Identification of 12-Lipoxygenase Interaction with Cellular Proteins by Yeast Two-Hybrid Screening
The platelet isoform of 12-lipoxygenase (12-LOX) is expressed in a variety of human tumors. 12-LOX metabolizes arachidonic acid to 12(S)-hydroxyeicosateraenoic acid (12(S)-HETE), which induces a number of cellular responses associated with tumor progression and metastasis. Little is known about 12-L...
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| Veröffentlicht in: | Biochemistry (Easton) 2000-03, Vol.39 (12), p.3185-3191 |
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| container_title | Biochemistry (Easton) |
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| creator | Tang, Keqin Finley, Russell L Nie, Daotai Honn, Kenneth V |
| description | The platelet isoform of 12-lipoxygenase (12-LOX) is expressed in a variety of human tumors. 12-LOX metabolizes arachidonic acid to 12(S)-hydroxyeicosateraenoic acid (12(S)-HETE), which induces a number of cellular responses associated with tumor progression and metastasis. Little is known about 12-LOX regulation and no direct regulators of 12-LOX activity have been identified. To identify potential regulators of 12-LOX, we isolated cDNAs encoding 12-LOX interacting proteins using the yeast two-hybrid system. We screened a yeast two-hybrid interaction library from human epidermoid carcinoma A431 cells and identified four cellular proteins that interact specifically with 12-LOX. We identified type II keratin 5, lamin A, the cytoplasmic domain of integrin β4 subunit and a phosphoprotein C8FW as 12-LOX interacting proteins. Here, we demonstrated that keratin 5, a 58 kD protein required for formation of 8 nm intermediate filaments, binds to 12-LOX in human tumor cells and may contribute to the regulated trafficking of 12-LOX. We also showed that lamin A binds 12-LOX in human tumor cells. These proteins provide the first candidate regulators of 12-LOX. |
| doi_str_mv | 10.1021/bi992664v |
| format | Article |
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Little is known about 12-LOX regulation and no direct regulators of 12-LOX activity have been identified. To identify potential regulators of 12-LOX, we isolated cDNAs encoding 12-LOX interacting proteins using the yeast two-hybrid system. We screened a yeast two-hybrid interaction library from human epidermoid carcinoma A431 cells and identified four cellular proteins that interact specifically with 12-LOX. We identified type II keratin 5, lamin A, the cytoplasmic domain of integrin β4 subunit and a phosphoprotein C8FW as 12-LOX interacting proteins. Here, we demonstrated that keratin 5, a 58 kD protein required for formation of 8 nm intermediate filaments, binds to 12-LOX in human tumor cells and may contribute to the regulated trafficking of 12-LOX. We also showed that lamin A binds 12-LOX in human tumor cells. These proteins provide the first candidate regulators of 12-LOX.</description><identifier>ISSN: 0006-2960</identifier><identifier>EISSN: 1520-4995</identifier><identifier>DOI: 10.1021/bi992664v</identifier><identifier>PMID: 10727209</identifier><language>eng</language><publisher>United States: American Chemical Society</publisher><subject>12-Lipoxygenase ; Antigens, CD - genetics ; Antigens, CD - metabolism ; Arachidonate 12-Lipoxygenase - blood ; Arachidonate 12-Lipoxygenase - genetics ; Arachidonate 12-Lipoxygenase - metabolism ; Blood Platelets - enzymology ; Cloning, Molecular ; Gene Library ; Humans ; Integrin beta4 ; Integrins - genetics ; Integrins - metabolism ; Isoenzymes - blood ; Isoenzymes - genetics ; Isoenzymes - metabolism ; Keratins - genetics ; Keratins - metabolism ; Lamin Type A ; Lamins ; Neoplasm Proteins - genetics ; Neoplasm Proteins - metabolism ; Nuclear Proteins - genetics ; Nuclear Proteins - metabolism ; Phosphoproteins - genetics ; Phosphoproteins - metabolism ; Saccharomyces cerevisiae - genetics ; Tumor Cells, Cultured ; Two-Hybrid System Techniques</subject><ispartof>Biochemistry (Easton), 2000-03, Vol.39 (12), p.3185-3191</ispartof><rights>Copyright © 2000 American Chemical