein</topic><topic>Physiological aspects</topic><topic>Polymerase chain reaction</topic><topic>Proteases</topic><topic>Protein expression</topic><topic>Protein kinase C</topic><topic>Protein kinases</topic><topic>Protein-serine/threonine kinase</topic><topic>Proteins</topic><topic>Reverse transcription</topic><topic>siRNA</topic><topic>Studies</topic><topic>Transcription factors</topic><topic>Tumorigenesis</topic><toplevel>online_resources</toplevel><creatorcontrib>Kim, Jeong-Mi</creatorcontrib><creatorcontrib>Noh, Eun-Mi</creatorcontrib><creatorcontrib>Song, Hyun-Kyung</creatorcontrib><creatorcontrib>You, Yong-Ouk</creatorcontrib><creatorcontrib>Jung, Sung Hoo</creatorcontrib><creatorcontrib>Kim, Jong-Suk</creatorcontrib><creatorcontrib>Kwon, Kang-Beom</creatorcontrib><creatorcontrib>Lee, Young-Rae</creatorcontrib><creatorcontrib>Youn, Hyun Jo</creatorcontrib><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>British Nursing Database</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Biological Science Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>MEDLINE - Academic</collection><jtitle>Molecular medicine reports</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kim, Jeong-Mi</au><au>Noh, Eun-Mi</au><au>Song, Hyun-Kyung</au><au>You, Yong-Ouk</au><au>Jung, Sung Hoo</au><au>Kim, Jong-Suk</au><au>Kwon, Kang-Beom</au><au>Lee, Young-Rae</au><au>Youn, Hyun Jo</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Silencing of casein kinase 2 inhibits PKC‑induced cell invasion by targeting MMP‑9 in MCF‑7 cells</atitle><jtitle>Molecular medicine reports</jtitle><addtitle>Mol Med Rep</addtitle><date>2018-06-01</date><risdate>2018</risdate><volume>17</volume><issue>6</issue><spage>8397</spage><epage>8402</epage><pages>8397-8402</pages><issn>1791-2997</issn><eissn>1791-3004</eissn><abstract>Casein kinase 2 (CK2) is a serine/threonine protein kinase that has been considered to represent an important factor in mammary tumorigenesis. Increased expression of matrix metalloproteinase‑9 (MMP‑9) via nuclear factor‑κB (NF‑κB) activation has been demonstrated to promote breast cancer cell invasion. In the present study, the involvement of CK2 in protein kinase C (PKC) induced cell invasion in MCF‑7 breast cancer cells was investigated as well as the underlying molecular mechanisms. The mRNA and protein levels of MMP‑9 in MCF‑7 cells were investigated using reverse transcription‑quantitative polymerase chain reaction, western blot analyses and a zymography assay. Cell invasiveness was investigated using a Matrigel invasion assay, and it was revealed that small interfering RNA specific for CK2 suppressed PKC induced cell invasion by regulating MMP‑9 expression via activation of the p38 kinase/c‑Jun N‑terminal kinase/NF‑κB pathway. In addition, it was demonstrated that CK2 inhibitors [apigenin (20 µM), emodin (20 µM) or 2‑dimethylamino‑4,5,6,7‑tetrabromo‑1H‑benzimidazole (2 µM)] suppressed PKC induced cell invasion and MMP‑9 expression. The results of the present study suggested that CK2 is an important factor involved in the induction of MCF‑7 breast cancer cell invasion by PKC. Therefore, CK2 may represent novel candidates for therapy intended to inhibit invasion in breast cancer.</abstract><cop>Greece</cop><pub>Spandidos Publications</pub><pmid>29658601</pmid><doi>10.3892/mmr.2018.8885</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Apoptosis Benzimidazoles Breast cancer c-Jun protein Cancer invasiveness Cancer research Casein Casein kinase II Cell cycle Cell division Development and progression Emodin Gelatinase B Health aspects Immunoglobulins Invasiveness JNK protein Kinases Matrix metalloproteinase Medical prognosis Metalloproteinase Metastasis Molecular modelling NF-κB protein Physiological aspects Polymerase chain reaction Proteases Protein expression Protein kinase C Protein kinases Protein-serine/threonine kinase Proteins Reverse transcription siRNA Studies Transcription factors Tumorigenesis |
| title | Silencing of casein kinase 2 inhibits PKC‑induced cell invasion by targeting MMP‑9 in MCF‑7 cells |
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