Nuclear sphingomyelin protects RNA from RNase action
Chromatin phospholipidic fraction, as previously demonstrated, shows the same localization as RNA inside the nuclei. DNase and RNase treatment of nuclei removed almost totally the DNA, 63% of RNA and caused a 50% loss of phospholipids. The aim of the present investigation is to study the fraction of...
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| Veröffentlicht in: | FEBS letters 1998-07, Vol.431 (3), p.443-447 |
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| creator | Micheli, Marta Albi, Elisabetta Leray, Claude Magni, Mariapia Viola |
| description | Chromatin phospholipidic fraction, as previously demonstrated, shows the same localization as RNA inside the nuclei. DNase and RNase treatment of nuclei removed almost totally the DNA, 63% of RNA and caused a 50% loss of phospholipids. The aim of the present investigation is to study the fraction of RNase undigested nuclear RNA and its relationship with the phospholipids still present in the nuclei. Isolated hepatocyte nuclei were treated with Triton X-100 and digested with RNase and DNase. The undigested nuclear material contained proteins (98%) and a small amount of RNA (1.7%), DNA (0.4%) and phospholipids (0.18%). The analysis of phospholipids showed the presence of two components only, namely phosphatidylcholine and sphingomyelin. In the same complex, the activity of sphingomyelin synthase, phosphatidylcholine-dependent phospholipase C and neutral sphingomyelinase has been detected. Treatment of isolated RNA with neutral sphingomyelinase modified the RNA in RNase sensitive RNA, thus suggesting that the SM may represent a bridge between two RNA strands possibly regulating transcription. |
| doi_str_mv | 10.1016/S0014-5793(98)00810-2 |
| format | Article |
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DNase and RNase treatment of nuclei removed almost totally the DNA, 63% of RNA and caused a 50% loss of phospholipids. The aim of the present investigation is to study the fraction of RNase undigested nuclear RNA and its relationship with the phospholipids still present in the nuclei. Isolated hepatocyte nuclei were treated with Triton X-100 and digested with RNase and DNase. The undigested nuclear material contained proteins (98%) and a small amount of RNA (1.7%), DNA (0.4%) and phospholipids (0.18%). The analysis of phospholipids showed the presence of two components only, namely phosphatidylcholine and sphingomyelin. In the same complex, the activity of sphingomyelin synthase, phosphatidylcholine-dependent phospholipase C and neutral sphingomyelinase has been detected. Treatment of isolated RNA with neutral sphingomyelinase modified the RNA in RNase sensitive RNA, thus suggesting that the SM may represent a bridge between two RNA strands possibly regulating transcription.</description><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1016/S0014-5793(98)00810-2</identifier><identifier>PMID: 9714560</identifier><language>eng</language><publisher>England: Elsevier B.V</publisher><subject>Animals ; Cell Nucleus - enzymology ; Cell Nucleus - metabolism ; Cells, Cultured ; DAG, diacylglycerol ; DNT, digested nuclei after Triton X-100 treatment ; Double-stranded RNA ; EDTA, ethylendiaminetetra-acetic acid ; Female ; Liver - cytology ; Liver - enzymology ; Liver - metabolism ; Male ; N-SMase, neutral sphingomyelinase ; NT, nuclei after Triton X-100 treatment ; PC, phosphatidylcholine ; PC-PLC, phosphatidylcholine-dependent phospholipase C ; PE, phosphatidylethanolamine ; Phosphatidylcholine ; Phosphatidylcholine-dependent phospholipase C ; Phosphatidylcholines - metabolism ; PI, phosphatidylinositol ; PLs, phospholipids ; PS, phosphatidylserine ; Rats ; Rats, Sprague-Dawley ; Ribonucleases - metabolism ; RNA - metabolism ; SM synthase, sphingomyelin synthase ; SM, sphingomyelin ; Sphingomyelin ; Sphingomyelin Phosphodiesterase - metabolism ; Sphingomyelin synthase ; Sphingomyelinase ; Sphingomyelins - metabolism ; TLC, thin layer chromatography ; Tris, hydroxymethylaminomethane ; Type C Phospholipases - metabolism</subject><ispartof>FEBS letters, 1998-07, Vol.431 (3), p.443-447</ispartof><rights>1998 Federation of European Biochemical Societies</rights><rights>FEBS Letters 431 (1998) 1873-3468 © 2015 Federation of European Biochemical