Tyrosine Phosphorylation of Apoptotic Proteins During Hyperoxia in Mitochondria of the Cerebral Cortex of Newborn Piglets
The present study tests the hypothesis that hyperoxia results in increased tyrosine phosphorylation of apoptotic proteins Bcl-2, Bcl-xl, Bax & Bad in the mitochondrial fraction of the cerebral cortex of newborn piglets. Twelve newborn piglets were divided into normoxic [Nx, n = 6], exposed to a...
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| Veröffentlicht in: | Neurochemical research 2010-07, Vol.35 (7), p.1003-1009 |
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| creator | Mudduluru, Manjula Zubrow, Alan B. Ashraf, Q. M. Delivoria-Papadopoulos, Maria Mishra, Om P. |
| description | The present study tests the hypothesis that hyperoxia results in increased tyrosine phosphorylation of apoptotic proteins Bcl-2, Bcl-xl, Bax & Bad in the mitochondrial fraction of the cerebral cortex of newborn piglets. Twelve newborn piglets were divided into normoxic [Nx,
n
= 6], exposed to a FiO
2
of 0.21 for 1 h and hyperoxic [Hyx,
n
= 6], exposed to FiO
2
of 1.0 for 1 h. PaO
2
in Hyx group was maintained at 400 mmHg while the Nx group was kept at 80 to100 mmHg. The density (O.D.x mm
2
) of phosphorylated Bcl2 protein on westernblot was 19.3 ± 3.6 in Nx and 41.5 ± 18.3 in Hyx, (
P
|
| doi_str_mv | 10.1007/s11064-010-0147-x |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_744696115</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>2051457901</sourcerecordid><originalsourceid>FETCH-LOGICAL-c402t-3473495ae9506c8759ea8cc39d5b3c4093ca7fad5490d7bbb5d6dba97302f2063</originalsourceid><addsrcrecordid>eNqFkUFv3CAQhVGUqtmm_QG5RCiXntyCAROO0SZtKqXtHtIzwnicJfKCC1hZ__tibdpIlaoe0Ijhe2_EPITOKPlACZEfE6Wk4RWhpBwuq_0RWlEhWdUowo7RirDyyqgiJ-hNSo-kgKSmr9FJXQpjnK_QfD_HkJwHvNmGNG5DnAeTXfA49PhqDGMO2Vm8iSGD8wlfT9H5B3w7jxDD3hnsPP7qcrDb4LtY7kWWt4DXEKGNZsDrEDPsl_Y3eGpD9HjjHgbI6S161Zshwbvneop-fLq5X99Wd98_f1lf3VWWkzpXjEvGlTCgBGnspRQKzKW1THWiZQVRzBrZm05wRTrZtq3omq41SjJS9zVp2Cl6f_AdY_g5Qcp655KFYTAewpS05LxRDaXi_yRjVJS914W8-It8DFP05RuaNYJTKfkymB4gWzacIvR6jG5n4qwp0Ut--pCfLrHoJT-9L5rzZ-Op3UH3R_E7sALUByCNSxAQXyb_2_UX5DimzA</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>365417746</pqid></control><display><type>article</type><title>Tyrosine Phosphorylation of Apoptotic Proteins During Hyperoxia in Mitochondria of the Cerebral Cortex of Newborn Piglets</title><source>MEDLINE</source><source>SpringerLink (Online service)</source><creator>Mudduluru, Manjula ; Zubrow, Alan B. ; Ashraf, Q. M. ; Delivoria-Papadopoulos, Maria ; Mishra, Om P.</creator><creatorcontrib>Mudduluru, Manjula ; Zubrow, Alan B. ; Ashraf, Q. M. ; Delivoria-Papadopoulos, Maria ; Mishra, Om P.</creatorcontrib><description>The present study tests the hypothesis that hyperoxia results in increased tyrosine phosphorylation of apoptotic proteins Bcl-2, Bcl-xl, Bax & Bad in the mitochondrial fraction of the cerebral cortex of newborn piglets. Twelve newborn piglets were divided into normoxic [Nx,
n
= 6], exposed to a FiO
2
of 0.21 for 1 h and hyperoxic [Hyx,
n
= 6], exposed to FiO
2
of 1.0 for 1 h. PaO
2
in Hyx group was maintained at 400 mmHg while the Nx group was kept at 80 to100 mmHg. The density (O.D.x mm
2
) of phosphorylated Bcl2 protein on westernblot was 19.3 ± 3.6 in Nx and 41.5 ± 18.3 in Hyx, (
P
< 0.05). The density of phosphorylated Bcl-xl protein density was 26.9 ± 7.0 in Nx and 47.9 ± 2.5 in Hyx, (
P
