Sulfation of chlorotyrosine and nitrotyrosine by human lung endothelial and epithelial cells: Role of the human SULT1A3
During inflammation, potent reactive oxidants formed may cause chlorination and nitration of both free and protein-bound tyrosine. In addition to serving as biomarkers of inflammation-mediated oxidative stress, elevated levels of chlorotyrosine and nitrotyrosine have been linked to the pathogenesis...
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| Veröffentlicht in: | Toxicology and applied pharmacology 2011-03, Vol.251 (2), p.104-109 |
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| creator | Yasuda, Shin Yasuda, Tomoko Liu, Ming-Yih Shetty, Sreerama Idell, Steven Boggaram, Vijayakumar Suiko, Masahito Sakakibara, Yoichi Fu, Jian Liu, Ming-Cheh |
| description | During inflammation, potent reactive oxidants formed may cause chlorination and nitration of both free and protein-bound tyrosine. In addition to serving as biomarkers of inflammation-mediated oxidative stress, elevated levels of chlorotyrosine and nitrotyrosine have been linked to the pathogenesis of lung and vascular disorders. The current study was designed to investigate whether the lung cells are equipped with mechanisms for counteracting these tyrosine derivatives. By metabolic labeling, chlorotyrosine
O-[
35S]sulfate and nitrotyrosine
O-[
35S]sulfate were found to be generated and released into the labeling media of human lung endothelial and epithelial cells labeled with [
35S]sulfate in the presence of added chlorotyrosine and nitrotyrosine. Enzymatic assays using the eleven known human cytosolic sulfotransferases (SULTs) revealed SULT1A3 as the enzyme responsible for catalyzing the sulfation of chlorotyrosine and nitrotyrosine. Reverse transcription-polymerase chain reaction (RT-PCR) analysis demonstrated the expression of SULT1A3 in the lung endothelial and epithelial cells used in this study. Kinetic constants of the sulfation of chlorotyrosine and nitrotyrosine by SULT1A3 were determined. Collectively, these results suggest that sulfation by SULT1A3 in lung endothelial and epithelial cells may play a role in the inactivation and/or disposal of excess chlorotyrosine and nitrotyrosine generated during inflammation. |
| doi_str_mv | 10.1016/j.taap.2010.12.006 |
| format | Article |
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O-[
35S]sulfate and nitrotyrosine
O-[
35S]sulfate were found to be generated and released into the labeling media of human lung endothelial and epithelial cells labeled with [
35S]sulfate in the presence of added chlorotyrosine and nitrotyrosine. Enzymatic assays using the eleven known human cytosolic sulfotransferases (SULTs) revealed SULT1A3 as the enzyme responsible for catalyzing the sulfation of chlorotyrosine and nitrotyrosine. Reverse transcription-polymerase chain reaction (RT-PCR) analysis demonstrated the expression of SULT1A3 in the lung endothelial and epithelial cells used in this study. Kinetic constants of the sulfation of chlorotyrosine and nitrotyrosine by SULT1A3 were determined. Collectively, these results suggest that sulfation by SULT1A3 in lung endothelial and epithelial cells may play a role in the inactivation and/or disposal of excess chlorotyrosine and nitrotyrosine generated during inflammation.