Pattern of chick gene activation in chick erythrocyte heterokaryons
The reactivation of chicken erythrocyte nuclei in chick-mammalian heterokaryons resulted in the activation of chick globin gene expression. However, the level of chick globin synthesis was dependent on the mammalian parental cell type. The level of globin synthesis was high in chick erythrocyte-rat...
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| Veröffentlicht in: | The Journal of cell biology 1982-12, Vol.95 (3), p.885-892 |
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| container_title | The Journal of cell biology |
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| creator | Linder, S Zuckerman, S.H Ringertz, N.R |
| description | The reactivation of chicken erythrocyte nuclei in chick-mammalian heterokaryons resulted in the activation of chick globin gene expression. However, the level of chick globin synthesis was dependent on the mammalian parental cell type. The level of globin synthesis was high in chick erythrocyte-rat L6 myoblast heterokaryons but was 10-fold lower in chick erythrocyte-mouse A9 cell heterokaryons. Heterokaryons between chick erythrocytes and a hybrid cell line between L6 and A9 expressed chick globin at a level similar to that of A9 heterokaryons. Erythrocyte nuclei reactivated in murine NA neuroblastoma, 3T3, BHK and NRK cells, or in chicken fibroblasts expressed |
| doi_str_mv | 10.1083/jcb.95.3.885 |
| format | Article |
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However, the level of chick globin synthesis was dependent on the mammalian parental cell type. The level of globin synthesis was high in chick erythrocyte-rat L6 myoblast heterokaryons but was 10-fold lower in chick erythrocyte-mouse A9 cell heterokaryons. Heterokaryons between chick erythrocytes and a hybrid cell line between L6 and A9 expressed chick globin at a level similar to that of A9 heterokaryons. Erythrocyte nuclei reactivated in murine NA neuroblastoma, 3T3, BHK and NRK cells, or in chicken fibroblasts expressed <5% chick globin compared with the chick erythrocyte-L6 myoblast heterokaryons. The amount of globin expressed in heterokaryons correlated with globin mRNA levels. Hemin increased beta globin synthesis two- to threefold in chick erythrocyte-NA neuroblastoma heterokaryons; however, total globin synthesis was still <10% that of L6 heterokaryons. Distinct from the variability in globin expression, chick erythrocyte heterokaryons synthesized chick constitutive polypeptides in similar amounts independent of the mammalian parental cell type. ∼40 constitutive chick polypeptides were detected in heterokaryons after immunopurification and two-dimensional gel electrophoresis. The pattern of synthesis of these polypeptides was similar in heterokaryons formed by fusing chicken erythrocytes with rat L6 myoblasts, hamster BHK cells, or mouse neuroblastoma cells. Three polypeptides synthesized by non-erythroid chicken cells but less so by embryonic erythrocytes were conspicuous in heterokaryons. Two abundant erythrocyte polypeptides were insignificant in non-erythroid chicken cells and in heterokaryons.</description><identifier>ISSN: 0021-9525</identifier><identifier>EISSN: 1540-8140</identifier><identifier>DOI: 10.1083/jcb.95.3.885</identifier><identifier>PMID: 7153250</identifier><language>eng</language><publisher>United States: Rockefeller University Press</publisher><subject>Animals ; Blood Proteins - biosynthesis ; Blood Proteins - genetics ; Cell Line ; Cell lines ; Cells ; Chickens ; Chickens - blood ; Chickens - genetics ; Cricetinae ; Embryonic cells ; Embryos ; Erythrocytes ; Erythrocytes - metabolism ; Gels ; Gene Expression Regulation ; Globins - biosynthesis ; Globins - genetics ; Hemin - pharmacology ; Heterokaryon ; Hybrid Cells ; Mice ; Myoblasts ; Neurons ; Rats ; RNA, Messenger - metabolism ; Transcriptional Activation</subject><ispartof>The Journal of cell biology, 1982-12, Vol.95 (3), p.885-892</ispartof><rights>Copyright 1982 The Rockefeller University Press</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c450t-4eef86e691c61d49f93274a4f0fc96f35df7658f0dcb1779737c19fc707693a73</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>230,314,776,780,881,27903,27904</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/7153250$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Linder, S</creatorcontrib><creatorcontrib>Zuckerman, S.H</creatorcontrib><creatorcontrib>Ringertz, N.R</creatorcontrib><title>Pattern