Photoaffinity labelling of human leukotriene C4 synthase in THP‐1 cell membranes
Human leukotriene C4 synthase specific activity in the human monocytic leukemia cell line THP‐1 (0.302 ± 0.062 nmol LTC4 formed · min−1 mg−1) was 7.6‐fold higher than in U937 cells (0.040 ± 0.017 nmol LTC4 formed · min−1 · mg−1) and comparable to dimethylsulfoxide‐differentiated U937 cells (0.399 ±...
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| Veröffentlicht in: | FEBS letters 1993-02, Vol.317 (3), p.195-201 |
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| creator | Ali, Ambereen Zamboni, Robert J. Ford-Hutchinson, Anthony W. Nicholson, Donald W. |
| description | Human leukotriene C4 synthase specific activity in the human monocytic leukemia cell line THP‐1 (0.302 ± 0.062 nmol LTC4 formed · min−1 mg−1) was 7.6‐fold higher than in U937 cells (0.040 ± 0.017 nmol LTC4 formed · min−1 · mg−1) and comparable to dimethylsulfoxide‐differentiated U937 cells (0.399 ± 0.084 nmol LTC4 formed · min−1 · mg−1). Using the photoaffinity probe, azido[125I]‐LTC4, a single polypeptide with a molecular mass of 18 kDa was specifically labelled in THP‐1 microsomal membranes. The rank order of potencies for competition of azido[125I]‐LTC4 photolabelling of the 18 kDa protein by glutathione, leukotrienes and their analogs was found to be LTC2 > (azido[127I]‐LTC4 ≈ LTC4) > (LTD4 ≈ LTE4) > (LTA4 ≈ LTB4) > S‐hexyl glutathione > glutathione, corresponded with the rank order of potencies for inhibition of LTC4 synthase activity but not inhibition of microsomal glutathione S‐transferase activity. The 18 kDa protein specifically labelled by azido[125I]‐LTC4 had high specificity for LTC4 and closely related leukotrienes and was separable from microsomal glutathione S‐transferase. We conclude that azido[125I]‐LTC4 specifically photolabels LTC4 synthase which is an 18 kDa polypeptide or contains an 18 kDa subunit. |
| doi_str_mv | 10.1016/0014-5793(93)81275-5 |
| format | Article |
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Using the photoaffinity probe, azido[125I]‐LTC4, a single polypeptide with a molecular mass of 18 kDa was specifically labelled in THP‐1 microsomal membranes. The rank order of potencies for competition of azido[125I]‐LTC4 photolabelling of the 18 kDa protein by glutathione, leukotrienes and their analogs was found to be LTC2 > (azido[127I]‐LTC4 ≈ LTC4) > (LTD4 ≈ LTE4) > (LTA4 ≈ LTB4) > S‐hexyl glutathione > glutathione, corresponded with the rank order of potencies for inhibition of LTC4 synthase activity but not inhibition of microsomal glutathione S‐transferase activity. The 18 kDa protein specifically labelled by azido[125I]‐LTC4 had high specificity for LTC4 and closely related leukotrienes and was separable from microsomal glutathione S‐transferase. We conclude that azido[125I]‐LTC4 specifically photolabels LTC4 synthase which is an 18 kDa polypeptide or contains an 18 kDa subunit.</description><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1016/0014-5793(93)81275-5</identifier><identifier>PMID: 8425605</identifier><identifier>CODEN: FEBLAL</identifier><language>eng</language><publisher>Amsterdam: Elsevier</publisher><subject>Affinity Labels ; Analytical, structural and metabolic biochemistry ; Binding, Competitive ; Biological and medical sciences ; Cell Line ; Enzymes and enzyme inhibitors ; Fundamental and applied biological sciences. Psychology ; Glutathione S-transferase ; Glutathione Transferase - analysis ; Glutathione Transferase - antagonists & inhibitors ; Glutathione Transferase - chemistry ; Humans ; Intracellular Membranes - enzymology ; Leukotriene ; LTC4 synthase ; Membrane photolabel ; Microsomes - enzymology ; Molecular Weight ; Monocytes - enzymology ; PBS ; phosphate-buffered saline ; Photochemistry ; SDS ; sodium dodecyl sulfate ; Solubility ; Taurocholic Acid ; Transferases</subject><ispartof>FEBS letters, 1993-02, Vol.317 (3), p.195-201</ispartof><rights>FEBS Letters 317 (1993) 1873-3468 © 2015 Federation of European Biochemical Societies</rights><rights>1993 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27903,27904</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=4573817$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8425605$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Ali, Ambereen</creatorcontrib><creatorcontrib>Zamboni, Robert J.