< 0.05). Phosphorylated Bax density was 43.5 ± 5.0 in Nx and 43.3 ± 5.2 in Hyx. Phosphorylated Bad density was 23.6 ± 3.9 in Nx, 24.4 ± 4.7 in Hyx. The data show that during hyperoxia there is a significant increase in tyrosine phosphorylation of Bcl2 and Bcl-xl, while the phosphorylation of proapototic proteins Bax & Bad was not altered. We conclude that hyperoxia leads to post translational modification of anti apoptotic proteins Bcl2 and Bcl-xl in cerebral cortical mitochondria. We propose that phosphorylation of Bcl2 will result in loss of its antiapoptotic potential by preventing its dimerization with Bax leading to activation of the caspase pathway and subsequent neuronal death in the cerebral cortex of the newborn piglets.</description><identifier>ISSN: 0364-3190</identifier><identifier>EISSN: 1573-6903</identifier><identifier>DOI: 10.1007/s11064-010-0147-x</identifier><identifier>PMID: 20213344</identifier><language>eng</language><publisher>Boston: Springer US</publisher><subject>Animals ; Animals, Newborn ; Biochemistry ; Biomedical and Life Sciences ; Biomedicine ; Cell Biology ; Cerebral Cortex - metabolism ; Hyperoxia - metabolism ; Mitochondria - metabolism ; Neurochemistry ; Neurology ; Neurosciences ; Original Paper ; Phosphorylation ; Proto-Oncogene Proteins c-bcl-2 - metabolism ; Swine ; Tyrosine - metabolism</subject><ispartof>Neurochemical research, 2010-07, Vol.35 (7), p.1003-1009</ispartof><rights>Springer Science+Business Media, LLC 2010</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c402t-3473495ae9506c8759ea8cc39d5b3c4093ca7fad5490d7bbb5d6dba97302f2063</citedby><cites>FETCH-LOGICAL-c402t-3473495ae9506c8759ea8cc39d5b3c4093ca7fad5490d7bbb5d6dba97302f2063</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s11064-010-0147-x$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s11064-010-0147-x$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,776,780,27901,27902,41464,42533,51294</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/20213344$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Mudduluru, Manjula</creatorcontrib><creatorcontrib>Zubrow, Alan B.</creatorcontrib><creatorcontrib>Ashraf, Q. M.</creatorcontrib><creatorcontrib>Delivoria-Papadopoulos, Maria</creatorcontrib><creatorcontrib>Mishra, Om P.</creatorcontrib><title>Tyrosine Phosphorylation of Apoptotic Proteins During Hyperoxia in Mitochondria of the Cerebral Cortex of Newborn Piglets</title><title>Neurochemical research</title><addtitle>Neurochem Res</addtitle><addtitle>Neurochem Res</addtitle><description>The present study tests the hypothesis that hyperoxia results in increased tyrosine phosphorylation of apoptotic proteins Bcl-2, Bcl-xl, Bax & Bad in the mitochondrial fraction of the cerebral cortex of newborn piglets. Twelve newborn piglets were divided into normoxic [Nx,
n
= 6], exposed to a FiO
2
of 0.21 for 1 h and hyperoxic [Hyx,
n
= 6], exposed to FiO
2
of 1.0 for 1 h. PaO
2
in Hyx group was maintained at 400 mmHg while the Nx group was kept at 80 to100 mmHg. The density (O.D.x mm
2
) of phosphorylated Bcl2 protein on westernblot was 19.3 ± 3.6 in Nx and 41.5 ± 18.3 in Hyx, (
P
< 0.05). The density of phosphorylated Bcl-xl protein density was 26.9 ± 7.0 in Nx and 47.9 ± 2.5 in Hyx, (
P