of chick gene activation in chick erythrocyte heterokaryons</title><title>The Journal of cell biology</title><addtitle>J Cell Biol</addtitle><description>The reactivation of chicken erythrocyte nuclei in chick-mammalian heterokaryons resulted in the activation of chick globin gene expression. However, the level of chick globin synthesis was dependent on the mammalian parental cell type. The level of globin synthesis was high in chick erythrocyte-rat L6 myoblast heterokaryons but was 10-fold lower in chick erythrocyte-mouse A9 cell heterokaryons. Heterokaryons between chick erythrocytes and a hybrid cell line between L6 and A9 expressed chick globin at a level similar to that of A9 heterokaryons. Erythrocyte nuclei reactivated in murine NA neuroblastoma, 3T3, BHK and NRK cells, or in chicken fibroblasts expressed <5% chick globin compared with the chick erythrocyte-L6 myoblast heterokaryons. The amount of globin expressed in heterokaryons correlated with globin mRNA levels. Hemin increased beta globin synthesis two- to threefold in chick erythrocyte-NA neuroblastoma heterokaryons; however, total globin synthesis was still <10% that of L6 heterokaryons. Distinct from the variability in globin expression, chick erythrocyte heterokaryons synthesized chick constitutive polypeptides in similar amounts independent of the mammalian parental cell type. ∼40 constitutive chick polypeptides were detected in heterokaryons after immunopurification and two-dimensional gel electrophoresis. The pattern of synthesis of these polypeptides was similar in heterokaryons formed by fusing chicken erythrocytes with rat L6 myoblasts, hamster BHK cells, or mouse neuroblastoma cells. Three polypeptides synthesized by non-erythroid chicken cells but less so by embryonic erythrocytes were conspicuous in heterokaryons. Two abundant erythrocyte polypeptides were insignificant in non-erythroid chicken cells and in heterokaryons.</description><subject>Animals</subject><subject>Blood Proteins - biosynthesis</subject><subject>Blood Proteins - genetics</subject><subject>Cell Line</subject><subject>Cell lines</subject><subject>Cells</subject><subject>Chickens</subject><subject>Chickens - blood</subject><subject>Chickens - genetics</subject><subject>Cricetinae</subject><subject>Embryonic cells</subject><subject>Embryos</subject><subject>Erythrocytes</subject><subject>Erythrocytes - metabolism</subject><subject>Gels</subject><subject>Gene Expression Regulation</subject><subject>Globins - biosynthesis</subject><subject>Globins - genetics</subject><subject>Hemin - pharmacology</subject><subject>Heterokaryon</subject><subject>Hybrid Cells</subject><subject>Mice</subject><subject>Myoblasts</subject><subject>Neurons</subject><subject>Rats</subject><subject>RNA, Messenger - metabolism</subject><subject>Transcriptional Activation</subject><issn>0021-9525</issn><issn>1540-8140</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1982</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkU2LUzEUhoMoYx3duRKFu3LlrefkOxtBil8woKCzDmmatOm0N2OSDvTfG2kZdeXqLJ4nL-fkJeQ5whxBs7dbv5wbMWdzrcUDMkPBYdTI4SGZAVAcjaDiMXlS6xYAuOLsglwoFIwKmJHFN9daKNOQ4-A3yd8M6zCFwfmW7lxLeRrSdAahHNumZH9sYdiE_ijfuHLMU31KHkW3q-HZeV6S648ffiw-j1dfP31ZvL8aPRfQRh5C1DJIg17iiptoGFXc8QjRGxmZWEUlhY6w8ktUyiimPJroFShpmFPskrw75d4elvuw8mFqxe3sbUn7vojNLtl_yZQ2dp3vLEWkhkIPeH0OKPnnIdRm96n6sNu5KeRDtRqoECDlf0VkgoGQ2MU3J9GXXGsJ8X4bBPu7HdvbsUZYZns7XX_19wX38rmOzl-e-La2XP5kSQSUuuMXJxxdtm5dUrXX3zUVyPoH_QLdnJ1v</recordid><startdate>19821201</startdate><enddate>19821201</enddate><creator>Linder, S</creator><creator>Zuckerman, S.H</creator><creator>Ringertz, N.R</creator><general>Rockefeller University Press</general><general>The Rockefeller University Press</general><scope>FBQ</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>7TM</scope><scope>8FD</scope><scope>FR3</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>19821201</creationdate><title>Pattern of chick gene activation in chick erythrocyte heterokaryons</title><author>Linder, S ; Zuckerman, S.H ; Ringertz, N.R</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c450t-4eef86e691c61d49f93274a4f0fc96f35df7658f0dcb1779737c19fc707693a73</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1982</creationdate><topic>Animals</topic><topic>Blood Proteins - biosynthesis</topic><topic>Blood