Increased PARP-1 levels in nuclear matrix isolated from heat shock treated rat liver
Poly(ADP-ribose) polymerase-1 (PARP-1), a chromatin-associated enzyme that catalyzes the NAD + -dependent addition of ADP-ribose polymers onto a variety of nuclear proteins, has been shown to be associated with the nuclear matrix. PARP-1 levels in the nuclear matrix vary depending on the matrix isol...
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| Veröffentlicht in: | Biochemistry (Moscow) 2012, Vol.77 (1), p.105-110 |
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| creator | Zaalishvili, G. Zaldastanishvili, E. Karapetian, M. Zaalishvili, T. |
| description | Poly(ADP-ribose) polymerase-1 (PARP-1), a chromatin-associated enzyme that catalyzes the NAD
+
-dependent addition of ADP-ribose polymers onto a variety of nuclear proteins, has been shown to be associated with the nuclear matrix. PARP-1 levels in the nuclear matrix vary depending on the matrix isolation method used. The nuclear matrix appears to be the most thermosensitive nuclear structure during heat shock. Here we provide evidence for the extensive translocation of PARP-1 from chromatin to the nuclear matrix during heat shock. This translocation is accompanied by inhibition of PARP activity in the nucleus and elevation of PARP activity in the nuclear matrix. Our data suggest that thermal destabilization of the nuclear matrix is less likely to contribute to the translocation of PARP-1 to the nuclear matrix. |
| doi_str_mv | 10.1134/S0006297912010130 |
| format | Article |
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+
-dependent addition of ADP-ribose polymers onto a variety of nuclear proteins, has been shown to be associated with the nuclear matrix. PARP-1 levels in the nuclear matrix vary depending on the matrix isolation method used. The nuclear matrix appears to be the most thermosensitive nuclear structure during heat shock. Here we provide evidence for the extensive translocation of PARP-1 from chromatin to the nuclear matrix during heat shock. This translocation is accompanied by inhibition of PARP activity in the nucleus and elevation of PARP activity in the nuclear matrix. Our data suggest that thermal destabilization of the nuclear matrix is less likely to contribute to the translocation of PARP-1 to the nuclear matrix.</description><identifier>ISSN: 0006-2979</identifier><identifier>EISSN: 1608-3040</identifier><identifier>DOI: 10.1134/S0006297912010130</identifier><identifier>PMID: 22339640</identifier><language>eng</language><publisher>Dordrecht: SP MAIK Nauka/Interperiodica</publisher><subject>Adenosine diphosphate ; Animals ; Biochemistry ; Biomedical and Life Sciences ; Biomedicine ; Bioorganic Chemistry ; Catalysis ; Chromatin - metabolism ; Enzymes ; Heat shock proteins ; Heat-Shock Response ; Life Sciences ; Liver - metabolism ; Male ; Microbiology ; Monosaccharides ; Nuclear Matrix - enzymology ; Poly (ADP-Ribose) Polymerase-1 ; Poly(ADP-ribose) Polymerases - metabolism ; Polymerase chain reaction ; Polymers ; Rats ; Rats, Wistar ; Sugars ; Temperature ; Translocation</subject><ispartof>Biochemistry (Moscow), 2012, Vol.77 (1), p.105-110</ispartof><rights>Pleiades Publishing, Ltd. 2012</rights><rights>COPYRIGHT 2012 Springer</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c437t-1ab2490f0e139f644222f3a9a370127d1b7958e3f41100ed88e48466c14f75a13</citedby><cites>FETCH-LOGICAL-c437t-1ab2490f0e139f644222f3a9a370127d1b7958e3f41100ed88e48466c14f75a13</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1134/S0006297912010130$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1134/S0006297912010130$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,780,784,27923,27924,41487,42556,51318</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/22339640$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Zaalishvili, G.</creatorcontrib><creatorcontrib>Zaldastanishvili, E.</creatorcontrib><creatorcontrib>Karapetian, M.</creatorcontrib><creatorcontrib>Zaalishvili, T.</creatorcontrib><title>Increased PARP-1 levels in nuclear matrix isolated from heat shock treated rat liver</title><title>Biochemistry (Moscow)</title><addtitle>Biochemistry Moscow</addtitle><addtitle>Biochemistry (Mosc)</addtitle><description>Poly(ADP-ribose) polymerase-1 (PARP-1), a chromatin-associated enzyme that catalyzes the NAD
+