</creatorcontrib><creatorcontrib>Ford-Hutchinson, Anthony W.</creatorcontrib><creatorcontrib>Nicholson, Donald W.</creatorcontrib><title>Photoaffinity labelling of human leukotriene C4 synthase in THP‐1 cell membranes</title><title>FEBS letters</title><addtitle>FEBS Lett</addtitle><description>Human leukotriene C4 synthase specific activity in the human monocytic leukemia cell line THP‐1 (0.302 ± 0.062 nmol LTC4 formed · min−1 mg−1) was 7.6‐fold higher than in U937 cells (0.040 ± 0.017 nmol LTC4 formed · min−1 · mg−1) and comparable to dimethylsulfoxide‐differentiated U937 cells (0.399 ± 0.084 nmol LTC4 formed · min−1 · mg−1). Using the photoaffinity probe, azido[125I]‐LTC4, a single polypeptide with a molecular mass of 18 kDa was specifically labelled in THP‐1 microsomal membranes. The rank order of potencies for competition of azido[125I]‐LTC4 photolabelling of the 18 kDa protein by glutathione, leukotrienes and their analogs was found to be LTC2 > (azido[127I]‐LTC4 ≈ LTC4) > (LTD4 ≈ LTE4) > (LTA4 ≈ LTB4) > S‐hexyl glutathione > glutathione, corresponded with the rank order of potencies for inhibition of LTC4 synthase activity but not inhibition of microsomal glutathione S‐transferase activity. The 18 kDa protein specifically labelled by azido[125I]‐LTC4 had high specificity for LTC4 and closely related leukotrienes and was separable from microsomal glutathione S‐transferase. We conclude that azido[125I]‐LTC4 specifically photolabels LTC4 synthase which is an 18 kDa polypeptide or contains an 18 kDa subunit.</description><subject>Affinity Labels</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Binding, Competitive</subject><subject>Biological and medical sciences</subject><subject>Cell Line</subject><subject>Enzymes and enzyme inhibitors</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Glutathione S-transferase</subject><subject>Glutathione Transferase - analysis</subject><subject>Glutathione Transferase - antagonists & inhibitors</subject><subject>Glutathione Transferase - chemistry</subject><subject>Humans</subject><subject>Intracellular Membranes - enzymology</subject><subject>Leukotriene</subject><subject>LTC4 synthase</subject><subject>Membrane photolabel</subject><subject>Microsomes - enzymology</subject><subject>Molecular Weight</subject><subject>Monocytes - enzymology</subject><subject>PBS</subject><subject>phosphate-buffered saline</subject><subject>Photochemistry</subject><subject>SDS</subject><subject>sodium dodecyl sulfate</subject><subject>Solubility</subject><subject>Taurocholic Acid</subject><subject>Transferases</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1993</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNo9kc9KAzEQxoMotVbfQCEHET2sJpvMJjlqaa1QsEg9h-xu1kb3T93sIr35CD6jT-KuLYWBYeb7TZh8g9A5JbeU0OiOEMoDEIpdK3YjaSgggAM0pFKwgPFIHqLhHjlGJ96_k66WVA3QQPIQIgJD9LJYVU1lssyVrtng3MQ2z135hqsMr9rClDi37UfV1M6WFo859puyWRlvsSvxcrb4_f6hOOlmcGGLuDal9afoKDO5t2e7PEKv08lyPAvmz49P4_t5sGacQ0BDQ5hSSZQpBqHKgJtImjQhMlVEgKUhjVObMAIqljEkVrFIxTFTIkuJkpyN0NX23XVdfbbWN7pwvl-lW6JqvRYAXAoFHXixA9u4sKle164w9UbvTOj0y51ufGLyrPtF4vwe4yCYpKLDplvsy-V2s5cp0f05dO-17r3WXfyfQ4OeTh7CXuj7iv13gf0Bi-p-_w</recordid><startdate>19930215</startdate><enddate>19930215</enddate><creator>Ali, Ambereen</creator><creator>Zamboni, Robert J.</creator><creator>Ford-Hutchinson, Anthony W.</creator><creator>Nicholson, Donald W.</creator><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>7X8</scope></search><sort><creationdate>19930215</creationdate><title>Photoaffinity labelling of human leukotriene C4 synthase in THP‐1 cell membranes</title><author>Ali, Ambereen ; Zamboni, Robert J. ; Ford-Hutchinson, Anthony W. ; Nicholson, Donald W.