</description><identifier>ISSN: 0041-008X</identifier><identifier>EISSN: 1096-0333</identifier><identifier>DOI: 10.1016/j.taap.2010.12.006</identifier><identifier>PMID: 21168432</identifier><identifier>CODEN: TXAPA9</identifier><language>eng</language><publisher>Amsterdam: Elsevier Inc</publisher><subject>60 APPLIED LIFE SCIENCES ; AMINO ACIDS ; ANIMAL CELLS ; Arylsulfotransferase ; Biological and medical sciences ; BIOLOGICAL MARKERS ; BODY ; CARBOXYLIC ACIDS ; Cell Line ; CHEMICAL REACTIONS ; CHLORINATION ; Chlorotyrosine ; Endothelial Cells - metabolism ; Endothelial Cells - pathology ; ENZYMES ; GENE AMPLIFICATION ; HALOGENATION ; HUMAN POPULATIONS ; Humans ; HYDROXY ACIDS ; INFLAMMATION ; Inflammation Mediators - physiology ; LABELLING ; Lung - metabolism ; Lung - pathology ; LUNGS ; Medical sciences ; NITRATION ; Nitrotyrosine ; ORGANIC ACIDS ; ORGANIC COMPOUNDS ; ORGANS ; OXIDATION ; OXYGEN COMPOUNDS ; PATHOGENESIS ; PATHOLOGICAL CHANGES ; POLYMERASE CHAIN REACTION ; POPULATIONS ; PROTEINS ; Respiratory Mucosa - metabolism ; Respiratory Mucosa - pathology ; RESPIRATORY SYSTEM ; RESPIRATORY TRACT CELLS ; SOMATIC CELLS ; SULFATES ; Sulfates - chemistry ; Sulfates - metabolism ; SULFATION ; Sulfotransferase ; Sulfotransferases - physiology ; SULFUR COMPOUNDS ; SULT1A3 ; SYMPTOMS ; Toxicology ; TYROSINE ; Tyrosine - analogs & derivatives ; Tyrosine - antagonists & inhibitors ; Tyrosine - chemistry ; Tyrosine - metabolism</subject><ispartof>Toxicology and applied pharmacology, 2011-03, Vol.251 (2), p.104-109</ispartof><rights>2010 Elsevier Inc.</rights><rights>2015 INIST-CNRS</rights><rights>Copyright © 2010 Elsevier Inc. All rights reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c511t-7f28545b632fffa7445386b22a233dc2f6f7037f0e30af37624a3653ec9a71fa3</citedby><cites>FETCH-LOGICAL-c511t-7f28545b632fffa7445386b22a233dc2f6f7037f0e30af37624a3653ec9a71fa3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0041008X10004552$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>230,314,776,780,881,3537,27901,27902,65534</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=23972924$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/21168432$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://www.osti.gov/biblio/21535248$$D View this record in Osti.gov$$Hfree_for_read</backlink></links><search><creatorcontrib>Yasuda, Shin</creatorcontrib><creatorcontrib>Yasuda, Tomoko</creatorcontrib><creatorcontrib>Liu, Ming-Yih</creatorcontrib><creatorcontrib>Shetty, Sreerama</creatorcontrib><creatorcontrib>Idell, Steven</creatorcontrib><creatorcontrib>Boggaram, Vijayakumar</creatorcontrib><creatorcontrib>Suiko, Masahito</creatorcontrib><creatorcontrib>Sakakibara, Yoichi</creatorcontrib><creatorcontrib>Fu, Jian</creatorcontrib><creatorcontrib>Liu, Ming-Cheh</creatorcontrib><title>Sulfation of chlorotyrosine and nitrotyrosine by human lung endothelial and epithelial cells: Role of the human SULT1A3</title><title>Toxicology and applied pharmacology</title><addtitle>Toxicol Appl Pharmacol</addtitle><description>During inflammation, potent reactive oxidants formed may cause chlorination and nitration of both free and protein-bound tyrosine. In addition to serving as biomarkers of inflammation-mediated oxidative stress, elevated levels of chlorotyrosine and nitrotyrosine have been linked to the pathogenesis of lung and vascular disorders. The current study was designed to investigate whether the lung cells are equipped with mechanisms for counteracting these tyrosine derivatives. By metabolic labeling, chlorotyrosine
O-[
35S]sulfate and nitrotyrosine
O-[
35S]sulfate were found to be generated and released into the labeling media of human lung endothelial and epithelial cells labeled with [
