Overexpression and Activation of the Tyrosine Kinase Src in Human Pancreatic Carcinoma
Src family tyrosine kinases participate in the regulation of cell adhesion, cell growth and differentiation. Here, we examine for the first time the potential role of Src for growth regulation of human pancreatic carcinoma cells. By immunohistochemical analysis, Src was overexpressed in 13/13 pancre...
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| Veröffentlicht in: | Biochemical and biophysical research communications 1998-02, Vol.243 (2), p.503-508 |
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| creator | Lutz, Manfred P. Eßer, I.B.Silke Flossmann-Kast, Berenike B.M. Vogelmann, Roger Lührs, Hardi Friess, Helmut Büchler, Markus W. Adler, Guido |
| description | Src family tyrosine kinases participate in the regulation of cell adhesion, cell growth and differentiation. Here, we examine for the first time the potential role of Src for growth regulation of human pancreatic carcinoma cells. By immunohistochemical analysis, Src was overexpressed in 13/13 pancreatic carcinoma tissue but not in 6 normal pancreatic tissue specimen. In Western blots of total cellular extracts, Src protein expression was elevated in 14/17 carcinoma cell lines as compared to normal pancreas or cultured human pancreatic duct cells. Kinase activity was only detectable in cancer cells and did not correlate with the amount of kinase protein or with the expression of the regulatory kinase Csk, indicating that Src is not regulated through protein expression or through expression of Csk. The Src-specific tyrosine kinase inhibitor herbimycin A decreased cell growth in a dose-dependent manner. We suggest that Src family kinases participate in growth regulation of pancreatic cancer cells. |
| doi_str_mv | 10.1006/bbrc.1997.8043 |
| format | Article |
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Here, we examine for the first time the potential role of Src for growth regulation of human pancreatic carcinoma cells. By immunohistochemical analysis, Src was overexpressed in 13/13 pancreatic carcinoma tissue but not in 6 normal pancreatic tissue specimen. In Western blots of total cellular extracts, Src protein expression was elevated in 14/17 carcinoma cell lines as compared to normal pancreas or cultured human pancreatic duct cells. Kinase activity was only detectable in cancer cells and did not correlate with the amount of kinase protein or with the expression of the regulatory kinase Csk, indicating that Src is not regulated through protein expression or through expression of Csk. The Src-specific tyrosine kinase inhibitor herbimycin A decreased cell growth in a dose-dependent manner. We suggest that Src family kinases participate in growth regulation of pancreatic cancer cells.</description><identifier>ISSN: 0006-291X</identifier><identifier>EISSN: 1090-2104</identifier><identifier>DOI: 10.1006/bbrc.1997.8043</identifier><identifier>PMID: 9480838</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Aged ; Benzoquinones ; Cell Division - drug effects ; Enzyme Activation ; Enzyme Inhibitors - pharmacology ; Gene Expression Regulation, Neoplastic - genetics ; Humans ; Immunohistochemistry ; Lactams, Macrocyclic ; Middle Aged ; Neoplasm Staging ; Pancreatic Neoplasms - enzymology ; Pancreatic Neoplasms - pathology ; Protein-Tyrosine Kinases - analysis ; Proto-Oncogene Proteins pp60(c-src) - analysis ; Quinones - pharmacology ; Rifabutin - analogs & derivatives ; src-Family Kinases - genetics ; src-Family Kinases - metabolism ; Tumor Cells, Cultured</subject><ispartof>Biochemical and biophysical research communications, 1998-02, Vol.243 (2), p.503-508</ispartof><rights>1998 Academic Press</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c405t-cce1b7309ab17ffa0af9b7302d5479ecdb0058d9050cf993a21413a4c85df3253</citedby><cites>FETCH-LOGICAL-c405t-cce1b7309ab17ffa0af9b7302d5479ecdb0058d9050cf993a21413a4c85df3253</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1006/bbrc.1997.8043$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,778,782,3539,27907,27908,45978</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9480838$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Lutz, Manfred P.