1-O-alkenyl-sn-glyceryl-3-phosphorylcholine may be a novel posttranslational modification used by the placenta
Neurokinin B (NKB) secreted by the placenta was previously found to be raised in preeclampsia and most of the symptoms in this disease appeared to be through progressive activation of the three neurokinin receptors. Further characterization of placental NKB revealed that placental NKB eluted in the...
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Veröffentlicht in: | Biopolymers 2011, Vol.96 (2), p.189-192 |
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description | Neurokinin B (NKB) secreted by the placenta was previously found to be raised in preeclampsia and most of the symptoms in this disease appeared to be through progressive activation of the three neurokinin receptors. Further characterization of placental NKB revealed that placental NKB eluted in the approximate position of a 13mer and this was confirmed by TOF mass spectrometry which gave a mass of 1580. Although this is consistent with dimethylated NKB‐Gly‐Lys‐Arg, further characterization (immunological and mass spectrometric fragment analysis) suggested a novel posttranslational modification containing phosphocholine (PC) with some evidence for glycerol and a coordinated alkene. The structure that fits all the data is that a form of platelet activating factor is attached to the aspartyl side chain at position 4 of NKB and thus now implicates placental NKB in the platelet pathology seen in preeclampsia. As it has been reported that it is the PC group per se attached to certain proteins secreted by filarial nematodes imparts them with immune inhibitory properties and thus survival in the host over long periods, attaching PC to placental secretory peptide hormones (also be found on the placental precursors of CRF, ACTH, and activin) may result in a similar situation. © 2010 Wiley Periodicals,Inc. Biopolymers (Pept Sci) 96: 189–192, 2011. |
doi_str_mv | 10.1002/bip.21407 |
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Further characterization of placental NKB revealed that placental NKB eluted in the approximate position of a 13mer and this was confirmed by TOF mass spectrometry which gave a mass of 1580. Although this is consistent with dimethylated NKB‐Gly‐Lys‐Arg, further characterization (immunological and mass spectrometric fragment analysis) suggested a novel posttranslational modification containing phosphocholine (PC) with some evidence for glycerol and a coordinated alkene. The structure that fits all the data is that a form of platelet activating factor is attached to the aspartyl side chain at position 4 of NKB and thus now implicates placental NKB in the platelet pathology seen in preeclampsia. As it has been reported that it is the PC group per se attached to certain proteins secreted by filarial nematodes imparts them with immune inhibitory properties and thus survival in the host over long periods, attaching PC to placental secretory peptide hormones (also be found on the placental precursors of CRF, ACTH, and activin) may result in a similar situation. © 2010 Wiley Periodicals,Inc. Biopolymers (Pept Sci) 96: 189–192, 2011.</description><identifier>ISSN: 0006-3525</identifier><identifier>EISSN: 1097-0282</identifier><identifier>DOI: 10.1002/bip.21407</identifier><identifier>PMID: 20564011</identifier><language>eng</language><publisher>Hoboken: Wiley Subscription Services, Inc., A Wiley Company</publisher><subject>Animals ; CRF ; Female ; Humans ; Lipoylation - physiology ; NKB ; phosphocholine ; placenta ; Placenta - metabolism ; Platelet Activating Factor - analogs & derivatives ; Platelet Activating Factor - chemistry ; Platelet Activating Factor - metabolism ; Pregnancy ; Pregnancy Proteins - metabolism ; Protein Processing, Post-Translational - physiology</subject><ispartof>Biopolymers, 2011, Vol.96 (2), p.189-192</ispartof><rights>Copyright © 2010 Wiley Periodicals, Inc.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c2927-4ed3336fb3dbd4ed69242ede2256525fdfe8ee1d20feaa3c89b8762ca35732193</citedby><cites>FETCH-LOGICAL-c2927-4ed3336fb3dbd4ed69242ede2256525fdfe8ee1d20feaa3c89b8762ca35732193</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1002%2Fbip.21407$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1002%2Fbip.21407$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,780,784,1416,4022,27922,27923,27924,45573,45574</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/20564011$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Lowry, Philip</creatorcontrib><title>1-O-alkenyl-sn-glyceryl-3-phosphorylcholine may be a novel posttranslational modification used by the placenta</title><title>Biopolymers</title><addtitle>Biopolymers</addtitle><description>Neurokinin B (NKB) secreted by the placenta was previously found to be raised in preeclampsia and most of the symptoms in this disease appeared to be through progressive activation of the three neurokinin receptors. Further characterization of placental NKB revealed that placental NKB eluted in the approximate position of a 13mer and this was confirmed by TOF mass spectrometry which gave a mass of 1580. Although this is consistent with dimethylated NKB‐Gly‐Lys‐Arg, further characterization (immunological and mass spectrometric fragment