Differential Prenylation of Proteins as a Function of Mevalonate Concentration in CHO Cells
The incorporation of [5- 3H]mevalonate into prenylated proteins and polyisoprenoid lipids has been determined as a function of mevalonate concentration in Chinese hamster ovary (CHO) cells that are inhibited in mevalonate synthesis. The relative incorporation of mevalonate into the different end pro...
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| Veröffentlicht in: | Archives of biochemistry and biophysics 1993-03, Vol.301 (2), p.210-215 |
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| container_title | Archives of biochemistry and biophysics |
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| creator | Rilling, H.C. Bruenger, E. Leining, L.M. Buss, J.E. Epstein, W.W. |
| description | The incorporation of [5-
3H]mevalonate into prenylated proteins and polyisoprenoid lipids has been determined as a function of mevalonate concentration in Chinese hamster ovary (CHO) cells that are inhibited in mevalonate synthesis. The relative incorporation of mevalonate into the different end products of isoprenoid metabolism was markedly dependent upon the concentration of mevalonate in the medium. The synthesis of cholesterol was dominant at higher concentrations of mevalonate while higher molecular weight isoprenoids were favored at the lower concentrations. The relative incorporation of mevalonate into the different prenylcysteines of prenylated proteins was dependent upon mevalonate concentration with geranylgeranylcysteine being the principal product at higher concentrations. At low levels of mevalonate farnesylcysteine synthesis predominated and geranylcysteine was detected. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of proteins from CHO cells that had been radiolabeled at different concentrations of [
3H]mevalonate had different patterns on fluorography with relatively few proteins labeled at low concentrations. A study of this effect on the prenylcysteines of a specific protein, Ras, showed considerably less sensitivity to mevalonate concentration than bulk protein. These results indicate that the specific proteins that are prenylated depend upon the availability of the isoprenyl diphosphate substrates. |
| doi_str_mv | 10.1006/abbi.1993.1135 |
| format | Article |
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3H]mevalonate into prenylated proteins and polyisoprenoid lipids has been determined as a function of mevalonate concentration in Chinese hamster ovary (CHO) cells that are inhibited in mevalonate synthesis. The relative incorporation of mevalonate into the different end products of isoprenoid metabolism was markedly dependent upon the concentration of mevalonate in the medium. The synthesis of cholesterol was dominant at higher concentrations of mevalonate while higher molecular weight isoprenoids were favored at the lower concentrations. The relative incorporation of mevalonate into the different prenylcysteines of prenylated proteins was dependent upon mevalonate concentration with geranylgeranylcysteine being the principal product at higher concentrations. At low levels of mevalonate farnesylcysteine synthesis predominated and geranylcysteine was detected. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of proteins from CHO cells that had been radiolabeled at different concentrations of [
3H]mevalonate had different patterns on fluorography with relatively few proteins labeled at low concentrations. A study of this effect on the prenylcysteines of a specific protein, Ras, showed considerably less sensitivity to mevalonate concentration than bulk protein. These results indicate that the specific proteins that are prenylated depend upon the availability of the isoprenyl diphosphate substrates.