</creatorcontrib><creatorcontrib>Eßer, I.B.Silke</creatorcontrib><creatorcontrib>Flossmann-Kast, Berenike B.M.</creatorcontrib><creatorcontrib>Vogelmann, Roger</creatorcontrib><creatorcontrib>Lührs, Hardi</creatorcontrib><creatorcontrib>Friess, Helmut</creatorcontrib><creatorcontrib>Büchler, Markus W.</creatorcontrib><creatorcontrib>Adler, Guido</creatorcontrib><title>Overexpression and Activation of the Tyrosine Kinase Src in Human Pancreatic Carcinoma</title><title>Biochemical and biophysical research communications</title><addtitle>Biochem Biophys Res Commun</addtitle><description>Src family tyrosine kinases participate in the regulation of cell adhesion, cell growth and differentiation. Here, we examine for the first time the potential role of Src for growth regulation of human pancreatic carcinoma cells. By immunohistochemical analysis, Src was overexpressed in 13/13 pancreatic carcinoma tissue but not in 6 normal pancreatic tissue specimen. In Western blots of total cellular extracts, Src protein expression was elevated in 14/17 carcinoma cell lines as compared to normal pancreas or cultured human pancreatic duct cells. Kinase activity was only detectable in cancer cells and did not correlate with the amount of kinase protein or with the expression of the regulatory kinase Csk, indicating that Src is not regulated through protein expression or through expression of Csk. The Src-specific tyrosine kinase inhibitor herbimycin A decreased cell growth in a dose-dependent manner. We suggest that Src family kinases participate in growth regulation of pancreatic cancer cells.</description><subject>Aged</subject><subject>Benzoquinones</subject><subject>Cell Division - drug effects</subject><subject>Enzyme Activation</subject><subject>Enzyme Inhibitors - pharmacology</subject><subject>Gene Expression Regulation, Neoplastic - genetics</subject><subject>Humans</subject><subject>Immunohistochemistry</subject><subject>Lactams, Macrocyclic</subject><subject>Middle Aged</subject><subject>Neoplasm Staging</subject><subject>Pancreatic Neoplasms - enzymology</subject><subject>Pancreatic Neoplasms - pathology</subject><subject>Protein-Tyrosine Kinases - analysis</subject><subject>Proto-Oncogene Proteins pp60(c-src) - analysis</subject><subject>Quinones - pharmacology</subject><subject>Rifabutin - analogs & derivatives</subject><subject>src-Family Kinases - genetics</subject><subject>src-Family Kinases - metabolism</subject><subject>Tumor Cells, Cultured</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1998</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kE1LAzEQhoMotVav3oScvG2d7Ec3OZaiVixUsIq3kJ2dxUg3W5Ntsf_eXVq8eRpe5pkX5mHsWsBYAEzuisLjWCiVjyWkyQkbClAQxQLSUzaEjohiJT7O2UUIXwBCpBM1YAOVSpCJHLL35Y48_Ww8hWAbx40r-RRbuzNtH5uKt5_EV3vfBOuIP1tnAvFXj9w6Pt_WxvEX49BTxyOfGY_WNbW5ZGeVWQe6Os4Re3u4X83m0WL5-DSbLiJMIWsjRBJFnoAyhciryoCpVJ_jMktzRVgWAJksFWSAlVKJiUUqEpOizMoqibNkxG4PvRvffG8ptLq2AWm9No6abdC5yoWUOXTg-ABi90nwVOmNt7Xxey1A9yJ1L1L3InUvsju4OTZvi5rKP_xortvLw56693aWvA5oySGV1hO2umzsf9W_f1KCZw</recordid><startdate>19980213</startdate><enddate>19980213</enddate><creator>Lutz, Manfred P.</creator><creator>Eßer, I.B.Silke</creator><creator>Flossmann-Kast, Berenike B.M.</creator><creator>Vogelmann, Roger</creator><creator>Lührs, Hardi</creator><creator>Friess, Helmut</creator><creator>Büchler, Markus W.