analysis) suggested a novel posttranslational modification containing phosphocholine (PC) with some evidence for glycerol and a coordinated alkene. The structure that fits all the data is that a form of platelet activating factor is attached to the aspartyl side chain at position 4 of NKB and thus now implicates placental NKB in the platelet pathology seen in preeclampsia. As it has been reported that it is the PC group per se attached to certain proteins secreted by filarial nematodes imparts them with immune inhibitory properties and thus survival in the host over long periods, attaching PC to placental secretory peptide hormones (also be found on the placental precursors of CRF, ACTH, and activin) may result in a similar situation. © 2010 Wiley Periodicals,Inc. Biopolymers (Pept Sci) 96: 189–192, 2011.</description><subject>Animals</subject><subject>CRF</subject><subject>Female</subject><subject>Humans</subject><subject>Lipoylation - physiology</subject><subject>NKB</subject><subject>phosphocholine</subject><subject>placenta</subject><subject>Placenta - metabolism</subject><subject>Platelet Activating Factor - analogs & derivatives</subject><subject>Platelet Activating Factor - chemistry</subject><subject>Platelet Activating Factor - metabolism</subject><subject>Pregnancy</subject><subject>Pregnancy Proteins - metabolism</subject><subject>Protein Processing, Post-Translational - physiology</subject><issn>0006-3525</issn><issn>1097-0282</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2011</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kEFv1DAQhS0EokvhwB9AviEObsd2EidHKLRUWrUcQHCzHHvCmjp2iLNA_j2m2_bGYTTzpO89aR4hLzmccABx2vvpRPAK1COy4dApBqIVj8kGABoma1EfkWc5_wCoKsnhKTkSUDcVcL4hkbNrZsINxjWwHNn3sFqcyy3ZtEu5TBF2l4KPSEez0h6poTH9wkCnlJdlNjEHs_gUTaBjcn7w9lbSfUZH-5UuO6RTMBbjYp6TJ4MJGV_c7WPy5fzD57OPbHt9cXn2dsus6IRiFTopZTP00vWuiKYTlUCHQtRNeWdwA7aI3AkY0Bhp265vVSOskbWSgnfymLw-5E5z-rnHvOjRZ4shmIhpn3WrKtF1wOtCvjmQdk45zzjoafajmVfNQf9rV5d29W27hX11l7rvR3QP5H2dBTg9AL99wPX_Sfrd5af7SHZw-LzgnweHmW90o6Sq9deri2J-f66a7ZX-Jv8Cgv-UWQ</recordid><startdate>2011</startdate><enddate>2011</enddate><creator>Lowry, Philip</creator><general>Wiley Subscription Services, Inc., A Wiley Company</general><scope>BSCLL</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>2011</creationdate><title>1-O-alkenyl-sn-glyceryl-3-phosphorylcholine may be a novel posttranslational modification used by the placenta</title><author>Lowry, Philip</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c2927-4ed3336fb3dbd4ed69242ede2256525fdfe8ee1d20feaa3c89b8762ca35732193</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2011</creationdate><topic>Animals</topic><topic>CRF</topic><topic>Female</topic><topic>Humans</topic><topic>Lipoylation - physiology</topic><topic>NKB</topic><topic>phosphocholine</topic><topic>placenta</topic><topic>Placenta - metabolism</topic><topic>Platelet Activating Factor - analogs & derivatives</topic><topic>Platelet Activating Factor - chemistry</topic><topic>Platelet Activating Factor - metabolism</topic><topic>Pregnancy</topic><topic>Pregnancy Proteins - metabolism</topic><topic>Protein Processing, Post-Translational - physiology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Lowry, Philip</creatorcontrib><collection>Istex</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>Biopolymers</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Lowry, Philip</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>1-O-alkenyl-sn-glyceryl-3-phosphorylcholine may be a novel posttranslational modification used by the placenta</atitle><jtitle>Biopolymers</jtitle><addtitle>Biopolymers</addtitle><date>2011</date><risdate>2011</risdate><volume>96</volume><issue>2</issue><spage>189</spage><epage>192</epage><pages>189-192</pages><issn>0006-3525</issn><eissn>1097-0282</eissn><abstract>Neurokinin B (NKB) secreted by the placenta was previously found to be raised in preeclampsia and most of the symptoms in this disease appeared to be through progressive activation of the three neurokinin receptors. Further characterization of placental NKB revealed that placental NKB eluted in the approximate position of a 13mer and this was confirmed by TOF mass spectrometry which gave a mass of 1580. Although this is consistent with dimethylated NKB‐Gly‐Lys‐Arg, further characterization (immunological and mass spectrometric fragment analysis) suggested a novel posttranslational modification containing phosphocholine (PC) with some evidence for glycerol and a coordinated alkene. The structure that fits all the data is that a form of platelet activating factor is attached to the aspartyl side chain at position 4 of NKB and thus now implicates placental NKB in the platelet pathology seen in preeclampsia. 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subjects | Animals CRF Female Humans Lipoylation - physiology NKB phosphocholine placenta Placenta - metabolism Platelet Activating Factor - analogs & derivatives Platelet Activating Factor - chemistry Platelet Activating Factor - metabolism Pregnancy Pregnancy Proteins - metabolism Protein Processing, Post-Translational - physiology |
title | 1-O-alkenyl-sn-glyceryl-3-phosphorylcholine may be a novel posttranslational modification used by the placenta |
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