Kinetics of Steroid Induction and Deinduction of Tyrosine Aminotransferase Synthesis in Cultured Hepatoma Cells
The specific rate of synthesis of tyrosine aminotransferase (EC 2.6.1.5; L-tyrosine:2-oxoglutarate aminotransferase) is used as a measure of the level of functional, cytoplasmic, tyrosine aminotransferase-specific mRNA in cultured rat hepatoma cells. An analysis of the kinetics of change in this rat...
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| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 1975-06, Vol.72 (6), p.2007-2011 |
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| container_end_page | 2011 |
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| container_issue | 6 |
| container_start_page | 2007 |
| container_title | Proceedings of the National Academy of Sciences - PNAS |
| container_volume | 72 |
| creator | Steinberg, Robert A. Levinson, Barbara B. Tomkins, Gordon M. |
| description | The specific rate of synthesis of tyrosine aminotransferase (EC 2.6.1.5; L-tyrosine:2-oxoglutarate aminotransferase) is used as a measure of the level of functional, cytoplasmic, tyrosine aminotransferase-specific mRNA in cultured rat hepatoma cells. An analysis of the kinetics of change in this rate after the addition or withdrawal of glucocorticosteroids sets an upper limit on the half-life of the enzyme-specific mRNA of 1-1.5 hr, whether or not steroid is present. The inactivation rate of the enzyme mRNA is independent of the growth condition of the cells, occurring equally rapidly in the presence or absence of serum or insulin, both of which induce tyrosine aminotransferase in these cells. The implications of these results for the mechanism of steroid induction are discussed. |
| doi_str_mv | 10.1073/pnas.72.6.2007 |
| format | Article |
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An analysis of the kinetics of change in this rate after the addition or withdrawal of glucocorticosteroids sets an upper limit on the half-life of the enzyme-specific mRNA of 1-1.5 hr, whether or not steroid is present. The inactivation rate of the enzyme mRNA is independent of the growth condition of the cells, occurring equally rapidly in the presence or absence of serum or insulin, both of which induce tyrosine aminotransferase in these cells. 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An analysis of the kinetics of change in this rate after the addition or withdrawal of glucocorticosteroids sets an upper limit on the half-life of the enzyme-specific mRNA of 1-1.5 hr, whether or not steroid is present. The inactivation rate of the enzyme mRNA is independent of the growth condition of the cells, occurring equally rapidly in the presence or absence of serum or insulin, both of which induce tyrosine aminotransferase in these cells. The implications of these results for the mechanism of steroid induction are discussed.</description><subject>Animals</subject><subject>Blood</subject><subject>Carcinoma, Hepatocellular - enzymology</subject><subject>Carcinoma, Hepatocellular - metabolism</subject><subject>Cattle</subject><subject>Cells, Cultured</subject><subject>Computers</subject><subject>Cultured cells</subject><subject>Dexamethasone - pharmacology</subject><subject>Enzyme Induction - drug effects</subject><subject>Enzymes</subject><subject>Gene induction</subject><subject>Half lives</subject><subject>Insulin - pharmacology</subject><subject>Kinetics</subject><subject>Leucine - metabolism</subject><subject>Liver Neoplasms</subject><subject>Mathematical constants</subject><subject>Messenger RNA</subject><subject>Modeling</subject><subject>Models, Chemical</subject><subject>Precipitin Tests</subject><subject>Radioactive decay</subject><subject>Rats</subject><subject>RNA, Messenger - metabolism</subject><subject>Steroids</subject><subject>Tyrosine Transaminase - biosynthesis</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1975</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kTtvHCEUhVGU18ZOmyJKJCp3M-ExMFCksNZJbNlSCts1wsDEWDOwASbK_nsz2s3KaVwhdL4D954DwAeMWox6-mUTdG570vKWINS_ACuMJG54J9FLsEKI9I3oSPcWvMv5ASEkmUBvwGtCe8LFCsRLH1zxJsM4wOviUvQWXgQ7m-JjgDpYeOb84V6hm22KuZrg6eRDLEmHPLiks4PX21DuXfYZ-gDX81jm5Cw8dxtd4qTh2o1jPgavBj1m935_HoHb799u1ufN1c8fF-vTq8Z0jJVGSM6Y6CQjDBODHUHS8Z6THnVa4gFLQfRgjNVaMs4s5kRo01tLh5qJ4Hf0CHzdvbuZ7yZnjQt10lFtkp902qqovfpfCf5e_Yp_VEdrLrj6T_b-FH_PLhc1-WzqBjq4OGcliEQUowVsd6CpseTkhsMfGKmlILUUpHqiuFoKqoZPTyc74LtGqvx5Ly-2f-JT-8lzuhrmcSzub6ngxx34kEtMB5J3nFL6CDffrvU</recordid><startdate>19750601</startdate><enddate>19750601</enddate><creator>Steinberg, Robert A.