Societies</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5382-b1af13678d15932c5c59a3578779b17012677be4d57008b85a6d717b5e3b70803</citedby><cites>FETCH-LOGICAL-c5382-b1af13678d15932c5c59a3578779b17012677be4d57008b85a6d717b5e3b70803</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1016%2FS0014-5793%2898%2900810-2$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://dx.doi.org/10.1016/S0014-5793(98)00810-2$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,777,781,1412,1428,3537,27905,27906,45555,45556,45976,46390,46814</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9714560$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Micheli, Marta</creatorcontrib><creatorcontrib>Albi, Elisabetta</creatorcontrib><creatorcontrib>Leray, Claude</creatorcontrib><creatorcontrib>Magni, Mariapia Viola</creatorcontrib><title>Nuclear sphingomyelin protects RNA from RNase action</title><title>FEBS letters</title><addtitle>FEBS Lett</addtitle><description>Chromatin phospholipidic fraction, as previously demonstrated, shows the same localization as RNA inside the nuclei. DNase and RNase treatment of nuclei removed almost totally the DNA, 63% of RNA and caused a 50% loss of phospholipids. The aim of the present investigation is to study the fraction of RNase undigested nuclear RNA and its relationship with the phospholipids still present in the nuclei. Isolated hepatocyte nuclei were treated with Triton X-100 and digested with RNase and DNase. The undigested nuclear material contained proteins (98%) and a small amount of RNA (1.7%), DNA (0.4%) and phospholipids (0.18%). The analysis of phospholipids showed the presence of two components only, namely phosphatidylcholine and sphingomyelin. In the same complex, the activity of sphingomyelin synthase, phosphatidylcholine-dependent phospholipase C and neutral sphingomyelinase has been detected. Treatment of isolated RNA with neutral sphingomyelinase modified the RNA in RNase sensitive RNA, thus suggesting that the SM may represent a bridge between two RNA strands possibly regulating transcription.</description><subject>Animals</subject><subject>Cell Nucleus - enzymology</subject><subject>Cell Nucleus - metabolism</subject><subject>Cells, Cultured</subject><subject>DAG, diacylglycerol</subject><subject>DNT, digested nuclei after Triton X-100 treatment</subject><subject>Double-stranded RNA</subject><subject>EDTA, ethylendiaminetetra-acetic acid</subject><subject>Female</subject><subject>Liver - cytology</subject><subject>Liver - enzymology</subject><subject>Liver - metabolism</subject><subject>Male</subject><subject>N-SMase, neutral sphingomyelinase</subject><subject>NT, nuclei after Triton X-100 treatment</subject><subject>PC, phosphatidylcholine</subject><subject>PC-PLC, phosphatidylcholine-dependent phospholipase C</subject><subject>PE, phosphatidylethanolamine</subject><subject>Phosphatidylcholine</subject><subject>Phosphatidylcholine-dependent phospholipase C</subject><subject>Phosphatidylcholines - metabolism</subject><subject>PI, phosphatidylinositol</subject><subject>PLs, phospholipids</subject><subject>PS, phosphatidylserine</subject><subject>Rats</subject><subject>Rats, Sprague-Dawley</subject><subject>Ribonucleases - metabolism</subject><subject>RNA - metabolism</subject><subject>SM synthase, sphingomyelin synthase</subject><subject>SM, sphingomyelin</subject><subject>Sphingomyelin</subject><subject>Sphingomyelin Phosphodiesterase - metabolism</subject><subject>Sphingomyelin synthase</subject><subject>Sphingomyelinase</subject><subject>Sphingomyelins - metabolism</subject><subject>TLC, thin layer chromatography</subject><subject>Tris, hydroxymethylaminomethane</subject><subject>Type C Phospholipases - metabolism</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1998</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkFtLAzEQhYMotVZ_QmGfRB9Wk81mkzxJLa0VSgUvzyGbnWpkLzVplf57s9vSV4VAMjkzZw4fQkOCbwgm2e0LxiSNGZf0SoprjAXBcXKE-kRwGtM0E8eof2g5RWfef-JQCyJ7qCc5SVmG-yhdbEwJ2kV-9WHr96baQmnraOWaNZi1j54Xo2jpmio8tIdIm7Vt6nN0stSlh4v9PUBv08nreBbPnx4ex6N5bBgVSZwTvSQ046IgTNLEMMOkpowLzmVOOCZJxnkOacF4iJ8LprOCE54zoDnHAtMButz5hjhfG_BrVVlvoCx1Dc3GK05Fymk4A8R2jcY13jtYqpWzlXZbRbBqaamOlmpRKClUR0slYW64X7DJKygOU3s8QZ_t9B9bwvZ_pmo6uU86pRWk6L7bVXc7KwjAvi045Y2F2kBhXSCtisb-EfYX-tWKvw</recordid><startdate>19980724</startdate><enddate>19980724</enddate><creator>Micheli, Marta</creator><creator>Albi, Elisabetta</creator><creator>Leray, Claude</creator><creator>Magni, Mariapia Viola</creator><general>Elsevier B.V</general><scope>6I.