35S]sulfate in the presence of added chlorotyrosine and nitrotyrosine. Enzymatic assays using the eleven known human cytosolic sulfotransferases (SULTs) revealed SULT1A3 as the enzyme responsible for catalyzing the sulfation of chlorotyrosine and nitrotyrosine. Reverse transcription-polymerase chain reaction (RT-PCR) analysis demonstrated the expression of SULT1A3 in the lung endothelial and epithelial cells used in this study. Kinetic constants of the sulfation of chlorotyrosine and nitrotyrosine by SULT1A3 were determined. Collectively, these results suggest that sulfation by SULT1A3 in lung endothelial and epithelial cells may play a role in the inactivation and/or disposal of excess chlorotyrosine and nitrotyrosine generated during inflammation.</description><subject>60 APPLIED LIFE SCIENCES</subject><subject>AMINO ACIDS</subject><subject>ANIMAL CELLS</subject><subject>Arylsulfotransferase</subject><subject>Biological and medical sciences</subject><subject>BIOLOGICAL MARKERS</subject><subject>BODY</subject><subject>CARBOXYLIC ACIDS</subject><subject>Cell Line</subject><subject>CHEMICAL REACTIONS</subject><subject>CHLORINATION</subject><subject>Chlorotyrosine</subject><subject>Endothelial Cells - metabolism</subject><subject>Endothelial Cells - pathology</subject><subject>ENZYMES</subject><subject>GENE AMPLIFICATION</subject><subject>HALOGENATION</subject><subject>HUMAN POPULATIONS</subject><subject>Humans</subject><subject>HYDROXY ACIDS</subject><subject>INFLAMMATION</subject><subject>Inflammation Mediators - physiology</subject><subject>LABELLING</subject><subject>Lung - metabolism</subject><subject>Lung - pathology</subject><subject>LUNGS</subject><subject>Medical sciences</subject><subject>NITRATION</subject><subject>Nitrotyrosine</subject><subject>ORGANIC ACIDS</subject><subject>ORGANIC COMPOUNDS</subject><subject>ORGANS</subject><subject>OXIDATION</subject><subject>OXYGEN COMPOUNDS</subject><subject>PATHOGENESIS</subject><subject>PATHOLOGICAL CHANGES</subject><subject>POLYMERASE CHAIN REACTION</subject><subject>POPULATIONS</subject><subject>PROTEINS</subject><subject>Respiratory Mucosa - metabolism</subject><subject>Respiratory Mucosa - pathology</subject><subject>RESPIRATORY SYSTEM</subject><subject>RESPIRATORY TRACT CELLS</subject><subject>SOMATIC CELLS</subject><subject>SULFATES</subject><subject>Sulfates - chemistry</subject><subject>Sulfates - metabolism</subject><subject>SULFATION</subject><subject>Sulfotransferase</subject><subject>Sulfotransferases - physiology</subject><subject>SULFUR COMPOUNDS</subject><subject>SULT1A3</subject><subject>SYMPTOMS</subject><subject>Toxicology</subject><subject>TYROSINE</subject><subject>Tyrosine - analogs & derivatives</subject><subject>Tyrosine - antagonists & inhibitors</subject><subject>Tyrosine - chemistry</subject><subject>Tyrosine - metabolism</subject><issn>0041-008X</issn><issn>1096-0333</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2011</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kUuLFDEUhYMoTs_oH3AhBSKzqjavSlXJbIbBFzQIzgy4C-nUjZ0mnbRJSul_b2L3qCtX4V6-c8g9B6EXBC8JJuLNdpmV2i8prgu6xFg8QguCR9FixthjtMCYkxbj4esZOk9pizEeOSdP0RklRAyc0QX6eTs7o7INvgmm0RsXYsiHGJL10Cg_Nd7mfzbrQ7OZd8o3bvbfGvBTyBtwVrnfLOztw6jBufS2-RIcVOOyPglv71d35Jo9Q0-Mcgmen94LdP_-3d3Nx3b1-cOnm-tVqztCctsbOnS8WwtGjTGq57xjg1hTqihjk6ZGmB6z3mBgWBnWC8oVEx0DPaqeGMUu0Kujb0jZyqRtBr3RwXvQWVLSsY7yoVCXR2ofw_cZUpY7m-oJykOYkxw7LkqkopL0SOqSSIpg5D7anYoHSbCsrcitrK3I2ookVJZWiujlyX5e72D6I3mooQCvT4BKWjkTldc2_eXY2NOR8sJdHTkokf2wEOtF4DVMNtaDpmD_949fVIWqrQ</recordid><startdate>20110301</startdate><enddate>20110301</enddate><creator>Yasuda, Shin</creator><creator>Yasuda, Tomoko</creator><creator>Liu, Ming-Yih</creator><creator>Shetty, Sreerama</creator><creator>Idell, Steven</creator><creator>Boggaram, Vijayakumar</creator><creator>Suiko, Masahito</creator><creator>Sakakibara, Yoichi</creator><creator>Fu, Jian</creator><creator>Liu, Ming-Cheh</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>7U7</scope><scope>C1K</scope><scope>OTOTI</scope></search><sort><creationdate>20110301</creationdate><title>Sulfation