< 0.05). Phosphorylated Bax density was 43.5 ± 5.0 in Nx and 43.3 ± 5.2 in Hyx. Phosphorylated Bad density was 23.6 ± 3.9 in Nx, 24.4 ± 4.7 in Hyx. The data show that during hyperoxia there is a significant increase in tyrosine phosphorylation of Bcl2 and Bcl-xl, while the phosphorylation of proapototic proteins Bax & Bad was not altered. We conclude that hyperoxia leads to post translational modification of anti apoptotic proteins Bcl2 and Bcl-xl in cerebral cortical mitochondria. We propose that phosphorylation of Bcl2 will result in loss of its antiapoptotic potential by preventing its dimerization with Bax leading to activation of the caspase pathway and subsequent neuronal death in the cerebral cortex of the newborn piglets.</description><subject>Animals</subject><subject>Animals, Newborn</subject><subject>Biochemistry</subject><subject>Biomedical and Life Sciences</subject><subject>Biomedicine</subject><subject>Cell Biology</subject><subject>Cerebral Cortex - metabolism</subject><subject>Hyperoxia - metabolism</subject><subject>Mitochondria - metabolism</subject><subject>Neurochemistry</subject><subject>Neurology</subject><subject>Neurosciences</subject><subject>Original Paper</subject><subject>Phosphorylation</subject><subject>Proto-Oncogene Proteins c-bcl-2 - metabolism</subject><subject>Swine</subject><subject>Tyrosine - metabolism</subject><issn>0364-3190</issn><issn>1573-6903</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2010</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>BENPR</sourceid><recordid>eNqFkUFv3CAQhVGUqtmm_QG5RCiXntyCAROO0SZtKqXtHtIzwnicJfKCC1hZ__tibdpIlaoe0Ijhe2_EPITOKPlACZEfE6Wk4RWhpBwuq_0RWlEhWdUowo7RirDyyqgiJ-hNSo-kgKSmr9FJXQpjnK_QfD_HkJwHvNmGNG5DnAeTXfA49PhqDGMO2Vm8iSGD8wlfT9H5B3w7jxDD3hnsPP7qcrDb4LtY7kWWt4DXEKGNZsDrEDPsl_Y3eGpD9HjjHgbI6S161Zshwbvneop-fLq5X99Wd98_f1lf3VWWkzpXjEvGlTCgBGnspRQKzKW1THWiZQVRzBrZm05wRTrZtq3omq41SjJS9zVp2Cl6f_AdY_g5Qcp655KFYTAewpS05LxRDaXi_yRjVJS914W8-It8DFP05RuaNYJTKfkymB4gWzacIvR6jG5n4qwp0Ut--pCfLrHoJT-9L5rzZ-Op3UH3R_E7sALUByCNSxAQXyb_2_UX5DimzA</recordid><startdate>20100701</startdate><enddate>20100701</enddate><creator>Mudduluru, Manjula</creator><creator>Zubrow, Alan B.</creator><creator>Ashraf, Q. M.</creator><creator>Delivoria-Papadopoulos, Maria</creator><creator>Mishra, Om P.</creator><general>Springer US</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>7QR</scope><scope>7TK</scope><scope>7U7</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>8AO</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</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>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M7P</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>7X8</scope></search><sort><creationdate>20100701</creationdate><title>Tyrosine Phosphorylation of Apoptotic Proteins During Hyperoxia in Mitochondria of the Cerebral Cortex of Newborn Piglets</title><author>Mudduluru, Manjula ; Zubrow, Alan B. ; Ashraf, Q. M. ; Delivoria-Papadopoulos, Maria ; Mishra, Om P.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c402t-3473495ae9506c8759ea8cc39d5b3c4093ca7fad5490d7bbb5d6dba97302f2063</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2010</creationdate><topic>Animals</topic><topic>Animals, Newborn</topic><topic>Biochemistry</topic><topic>Biomedical and Life Sciences</topic><topic>Biomedicine</topic><topic>Cell Biology</topic><topic>Cerebral Cortex - metabolism</topic><topic>Hyperoxia - metabolism</topic><topic>Mitochondria - metabolism</topic><topic>Neurochemistry</topic><topic>Neurology</topic><topic>Neurosciences</topic><topic>Original Paper</topic><topic>Phosphorylation</topic><topic>Proto-Oncogene Proteins c-bcl-2 - metabolism</topic><topic>Swine</topic><topic>Tyrosine - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Mudduluru, Manjula</creatorcontrib><creatorcontrib>Zubrow, Alan B.</creatorcontrib><creatorcontrib>Ashraf, Q. M.</creatorcontrib><creatorcontrib>Delivoria-Papadopoulos, Maria</creatorcontrib><creatorcontrib>Mishra, Om P.