</description><identifier>ISSN: 0003-9861</identifier><identifier>EISSN: 1096-0384</identifier><identifier>DOI: 10.1006/abbi.1993.1135</identifier><identifier>PMID: 8460935</identifier><identifier>CODEN: ABBIA4</identifier><language>eng</language><publisher>San Diego, CA: Elsevier Inc</publisher><subject>Animals ; Biological and medical sciences ; CHO Cells ; Cholesterol - metabolism ; Cricetinae ; Cysteine - analogs & derivatives ; Cysteine - metabolism ; Diterpenes - metabolism ; Dose-Response Relationship, Drug ; Fundamental and applied biological sciences. Psychology ; Lipid Metabolism ; Lipoproteins - biosynthesis ; Mevalonic Acid - metabolism ; Molecular and cellular biology ; Molecular genetics ; Oncogene Protein p21(ras) - biosynthesis ; Protein Prenylation ; Translation. Translation factors. Protein processing</subject><ispartof>Archives of biochemistry and biophysics, 1993-03, Vol.301 (2), p.210-215</ispartof><rights>1993 Academic Press</rights><rights>1993 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c368t-9824ed856d74c9882990ccb7554d6ad2763127651c6116bee413ffbcfb5ba5cd3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0003986183711355$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=4663210$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8460935$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Rilling, H.C.</creatorcontrib><creatorcontrib>Bruenger, E.</creatorcontrib><creatorcontrib>Leining, L.M.</creatorcontrib><creatorcontrib>Buss, J.E.</creatorcontrib><creatorcontrib>Epstein, W.W.</creatorcontrib><title>Differential Prenylation of Proteins as a Function of Mevalonate Concentration in CHO Cells</title><title>Archives of biochemistry and biophysics</title><addtitle>Arch Biochem Biophys</addtitle><description>The incorporation of [5-
3H]mevalonate into prenylated proteins and polyisoprenoid lipids has been determined as a function of mevalonate concentration in Chinese hamster ovary (CHO) cells that are inhibited in mevalonate synthesis. The relative incorporation of mevalonate into the different end products of isoprenoid metabolism was markedly dependent upon the concentration of mevalonate in the medium. The synthesis of cholesterol was dominant at higher concentrations of mevalonate while higher molecular weight isoprenoids were favored at the lower concentrations. The relative incorporation of mevalonate into the different prenylcysteines of prenylated proteins was dependent upon mevalonate concentration with geranylgeranylcysteine being the principal product at higher concentrations. At low levels of mevalonate farnesylcysteine synthesis predominated and geranylcysteine was detected. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of proteins from CHO cells that had been radiolabeled at different concentrations of [
3H]mevalonate had different patterns on fluorography with relatively few proteins labeled at low concentrations. A study of this effect on the prenylcysteines of a specific protein, Ras, showed considerably less sensitivity to mevalonate concentration than bulk protein. These results indicate that the specific proteins that are prenylated depend upon the availability of the isoprenyl diphosphate substrates.</description><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>CHO Cells</subject><subject>Cholesterol - metabolism</subject><subject>Cricetinae</subject><subject>Cysteine - analogs & derivatives</subject><subject>Cysteine - metabolism</subject><subject>Diterpenes - metabolism</subject><subject>Dose-Response Relationship, Drug</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Lipid Metabolism</subject><subject>Lipoproteins - biosynthesis</subject><subject>Mevalonic Acid - metabolism</subject><subject>Molecular and cellular biology</subject><subject>Molecular genetics</subject><subject>Oncogene Protein p21(ras) - biosynthesis</subject><subject>Protein Prenylation</subject><subject>Translation. Translation factors. Protein processing</subject><issn>0003-9861</issn><issn>1096-0384</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1993</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kMFLwzAYxYMoc06v3oQexNtm0jRpe5TqVJjMg548hDT5ApEumUk32H9vxupuQki-8N77ePwQuiZ4RjDm97Jt7YzUNZ0RQtkJGhNc8ymmVXGKxhhjOq0rTs7RRYzfGBNS8HyERlXBcU3ZGH09WmMggOut7LL3NOw62VvvMm_S1_dgXcxkOtl849Sf8gZb2Xkne8ga71SKh0PKuqx5WWYNdF28RGdGdhGuhneCPudPH83LdLF8fm0eFlNFedWnfnkBumJcl4Wqqyqva6xUWzJWaC51XnJK0sWI4oTwFqAg1JhWmZa1kilNJ-jusHcd_M8GYi9WNqrUQDrwmyhKxjnOKU_G2cGogo8xgBHrYFcy7ATBYk9T7GmKPU2xp5kCN8PmTbsCfbQP-JJ-O-gyKtmZIJ2y8WgrOKc5wclWHWyQKGwtBBGVhYRN2wCqF9rb_xr8AoMTj_0</recordid><startdate>19930301</startdate><enddate>19930301</enddate><creator>Rilling, H.C.</creator><creator>Bruenger, E.</creator><creator>Leining, L.M.</creator><creator>Buss, J.E.</creator><creator>Epstein, W.W.</creator><general>Elsevier Inc</general><general>Elsevier</general><scope>IQODW</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>7X8</scope></search><sort><creationdate>19930301</creationdate><title>Differential Prenylation of Proteins as a Function of Mevalonate Concentration in CHO Cells</title><author>Rilling, H.C. ; Bruenger, E. ; Leining, L.M. ; Buss, J.E. ; Epstein, W.W.