</creator><creator>Adler, Guido</creator><general>Elsevier Inc</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>19980213</creationdate><title>Overexpression and Activation of the Tyrosine Kinase Src in Human Pancreatic Carcinoma</title><author>Lutz, Manfred P. ; Eßer, I.B.Silke ; Flossmann-Kast, Berenike B.M. ; Vogelmann, Roger ; Lührs, Hardi ; Friess, Helmut ; Büchler, Markus W. ; Adler, Guido</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c405t-cce1b7309ab17ffa0af9b7302d5479ecdb0058d9050cf993a21413a4c85df3253</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1998</creationdate><topic>Aged</topic><topic>Benzoquinones</topic><topic>Cell Division - drug effects</topic><topic>Enzyme Activation</topic><topic>Enzyme Inhibitors - pharmacology</topic><topic>Gene Expression Regulation, Neoplastic - genetics</topic><topic>Humans</topic><topic>Immunohistochemistry</topic><topic>Lactams, Macrocyclic</topic><topic>Middle Aged</topic><topic>Neoplasm Staging</topic><topic>Pancreatic Neoplasms - enzymology</topic><topic>Pancreatic Neoplasms - pathology</topic><topic>Protein-Tyrosine Kinases - analysis</topic><topic>Proto-Oncogene Proteins pp60(c-src) - analysis</topic><topic>Quinones - pharmacology</topic><topic>Rifabutin - analogs & derivatives</topic><topic>src-Family Kinases - genetics</topic><topic>src-Family Kinases - metabolism</topic><topic>Tumor Cells, Cultured</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Lutz, Manfred P.</creatorcontrib><creatorcontrib>Eßer, I.B.Silke</creatorcontrib><creatorcontrib>Flossmann-Kast, Berenike B.M.</creatorcontrib><creatorcontrib>Vogelmann, Roger</creatorcontrib><creatorcontrib>Lührs, Hardi</creatorcontrib><creatorcontrib>Friess, Helmut</creatorcontrib><creatorcontrib>Büchler, Markus W.</creatorcontrib><creatorcontrib>Adler, Guido</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Lutz, Manfred P.</au><au>Eßer, I.B.Silke</au><au>Flossmann-Kast, Berenike B.M.</au><au>Vogelmann, Roger</au><au>Lührs, Hardi</au><au>Friess, Helmut</au><au>Büchler, Markus W.</au><au>Adler, Guido</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Overexpression and Activation of the Tyrosine Kinase Src in Human Pancreatic Carcinoma</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>1998-02-13</date><risdate>1998</risdate><volume>243</volume><issue>2</issue><spage>503</spage><epage>508</epage><pages>503-508</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><abstract>Src family tyrosine kinases participate in the regulation of cell adhesion, cell growth and differentiation. Here, we examine for the first time the potential role of Src for growth regulation of human pancreatic carcinoma cells. By immunohistochemical analysis, Src was overexpressed in 13/13 pancreatic carcinoma tissue but not in 6 normal pancreatic tissue specimen. In Western blots of total cellular extracts, Src protein expression was elevated in 14/17 carcinoma cell lines as compared to normal pancreas or cultured human pancreatic duct cells. Kinase activity was only detectable in cancer cells and did not correlate with the amount of kinase protein or with the expression of the regulatory kinase Csk, indicating that Src is not regulated through protein expression or through expression of Csk. The Src-specific tyrosine kinase inhibitor herbimycin A decreased cell growth in a dose-dependent manner. We suggest that Src family kinases participate in growth regulation of pancreatic cancer cells.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>9480838</pmid><doi>10.1006/bbrc.1997.8043</doi><tpages>6</tpages></addata></record> |
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| subjects | Aged Benzoquinones Cell Division - drug effects Enzyme Activation Enzyme Inhibitors - pharmacology Gene Expression Regulation, Neoplastic - genetics Humans Immunohistochemistry Lactams, Macrocyclic Middle Aged Neoplasm Staging Pancreatic Neoplasms - enzymology Pancreatic Neoplasms - pathology Protein-Tyrosine Kinases - analysis Proto-Oncogene Proteins pp60(c-src) - analysis Quinones - pharmacology Rifabutin - analogs & derivatives src-Family Kinases - genetics src-Family Kinases - metabolism Tumor Cells, Cultured |
| title | Overexpression and Activation of the Tyrosine Kinase Src in Human Pancreatic Carcinoma |
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