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Chemoreception Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Toxicology Abstracts</collection><collection>ProQuest - Health & Medical Complete保健、医学与药学数据库</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni)</collection><collection>ProQuest Central</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>AUTh Library subscriptions: ProQuest Central</collection><collection>ProQuest Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Biological Sciences</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Biological Science Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>MEDLINE - Academic</collection><jtitle>Neurochemical research</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Mudduluru, Manjula</au><au>Zubrow, Alan B.</au><au>Ashraf, Q. M.</au><au>Delivoria-Papadopoulos, Maria</au><au>Mishra, Om P.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Tyrosine Phosphorylation of Apoptotic Proteins During Hyperoxia in Mitochondria of the Cerebral Cortex of Newborn Piglets</atitle><jtitle>Neurochemical research</jtitle><stitle>Neurochem Res</stitle><addtitle>Neurochem Res</addtitle><date>2010-07-01</date><risdate>2010</risdate><volume>35</volume><issue>7</issue><spage>1003</spage><epage>1009</epage><pages>1003-1009</pages><issn>0364-3190</issn><eissn>1573-6903</eissn><abstract>The present study tests the hypothesis that hyperoxia results in increased tyrosine phosphorylation of apoptotic proteins Bcl-2, Bcl-xl, Bax & Bad in the mitochondrial fraction of the cerebral cortex of newborn piglets. Twelve newborn piglets were divided into normoxic [Nx,
n
= 6], exposed to a FiO
2
of 0.21 for 1 h and hyperoxic [Hyx,
n
= 6], exposed to FiO
2
of 1.0 for 1 h. PaO
2
in Hyx group was maintained at 400 mmHg while the Nx group was kept at 80 to100 mmHg. The density (O.D.x mm
2
) of phosphorylated Bcl2 protein on westernblot was 19.3 ± 3.6 in Nx and 41.5 ± 18.3 in Hyx, (
P
< 0.05). The density of phosphorylated Bcl-xl protein density was 26.9 ± 7.0 in Nx and 47.9 ± 2.5 in Hyx, (
P
< 0.05). Phosphorylated Bax density was 43.5 ± 5.0 in Nx and 43.3 ± 5.2 in Hyx. Phosphorylated Bad density was 23.6 ± 3.9 in Nx, 24.4 ± 4.7 in Hyx. The data show that during hyperoxia there is a significant increase in tyrosine phosphorylation of Bcl2 and Bcl-xl, while the phosphorylation of proapototic proteins Bax & Bad was not altered. We conclude that hyperoxia leads to post translational modification of anti apoptotic proteins Bcl2 and Bcl-xl in cerebral cortical mitochondria. We propose that phosphorylation of Bcl2 will result in loss of its antiapoptotic potential by preventing its dimerization with Bax leading to activation of the caspase pathway and subsequent neuronal death in the cerebral cortex of the newborn piglets.</abstract><cop>Boston</cop><pub>Springer US</pub><pmid>20213344</pmid><doi>10.1007/s11064-010-0147-x</doi><tpages>7</tpages></addata></record> |
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| subjects | Animals Animals, Newborn Biochemistry Biomedical and Life Sciences Biomedicine Cell Biology Cerebral Cortex - metabolism Hyperoxia - metabolism Mitochondria - metabolism Neurochemistry Neurology Neurosciences Original Paper Phosphorylation Proto-Oncogene Proteins c-bcl-2 - metabolism Swine Tyrosine - metabolism |
| title | Tyrosine Phosphorylation of Apoptotic Proteins During Hyperoxia in Mitochondria of the Cerebral Cortex of Newborn Piglets |
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