Proteins - genetics</topic><topic>Cell Line</topic><topic>Cell lines</topic><topic>Cells</topic><topic>Chickens</topic><topic>Chickens - blood</topic><topic>Chickens - genetics</topic><topic>Cricetinae</topic><topic>Embryonic cells</topic><topic>Embryos</topic><topic>Erythrocytes</topic><topic>Erythrocytes - metabolism</topic><topic>Gels</topic><topic>Gene Expression Regulation</topic><topic>Globins - biosynthesis</topic><topic>Globins - genetics</topic><topic>Hemin - pharmacology</topic><topic>Heterokaryon</topic><topic>Hybrid Cells</topic><topic>Mice</topic><topic>Myoblasts</topic><topic>Neurons</topic><topic>Rats</topic><topic>RNA, Messenger - metabolism</topic><topic>Transcriptional Activation</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Linder, S</creatorcontrib><creatorcontrib>Zuckerman, S.H</creatorcontrib><creatorcontrib>Ringertz, N.R</creatorcontrib><collection>AGRIS</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Nucleic Acids Abstracts</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><collection>PubMed Central (Full Participant titles)</collection><jtitle>The Journal of cell biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Linder, S</au><au>Zuckerman, S.H</au><au>Ringertz, N.R</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Pattern of chick gene activation in chick erythrocyte heterokaryons</atitle><jtitle>The Journal of cell biology</jtitle><addtitle>J Cell Biol</addtitle><date>1982-12-01</date><risdate>1982</risdate><volume>95</volume><issue>3</issue><spage>885</spage><epage>892</epage><pages>885-892</pages><issn>0021-9525</issn><eissn>1540-8140</eissn><abstract>The reactivation of chicken erythrocyte nuclei in chick-mammalian heterokaryons resulted in the activation of chick globin gene expression. However, the level of chick globin synthesis was dependent on the mammalian parental cell type. The level of globin synthesis was high in chick erythrocyte-rat L6 myoblast heterokaryons but was 10-fold lower in chick erythrocyte-mouse A9 cell heterokaryons. Heterokaryons between chick erythrocytes and a hybrid cell line between L6 and A9 expressed chick globin at a level similar to that of A9 heterokaryons. Erythrocyte nuclei reactivated in murine NA neuroblastoma, 3T3, BHK and NRK cells, or in chicken fibroblasts expressed <5% chick globin compared with the chick erythrocyte-L6 myoblast heterokaryons. The amount of globin expressed in heterokaryons correlated with globin mRNA levels. Hemin increased beta globin synthesis two- to threefold in chick erythrocyte-NA neuroblastoma heterokaryons; however, total globin synthesis was still <10% that of L6 heterokaryons. Distinct from the variability in globin expression, chick erythrocyte heterokaryons synthesized chick constitutive polypeptides in similar amounts independent of the mammalian parental cell type. ∼40 constitutive chick polypeptides were detected in heterokaryons after immunopurification and two-dimensional gel electrophoresis. The pattern of synthesis of these polypeptides was similar in heterokaryons formed by fusing chicken erythrocytes with rat L6 myoblasts, hamster BHK cells, or mouse neuroblastoma cells. Three polypeptides synthesized by non-erythroid chicken cells but less so by embryonic erythrocytes were conspicuous in heterokaryons. Two abundant erythrocyte polypeptides were insignificant in non-erythroid chicken cells and in heterokaryons.</abstract><cop>United States</cop><pub>Rockefeller University Press</pub><pmid>7153250</pmid><doi>10.1083/jcb.95.3.885</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | The Journal of cell biology, 1982-12, Vol.95 (3), p.885-892 |
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| language | eng |
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| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
| subjects | Animals Blood Proteins - biosynthesis Blood Proteins - genetics Cell Line Cell lines Cells Chickens Chickens - blood Chickens - genetics Cricetinae Embryonic cells Embryos Erythrocytes Erythrocytes - metabolism Gels Gene Expression Regulation Globins - biosynthesis Globins - genetics Hemin - pharmacology Heterokaryon Hybrid Cells Mice Myoblasts Neurons Rats RNA, Messenger - metabolism Transcriptional Activation |
| title | Pattern of chick gene activation in chick erythrocyte heterokaryons |
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