Society</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a448t-e009f21e588398b47bc14b94e6170fe37e1e039e07956f2b0a56026fc5a301fb3</citedby><cites>FETCH-LOGICAL-a448t-e009f21e588398b47bc14b94e6170fe37e1e039e07956f2b0a56026fc5a301fb3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://pubs.acs.org/doi/pdf/10.1021/bi992664v$$EPDF$$P50$$Gacs$$H</linktopdf><linktohtml>$$Uhttps://pubs.acs.org/doi/10.1021/bi992664v$$EHTML$$P50$$Gacs$$H</linktohtml><link.rule.ids>314,776,780,2752,27053,27901,27902,56713,56763</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/10727209$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Tang, Keqin</creatorcontrib><creatorcontrib>Finley, Russell L</creatorcontrib><creatorcontrib>Nie, Daotai</creatorcontrib><creatorcontrib>Honn, Kenneth V</creatorcontrib><title>Identification of 12-Lipoxygenase Interaction with Cellular Proteins by Yeast Two-Hybrid Screening</title><title>Biochemistry (Easton)</title><addtitle>Biochemistry</addtitle><description>The platelet isoform of 12-lipoxygenase (12-LOX) is expressed in a variety of human tumors. 12-LOX metabolizes arachidonic acid to 12(S)-hydroxyeicosateraenoic acid (12(S)-HETE), which induces a number of cellular responses associated with tumor progression and metastasis. Little is known about 12-LOX regulation and no direct regulators of 12-LOX activity have been identified. To identify potential regulators of 12-LOX, we isolated cDNAs encoding 12-LOX interacting proteins using the yeast two-hybrid system. We screened a yeast two-hybrid interaction library from human epidermoid carcinoma A431 cells and identified four cellular proteins that interact specifically with 12-LOX. We identified type II keratin 5, lamin A, the cytoplasmic domain of integrin β4 subunit and a phosphoprotein C8FW as 12-LOX interacting proteins. Here, we demonstrated that keratin 5, a 58 kD protein required for formation of 8 nm intermediate filaments, binds to 12-LOX in human tumor cells and may contribute to the regulated trafficking of 12-LOX. We also showed that lamin A binds 12-LOX in human tumor cells. These proteins provide the first candidate regulators of 12-LOX.</description><subject>12-Lipoxygenase</subject><subject>Antigens, CD - genetics</subject><subject>Antigens, CD - metabolism</subject><subject>Arachidonate 12-Lipoxygenase - blood</subject><subject>Arachidonate 12-Lipoxygenase - genetics</subject><subject>Arachidonate 12-Lipoxygenase - metabolism</subject><subject>Blood Platelets - enzymology</subject><subject>Cloning, Molecular</subject><subject>Gene Library</subject><subject>Humans</subject><subject>Integrin beta4</subject><subject>Integrins - genetics</subject><subject>Integrins - metabolism</subject><subject>Isoenzymes - blood</subject><subject>Isoenzymes - genetics</subject><subject>Isoenzymes - metabolism</subject><subject>Keratins - genetics</subject><subject>Keratins - metabolism</subject><subject>Lamin Type A</subject><subject>Lamins</subject><subject>Neoplasm Proteins - genetics</subject><subject>Neoplasm Proteins - metabolism</subject><subject>Nuclear Proteins - genetics</subject><subject>Nuclear Proteins - metabolism</subject><subject>Phosphoproteins - genetics</subject><subject>Phosphoproteins - metabolism</subject><subject>Saccharomyces cerevisiae - genetics</subject><subject>Tumor Cells, Cultured</subject><subject>Two-Hybrid System Techniques</subject><issn>0006-2960</issn><issn>1520-4995</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2000</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqF0E1vEzEQBmALgWgoHPgDyBeQelgYe_0RH2lEaaQgihqEOFn2ZlxcEjvYu7T59yxsVXFAwpeRNY9mRi8hzxm8ZsDZGx-N4UqJnw_IjEkOjTBGPiQzAFANNwqOyJNar8evAC0ekyMGmmsOZkb8coOpjyF2ro850Rwo480q7vPt4QqTq0iXqcfiuj_tm9h_owvcboetK_Si5B5jqtQf6Fd0tafrm9ycH3yJG3rZFcQU09VT8ii4bcVnd_WYfD57t16cN6uP75eLt6vGCTHvGwQwgTOU83lr5l5o3zHhjUDFNARsNTKE1iBoI1XgHpxUwFXopGuBBd8ek1fT3H3JPwasvd3F2o23uoR5qFYzYOOT_4VMyxY0wAhPJtiVXGvBYPcl7lw5WAb2d_L2PvnRvrgbOvgdbv6SU9QjaCYQa4-3931XvlulWy3t-uLSKvlB8C-nyn4a_cvJu67a6zyUNIb3j8W_AB0dmKU</recordid><startdate>20000328</startdate><enddate>20000328</enddate><creator>Tang, Keqin</creator><creator>Finley, Russell L</creator><creator>Nie, Daotai</creator><creator>Honn, Kenneth V</creator><general>American Chemical Society</general><scope>BSCLL</scope><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>8FD</scope><scope>FR3</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>20000328</creationdate><title>Identification of 12-Lipoxygenase Interaction with Cellular Proteins by Yeast Two-Hybrid Screening</title><author>Tang, Keqin ; Finley, Russell L ; Nie, Daotai ; Honn, Kenneth