-dependent addition of ADP-ribose polymers onto a variety of nuclear proteins, has been shown to be associated with the nuclear matrix. PARP-1 levels in the nuclear matrix vary depending on the matrix isolation method used. The nuclear matrix appears to be the most thermosensitive nuclear structure during heat shock. Here we provide evidence for the extensive translocation of PARP-1 from chromatin to the nuclear matrix during heat shock. This translocation is accompanied by inhibition of PARP activity in the nucleus and elevation of PARP activity in the nuclear matrix. Our data suggest that thermal destabilization of the nuclear matrix is less likely to contribute to the translocation of PARP-1 to the nuclear matrix.</description><subject>Adenosine diphosphate</subject><subject>Animals</subject><subject>Biochemistry</subject><subject>Biomedical and Life Sciences</subject><subject>Biomedicine</subject><subject>Bioorganic Chemistry</subject><subject>Catalysis</subject><subject>Chromatin - metabolism</subject><subject>Enzymes</subject><subject>Heat shock proteins</subject><subject>Heat-Shock Response</subject><subject>Life Sciences</subject><subject>Liver - metabolism</subject><subject>Male</subject><subject>Microbiology</subject><subject>Monosaccharides</subject><subject>Nuclear Matrix - enzymology</subject><subject>Poly (ADP-Ribose) Polymerase-1</subject><subject>Poly(ADP-ribose) Polymerases - metabolism</subject><subject>Polymerase chain reaction</subject><subject>Polymers</subject><subject>Rats</subject><subject>Rats, Wistar</subject><subject>Sugars</subject><subject>Temperature</subject><subject>Translocation</subject><issn>0006-2979</issn><issn>1608-3040</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2012</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNp1kc1u1TAQhS0EopfCA7BBESxYpczYjhMvryoKlSpRQVlHvs64dXHiYicVvH0d3QLiT15YPuc7R2MNY88RjhCFfPMJABTXrUYOCCjgAduggq4WIOEh26x2vfoH7EnO1-XJQYvH7IBzIbSSsGEXp5NNZDIN1fn243mNVaBbCrnyUzUtNpBJ1Wjm5L9VPsdg5gK6FMfqisxc5atov1RzKVj1VJTgbyk9ZY-cCZme3d-H7PPJ24vj9_XZh3enx9uz2krRzjWaHZcaHBAK7ZSUnHMnjDaiBeTtgLtWNx0JJxEBaOg6kp1UyqJ0bWNQHLLX-96bFL8ulOd-9NlSCGaiuORec95Aozoo5Ms_yOu4pKkM12vshFCibQr0ag9dmkC9n1yck7FrZb8VUgG0XPFCHf2DKmeg0ds4kfNF_y2A-4BNMedErr9JfjTpe4_Qr3vs_9pjyby4n3fZjTT8TPxYXAH4HsjFmi4p_frQ_1vvAPApokA</recordid><startdate>2012</startdate><enddate>2012</enddate><creator>Zaalishvili, G.</creator><creator>Zaldastanishvili, E.</creator><creator>Karapetian, M.</creator><creator>Zaalishvili, T.</creator><general>SP MAIK Nauka/Interperiodica</general><general>Springer</general><general>Springer Nature B.V</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>3V.</scope><scope>7QL</scope><scope>7TM</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>88I</scope><scope>8AO</scope><scope>8C1</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2P</scope><scope>M7N</scope><scope>M7P</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>7X8</scope></search><sort><creationdate>2012</creationdate><title>Increased PARP-1 levels in nuclear matrix isolated from heat shock treated rat liver</title><author>Zaalishvili, G. ; 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+
-dependent addition of ADP-ribose polymers onto a variety of nuclear proteins, has been shown to be associated with the nuclear matrix. PARP-1 levels in the nuclear matrix vary depending on the matrix isolation method used. The nuclear matrix appears to be the most thermosensitive nuclear structure during heat shock. Here we provide evidence for the extensive translocation of PARP-1 from chromatin to the nuclear matrix during heat shock. This translocation is accompanied by inhibition of PARP activity in the nucleus and elevation of PARP activity in the nuclear matrix. Our data suggest that thermal destabilization of the nuclear matrix is less likely to contribute to the translocation of PARP-1 to the nuclear matrix.</abstract><cop>Dordrecht</cop><pub>SP MAIK Nauka/Interperiodica</pub><pmid>22339640</pmid><doi>10.1134/S0006297912010130</doi><tpages>6</tpages></addata></record> |
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| ispartof | Biochemistry (Moscow), 2012, Vol.77 (1), p.105-110 |
| issn | 0006-2979 1608-3040 |
| language | eng |
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| subjects | Adenosine diphosphate Animals Biochemistry Biomedical and Life Sciences Biomedicine Bioorganic Chemistry Catalysis Chromatin - metabolism Enzymes Heat shock proteins Heat-Shock Response Life Sciences Liver - metabolism Male Microbiology Monosaccharides Nuclear Matrix - enzymology Poly (ADP-Ribose) Polymerase-1 Poly(ADP-ribose) Polymerases - metabolism Polymerase chain reaction Polymers Rats Rats, Wistar Sugars Temperature Translocation |
| title | Increased PARP-1 levels in nuclear matrix isolated from heat shock treated rat liver |
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