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c368t-9824ed856d74c9882990ccb7554d6ad2763127651c6116bee413ffbcfb5ba5cd3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1993</creationdate><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>CHO Cells</topic><topic>Cholesterol - metabolism</topic><topic>Cricetinae</topic><topic>Cysteine - analogs & derivatives</topic><topic>Cysteine - metabolism</topic><topic>Diterpenes - metabolism</topic><topic>Dose-Response Relationship, Drug</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Lipid Metabolism</topic><topic>Lipoproteins - biosynthesis</topic><topic>Mevalonic Acid - metabolism</topic><topic>Molecular and cellular biology</topic><topic>Molecular genetics</topic><topic>Oncogene Protein p21(ras) - biosynthesis</topic><topic>Protein Prenylation</topic><topic>Translation. Translation factors. Protein processing</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Rilling, H.C.</creatorcontrib><creatorcontrib>Bruenger, E.</creatorcontrib><creatorcontrib>Leining, L.M.</creatorcontrib><creatorcontrib>Buss, J.E.</creatorcontrib><creatorcontrib>Epstein, W.W.</creatorcontrib><collection>Pascal-Francis</collection><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>Archives of biochemistry and biophysics</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Rilling, H.C.</au><au>Bruenger, E.</au><au>Leining, L.M.</au><au>Buss, J.E.</au><au>Epstein, W.W.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Differential Prenylation of Proteins as a Function of Mevalonate Concentration in CHO Cells</atitle><jtitle>Archives of biochemistry and biophysics</jtitle><addtitle>Arch Biochem Biophys</addtitle><date>1993-03-01</date><risdate>1993</risdate><volume>301</volume><issue>2</issue><spage>210</spage><epage>215</epage><pages>210-215</pages><issn>0003-9861</issn><eissn>1096-0384</eissn><coden>ABBIA4</coden><abstract>The incorporation of [5-
3H]mevalonate into prenylated proteins and polyisoprenoid lipids has been determined as a function of mevalonate concentration in Chinese hamster ovary (CHO) cells that are inhibited in mevalonate synthesis. The relative incorporation of mevalonate into the different end products of isoprenoid metabolism was markedly dependent upon the concentration of mevalonate in the medium. The synthesis of cholesterol was dominant at higher concentrations of mevalonate while higher molecular weight isoprenoids were favored at the lower concentrations. The relative incorporation of mevalonate into the different prenylcysteines of prenylated proteins was dependent upon mevalonate concentration with geranylgeranylcysteine being the principal product at higher concentrations. At low levels of mevalonate farnesylcysteine synthesis predominated and geranylcysteine was detected. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of proteins from CHO cells that had been radiolabeled at different concentrations of [
3H]mevalonate had different patterns on fluorography with relatively few proteins labeled at low concentrations. A study of this effect on the prenylcysteines of a specific protein, Ras, showed considerably less sensitivity to mevalonate concentration than bulk protein. These results indicate that the specific proteins that are prenylated depend upon the availability of the isoprenyl diphosphate substrates.</abstract><cop>San Diego, CA</cop><pub>Elsevier Inc</pub><pmid>8460935</pmid><doi>10.1006/abbi.1993.1135</doi><tpages>6</tpages></addata></record> |
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| ispartof | Archives of biochemistry and biophysics, 1993-03, Vol.301 (2), p.210-215 |
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| source | MEDLINE; Elsevier ScienceDirect Journals |
| subjects | Animals Biological and medical sciences CHO Cells Cholesterol - metabolism Cricetinae Cysteine - analogs & derivatives Cysteine - metabolism Diterpenes - metabolism Dose-Response Relationship, Drug Fundamental and applied biological sciences. Psychology Lipid Metabolism Lipoproteins - biosynthesis Mevalonic Acid - metabolism Molecular and cellular biology Molecular genetics Oncogene Protein p21(ras) - biosynthesis Protein Prenylation Translation. Translation factors. Protein processing |
| title | Differential Prenylation of Proteins as a Function of Mevalonate Concentration in CHO Cells |
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