V</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a448t-e009f21e588398b47bc14b94e6170fe37e1e039e07956f2b0a56026fc5a301fb3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2000</creationdate><topic>12-Lipoxygenase</topic><topic>Antigens, CD - genetics</topic><topic>Antigens, CD - metabolism</topic><topic>Arachidonate 12-Lipoxygenase - blood</topic><topic>Arachidonate 12-Lipoxygenase - genetics</topic><topic>Arachidonate 12-Lipoxygenase - metabolism</topic><topic>Blood Platelets - enzymology</topic><topic>Cloning, Molecular</topic><topic>Gene Library</topic><topic>Humans</topic><topic>Integrin beta4</topic><topic>Integrins - genetics</topic><topic>Integrins - metabolism</topic><topic>Isoenzymes - blood</topic><topic>Isoenzymes - genetics</topic><topic>Isoenzymes - metabolism</topic><topic>Keratins - genetics</topic><topic>Keratins - metabolism</topic><topic>Lamin Type A</topic><topic>Lamins</topic><topic>Neoplasm Proteins - genetics</topic><topic>Neoplasm Proteins - metabolism</topic><topic>Nuclear Proteins - genetics</topic><topic>Nuclear Proteins - metabolism</topic><topic>Phosphoproteins - genetics</topic><topic>Phosphoproteins - metabolism</topic><topic>Saccharomyces cerevisiae - genetics</topic><topic>Tumor Cells, Cultured</topic><topic>Two-Hybrid System Techniques</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Tang, Keqin</creatorcontrib><creatorcontrib>Finley, Russell L</creatorcontrib><creatorcontrib>Nie, Daotai</creatorcontrib><creatorcontrib>Honn, Kenneth V</creatorcontrib><collection>Istex</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Biochemistry (Easton)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Tang, Keqin</au><au>Finley, Russell L</au><au>Nie, Daotai</au><au>Honn, Kenneth V</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Identification of 12-Lipoxygenase Interaction with Cellular Proteins by Yeast Two-Hybrid Screening</atitle><jtitle>Biochemistry (Easton)</jtitle><addtitle>Biochemistry</addtitle><date>2000-03-28</date><risdate>2000</risdate><volume>39</volume><issue>12</issue><spage>3185</spage><epage>3191</epage><pages>3185-3191</pages><issn>0006-2960</issn><eissn>1520-4995</eissn><abstract>The platelet isoform of 12-lipoxygenase (12-LOX) is expressed in a variety of human tumors. 12-LOX metabolizes arachidonic acid to 12(S)-hydroxyeicosateraenoic acid (12(S)-HETE), which induces a number of cellular responses associated with tumor progression and metastasis. Little is known about 12-LOX regulation and no direct regulators of 12-LOX activity have been identified. To identify potential regulators of 12-LOX, we isolated cDNAs encoding 12-LOX interacting proteins using the yeast two-hybrid system. We screened a yeast two-hybrid interaction library from human epidermoid carcinoma A431 cells and identified four cellular proteins that interact specifically with 12-LOX. We identified type II keratin 5, lamin A, the cytoplasmic domain of integrin β4 subunit and a phosphoprotein C8FW as 12-LOX interacting proteins. Here, we demonstrated that keratin 5, a 58 kD protein required for formation of 8 nm intermediate filaments, binds to 12-LOX in human tumor cells and may contribute to the regulated trafficking of 12-LOX. We also showed that lamin A binds 12-LOX in human tumor cells. These proteins provide the first candidate regulators of 12-LOX.</abstract><cop>United States</cop><pub>American Chemical Society</pub><pmid>10727209</pmid><doi>10.1021/bi992664v</doi><tpages>7</tpages></addata></record> |
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| subjects | 12-Lipoxygenase Antigens, CD - genetics Antigens, CD - metabolism Arachidonate 12-Lipoxygenase - blood Arachidonate 12-Lipoxygenase - genetics Arachidonate 12-Lipoxygenase - metabolism Blood Platelets - enzymology Cloning, Molecular Gene Library Humans Integrin beta4 Integrins - genetics Integrins - metabolism Isoenzymes - blood Isoenzymes - genetics Isoenzymes - metabolism Keratins - genetics Keratins - metabolism Lamin Type A Lamins Neoplasm Proteins - genetics Neoplasm Proteins - metabolism Nuclear Proteins - genetics Nuclear Proteins - metabolism Phosphoproteins - genetics Phosphoproteins - metabolism Saccharomyces cerevisiae - genetics Tumor Cells, Cultured Two-Hybrid System Techniques |
| title | Identification of 12-Lipoxygenase Interaction with Cellular Proteins by Yeast Two-Hybrid Screening |
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