of chlorotyrosine and nitrotyrosine by human lung endothelial and epithelial cells: Role of the human SULT1A3</title><author>Yasuda, Shin ; Yasuda, Tomoko ; Liu, Ming-Yih ; Shetty, Sreerama ; Idell, Steven ; Boggaram, Vijayakumar ; Suiko, Masahito ; Sakakibara, Yoichi ; Fu, Jian ; Liu, Ming-Cheh</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c511t-7f28545b632fffa7445386b22a233dc2f6f7037f0e30af37624a3653ec9a71fa3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2011</creationdate><topic>60 APPLIED LIFE SCIENCES</topic><topic>AMINO ACIDS</topic><topic>ANIMAL CELLS</topic><topic>Arylsulfotransferase</topic><topic>Biological and medical sciences</topic><topic>BIOLOGICAL MARKERS</topic><topic>BODY</topic><topic>CARBOXYLIC ACIDS</topic><topic>Cell Line</topic><topic>CHEMICAL REACTIONS</topic><topic>CHLORINATION</topic><topic>Chlorotyrosine</topic><topic>Endothelial Cells - metabolism</topic><topic>Endothelial Cells - pathology</topic><topic>ENZYMES</topic><topic>GENE AMPLIFICATION</topic><topic>HALOGENATION</topic><topic>HUMAN POPULATIONS</topic><topic>Humans</topic><topic>HYDROXY ACIDS</topic><topic>INFLAMMATION</topic><topic>Inflammation Mediators - physiology</topic><topic>LABELLING</topic><topic>Lung - metabolism</topic><topic>Lung - pathology</topic><topic>LUNGS</topic><topic>Medical sciences</topic><topic>NITRATION</topic><topic>Nitrotyrosine</topic><topic>ORGANIC ACIDS</topic><topic>ORGANIC COMPOUNDS</topic><topic>ORGANS</topic><topic>OXIDATION</topic><topic>OXYGEN COMPOUNDS</topic><topic>PATHOGENESIS</topic><topic>PATHOLOGICAL CHANGES</topic><topic>POLYMERASE CHAIN REACTION</topic><topic>POPULATIONS</topic><topic>PROTEINS</topic><topic>Respiratory Mucosa - metabolism</topic><topic>Respiratory Mucosa - pathology</topic><topic>RESPIRATORY SYSTEM</topic><topic>RESPIRATORY TRACT CELLS</topic><topic>SOMATIC CELLS</topic><topic>SULFATES</topic><topic>Sulfates - chemistry</topic><topic>Sulfates - metabolism</topic><topic>SULFATION</topic><topic>Sulfotransferase</topic><topic>Sulfotransferases - physiology</topic><topic>SULFUR COMPOUNDS</topic><topic>SULT1A3</topic><topic>SYMPTOMS</topic><topic>Toxicology</topic><topic>TYROSINE</topic><topic>Tyrosine - analogs & derivatives</topic><topic>Tyrosine - antagonists & inhibitors</topic><topic>Tyrosine - chemistry</topic><topic>Tyrosine - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Yasuda, Shin</creatorcontrib><creatorcontrib>Yasuda, Tomoko</creatorcontrib><creatorcontrib>Liu, Ming-Yih</creatorcontrib><creatorcontrib>Shetty, Sreerama</creatorcontrib><creatorcontrib>Idell, Steven</creatorcontrib><creatorcontrib>Boggaram, Vijayakumar</creatorcontrib><creatorcontrib>Suiko, Masahito</creatorcontrib><creatorcontrib>Sakakibara, Yoichi</creatorcontrib><creatorcontrib>Fu, Jian</creatorcontrib><creatorcontrib>Liu, Ming-Cheh</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>Toxicology Abstracts</collection><collection>Environmental Sciences and Pollution Management</collection><collection>OSTI.GOV</collection><jtitle>Toxicology and applied pharmacology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Yasuda, Shin</au><au>Yasuda, Tomoko</au><au>Liu, Ming-Yih</au><au>Shetty, Sreerama</au><au>Idell, Steven</au><au>Boggaram, Vijayakumar</au><au>Suiko, Masahito</au><au>Sakakibara, Yoichi</au><au>Fu, Jian</au><au>Liu, Ming-Cheh</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Sulfation