</creator><creator>Levinson, Barbara B.</creator><creator>Tomkins, Gordon M.</creator><general>National Academy of Sciences of the United States of America</general><general>National Acad Sciences</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><scope>5PM</scope></search><sort><creationdate>19750601</creationdate><title>Kinetics of Steroid Induction and Deinduction of Tyrosine Aminotransferase Synthesis in Cultured Hepatoma Cells</title><author>Steinberg, Robert A. ; Levinson, Barbara B. ; Tomkins, Gordon M.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c455t-8965584952512c1e209e6762704a91f1982afccdaa9565d1628ac7dd3f10786b3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1975</creationdate><topic>Animals</topic><topic>Blood</topic><topic>Carcinoma, Hepatocellular - enzymology</topic><topic>Carcinoma, Hepatocellular - metabolism</topic><topic>Cattle</topic><topic>Cells, Cultured</topic><topic>Computers</topic><topic>Cultured cells</topic><topic>Dexamethasone - pharmacology</topic><topic>Enzyme Induction - drug effects</topic><topic>Enzymes</topic><topic>Gene induction</topic><topic>Half lives</topic><topic>Insulin - pharmacology</topic><topic>Kinetics</topic><topic>Leucine - metabolism</topic><topic>Liver Neoplasms</topic><topic>Mathematical constants</topic><topic>Messenger RNA</topic><topic>Modeling</topic><topic>Models, Chemical</topic><topic>Precipitin Tests</topic><topic>Radioactive decay</topic><topic>Rats</topic><topic>RNA, Messenger - metabolism</topic><topic>Steroids</topic><topic>Tyrosine Transaminase - biosynthesis</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Steinberg, Robert A.</creatorcontrib><creatorcontrib>Levinson, Barbara B.</creatorcontrib><creatorcontrib>Tomkins, Gordon M.</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><collection>PubMed Central (Full Participant titles)</collection><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Steinberg, Robert A.</au><au>Levinson, Barbara B.</au><au>Tomkins, Gordon M.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Kinetics of Steroid Induction and Deinduction of Tyrosine Aminotransferase Synthesis in Cultured Hepatoma Cells</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>1975-06-01</date><risdate>1975</risdate><volume>72</volume><issue>6</issue><spage>2007</spage><epage>2011</epage><pages>2007-2011</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><abstract>The specific rate of synthesis of tyrosine aminotransferase (EC 2.6.1.5; L-tyrosine:2-oxoglutarate aminotransferase) is used as a measure of the level of functional, cytoplasmic, tyrosine aminotransferase-specific mRNA in cultured rat hepatoma cells. An analysis of the kinetics of change in this rate after the addition or withdrawal of glucocorticosteroids sets an upper limit on the half-life of the enzyme-specific mRNA of 1-1.5 hr, whether or not steroid is present. The inactivation rate of the enzyme mRNA is independent of the growth condition of the cells, occurring equally rapidly in the presence or absence of serum or insulin, both of which induce tyrosine aminotransferase in these cells. The implications of these results for the mechanism of steroid induction are discussed.</abstract><cop>United States</cop><pub>National Academy of Sciences of the United States of America</pub><pmid>237268</pmid><doi>10.1073/pnas.72.6.2007</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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| identifier | ISSN: 0027-8424 |
| ispartof | Proceedings of the National Academy of Sciences - PNAS, 1975-06, Vol.72 (6), p.2007-2011 |
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| language | eng |
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| subjects | Animals Blood Carcinoma, Hepatocellular - enzymology Carcinoma, Hepatocellular - metabolism Cattle Cells, Cultured Computers Cultured cells Dexamethasone - pharmacology Enzyme Induction - drug effects Enzymes Gene induction Half lives Insulin - pharmacology Kinetics Leucine - metabolism Liver Neoplasms Mathematical constants Messenger RNA Modeling Models, Chemical Precipitin Tests Radioactive decay Rats RNA, Messenger - metabolism Steroids Tyrosine Transaminase - biosynthesis |
| title | Kinetics of Steroid Induction and Deinduction of Tyrosine Aminotransferase Synthesis in Cultured Hepatoma Cells |
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