</scope><scope>AAFTH</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>19980724</creationdate><title>Nuclear sphingomyelin protects RNA from RNase action</title><author>Micheli, Marta ; Albi, Elisabetta ; Leray, Claude ; Magni, Mariapia Viola</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5382-b1af13678d15932c5c59a3578779b17012677be4d57008b85a6d717b5e3b70803</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1998</creationdate><topic>Animals</topic><topic>Cell Nucleus - enzymology</topic><topic>Cell Nucleus - metabolism</topic><topic>Cells, Cultured</topic><topic>DAG, diacylglycerol</topic><topic>DNT, digested nuclei after Triton X-100 treatment</topic><topic>Double-stranded RNA</topic><topic>EDTA, ethylendiaminetetra-acetic acid</topic><topic>Female</topic><topic>Liver - cytology</topic><topic>Liver - enzymology</topic><topic>Liver - metabolism</topic><topic>Male</topic><topic>N-SMase, neutral sphingomyelinase</topic><topic>NT, nuclei after Triton X-100 treatment</topic><topic>PC, phosphatidylcholine</topic><topic>PC-PLC, phosphatidylcholine-dependent phospholipase C</topic><topic>PE, phosphatidylethanolamine</topic><topic>Phosphatidylcholine</topic><topic>Phosphatidylcholine-dependent phospholipase C</topic><topic>Phosphatidylcholines - metabolism</topic><topic>PI, phosphatidylinositol</topic><topic>PLs, phospholipids</topic><topic>PS, phosphatidylserine</topic><topic>Rats</topic><topic>Rats, Sprague-Dawley</topic><topic>Ribonucleases - metabolism</topic><topic>RNA - metabolism</topic><topic>SM synthase, sphingomyelin synthase</topic><topic>SM, sphingomyelin</topic><topic>Sphingomyelin</topic><topic>Sphingomyelin Phosphodiesterase - metabolism</topic><topic>Sphingomyelin synthase</topic><topic>Sphingomyelinase</topic><topic>Sphingomyelins - metabolism</topic><topic>TLC, thin layer chromatography</topic><topic>Tris, hydroxymethylaminomethane</topic><topic>Type C Phospholipases - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Micheli, Marta</creatorcontrib><creatorcontrib>Albi, Elisabetta</creatorcontrib><creatorcontrib>Leray, Claude</creatorcontrib><creatorcontrib>Magni, Mariapia Viola</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</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>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Micheli, Marta</au><au>Albi, Elisabetta</au><au>Leray, Claude</au><au>Magni, Mariapia Viola</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Nuclear sphingomyelin protects RNA from RNase action</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>1998-07-24</date><risdate>1998</risdate><volume>431</volume><issue>3</issue><spage>443</spage><epage>447</epage><pages>443-447</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><abstract>Chromatin phospholipidic fraction, as previously demonstrated, shows the same localization as RNA inside the nuclei. DNase and RNase treatment of nuclei removed almost totally the DNA, 63% of RNA and caused a 50% loss of phospholipids. The aim of the present investigation is to study the fraction of RNase undigested nuclear RNA and its relationship with the phospholipids still present in the nuclei. Isolated hepatocyte nuclei were treated with Triton X-100 and digested with RNase and DNase. The undigested nuclear material contained proteins (98%) and a small amount of RNA (1.7%), DNA (0.4%) and phospholipids (0.18%). The analysis of phospholipids showed the presence of two components only, namely phosphatidylcholine and sphingomyelin. In the same complex, the activity of sphingomyelin synthase, phosphatidylcholine-dependent phospholipase C and neutral sphingomyelinase has been detected. Treatment of isolated RNA with neutral sphingomyelinase modified the RNA in RNase sensitive RNA, thus suggesting that the SM may represent a bridge between two RNA strands possibly regulating transcription.</abstract><cop>England</cop><pub>Elsevier B.V</pub><pmid>9714560</pmid><doi>10.1016/S0014-5793(98)00810-2</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Animals Cell Nucleus - enzymology Cell Nucleus - metabolism Cells, Cultured DAG, diacylglycerol DNT, digested nuclei after Triton X-100 treatment Double-stranded RNA EDTA, ethylendiaminetetra-acetic acid Female Liver - cytology Liver - enzymology Liver - metabolism Male N-SMase, neutral sphingomyelinase NT, nuclei after Triton X-100 treatment PC, phosphatidylcholine PC-PLC, phosphatidylcholine-dependent phospholipase C PE, phosphatidylethanolamine Phosphatidylcholine Phosphatidylcholine-dependent phospholipase C Phosphatidylcholines - metabolism PI, phosphatidylinositol PLs, phospholipids PS, phosphatidylserine Rats Rats, Sprague-Dawley Ribonucleases - metabolism RNA - metabolism SM synthase, sphingomyelin synthase SM, sphingomyelin Sphingomyelin Sphingomyelin Phosphodiesterase - metabolism Sphingomyelin synthase Sphingomyelinase Sphingomyelins - metabolism TLC, thin layer chromatography Tris, hydroxymethylaminomethane Type C Phospholipases - metabolism |
| title | Nuclear sphingomyelin protects RNA from RNase action |
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