of chlorotyrosine and nitrotyrosine by human lung endothelial and epithelial cells: Role of the human SULT1A3</atitle><jtitle>Toxicology and applied pharmacology</jtitle><addtitle>Toxicol Appl Pharmacol</addtitle><date>2011-03-01</date><risdate>2011</risdate><volume>251</volume><issue>2</issue><spage>104</spage><epage>109</epage><pages>104-109</pages><issn>0041-008X</issn><eissn>1096-0333</eissn><coden>TXAPA9</coden><abstract>During inflammation, potent reactive oxidants formed may cause chlorination and nitration of both free and protein-bound tyrosine. In addition to serving as biomarkers of inflammation-mediated oxidative stress, elevated levels of chlorotyrosine and nitrotyrosine have been linked to the pathogenesis of lung and vascular disorders. The current study was designed to investigate whether the lung cells are equipped with mechanisms for counteracting these tyrosine derivatives. By metabolic labeling, chlorotyrosine
O-[
35S]sulfate and nitrotyrosine
O-[
35S]sulfate were found to be generated and released into the labeling media of human lung endothelial and epithelial cells labeled with [
35S]sulfate in the presence of added chlorotyrosine and nitrotyrosine. Enzymatic assays using the eleven known human cytosolic sulfotransferases (SULTs) revealed SULT1A3 as the enzyme responsible for catalyzing the sulfation of chlorotyrosine and nitrotyrosine. Reverse transcription-polymerase chain reaction (RT-PCR) analysis demonstrated the expression of SULT1A3 in the lung endothelial and epithelial cells used in this study. Kinetic constants of the sulfation of chlorotyrosine and nitrotyrosine by SULT1A3 were determined. Collectively, these results suggest that sulfation by SULT1A3 in lung endothelial and epithelial cells may play a role in the inactivation and/or disposal of excess chlorotyrosine and nitrotyrosine generated during inflammation.</abstract><cop>Amsterdam</cop><pub>Elsevier Inc</pub><pmid>21168432</pmid><doi>10.1016/j.taap.2010.12.006</doi><tpages>6</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0041-008X |
| ispartof | Toxicology and applied pharmacology, 2011-03, Vol.251 (2), p.104-109 |
| issn | 0041-008X 1096-0333 |
| language | eng |
| recordid | cdi_osti_scitechconnect_21535248 |
| source | MEDLINE; Elsevier ScienceDirect Journals |
| subjects | 60 APPLIED LIFE SCIENCES AMINO ACIDS ANIMAL CELLS Arylsulfotransferase Biological and medical sciences BIOLOGICAL MARKERS BODY CARBOXYLIC ACIDS Cell Line CHEMICAL REACTIONS CHLORINATION Chlorotyrosine Endothelial Cells - metabolism Endothelial Cells - pathology ENZYMES GENE AMPLIFICATION HALOGENATION HUMAN POPULATIONS Humans HYDROXY ACIDS INFLAMMATION Inflammation Mediators - physiology LABELLING Lung - metabolism Lung - pathology LUNGS Medical sciences NITRATION Nitrotyrosine ORGANIC ACIDS ORGANIC COMPOUNDS ORGANS OXIDATION OXYGEN COMPOUNDS PATHOGENESIS PATHOLOGICAL CHANGES POLYMERASE CHAIN REACTION POPULATIONS PROTEINS Respiratory Mucosa - metabolism Respiratory Mucosa - pathology RESPIRATORY SYSTEM RESPIRATORY TRACT CELLS SOMATIC CELLS SULFATES Sulfates - chemistry Sulfates - metabolism SULFATION Sulfotransferase Sulfotransferases - physiology SULFUR COMPOUNDS SULT1A3 SYMPTOMS Toxicology TYROSINE Tyrosine - analogs & derivatives Tyrosine - antagonists & inhibitors Tyrosine - chemistry Tyrosine - metabolism |
| title | Sulfation of chlorotyrosine and nitrotyrosine by human lung endothelial and epithelial cells: Role of the human SULT1A3 |
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