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-p3445-12a0399c6f93529f54a68adc08d9075e121bdec3059b8b5ce9369bb397fd09843</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1993</creationdate><topic>Affinity Labels</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Binding, Competitive</topic><topic>Biological and medical sciences</topic><topic>Cell Line</topic><topic>Enzymes and enzyme inhibitors</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Glutathione S-transferase</topic><topic>Glutathione Transferase - analysis</topic><topic>Glutathione Transferase - antagonists & inhibitors</topic><topic>Glutathione Transferase - chemistry</topic><topic>Humans</topic><topic>Intracellular Membranes - enzymology</topic><topic>Leukotriene</topic><topic>LTC4 synthase</topic><topic>Membrane photolabel</topic><topic>Microsomes - enzymology</topic><topic>Molecular Weight</topic><topic>Monocytes - enzymology</topic><topic>PBS</topic><topic>phosphate-buffered saline</topic><topic>Photochemistry</topic><topic>SDS</topic><topic>sodium dodecyl sulfate</topic><topic>Solubility</topic><topic>Taurocholic Acid</topic><topic>Transferases</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Ali, Ambereen</creatorcontrib><creatorcontrib>Zamboni, Robert J.</creatorcontrib><creatorcontrib>Ford-Hutchinson, Anthony W.</creatorcontrib><creatorcontrib>Nicholson, Donald W.</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>MEDLINE - Academic</collection><jtitle>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Ali, Ambereen</au><au>Zamboni, Robert J.</au><au>Ford-Hutchinson, Anthony W.</au><au>Nicholson, Donald W.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Photoaffinity labelling of human leukotriene C4 synthase in THP‐1 cell membranes</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>1993-02-15</date><risdate>1993</risdate><volume>317</volume><issue>3</issue><spage>195</spage><epage>201</epage><pages>195-201</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><coden>FEBLAL</coden><abstract>Human leukotriene C4 synthase specific activity in the human monocytic leukemia cell line THP‐1 (0.302 ± 0.062 nmol LTC4 formed · min−1 mg−1) was 7.6‐fold higher than in U937 cells (0.040 ± 0.017 nmol LTC4 formed · min−1 · mg−1) and comparable to dimethylsulfoxide‐differentiated U937 cells (0.399 ± 0.084 nmol LTC4 formed · min−1 · mg−1). Using the photoaffinity probe, azido[125I]‐LTC4, a single polypeptide with a molecular mass of 18 kDa was specifically labelled in THP‐1 microsomal membranes. The rank order of potencies for competition of azido[125I]‐LTC4 photolabelling of the 18 kDa protein by glutathione, leukotrienes and their analogs was found to be LTC2 > (azido[127I]‐LTC4 ≈ LTC4) > (LTD4 ≈ LTE4) > (LTA4 ≈ LTB4) > S‐hexyl glutathione > glutathione, corresponded with the rank order of potencies for inhibition of LTC4 synthase activity but not inhibition of microsomal glutathione S‐transferase activity. The 18 kDa protein specifically labelled by azido[125I]‐LTC4 had high specificity for LTC4 and closely related leukotrienes and was separable from microsomal glutathione S‐transferase. We conclude that azido[125I]‐LTC4 specifically photolabels LTC4 synthase which is an 18 kDa polypeptide or contains an 18 kDa subunit.</abstract><cop>Amsterdam</cop><pub>Elsevier</pub><pmid>8425605</pmid><doi>10.1016/0014-5793(93)81275-5</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; Elsevier ScienceDirect Journals; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
| subjects | Affinity Labels Analytical, structural and metabolic biochemistry Binding, Competitive Biological and medical sciences Cell Line Enzymes and enzyme inhibitors Fundamental and applied biological sciences. Psychology Glutathione S-transferase Glutathione Transferase - analysis Glutathione Transferase - antagonists & inhibitors Glutathione Transferase - chemistry Humans Intracellular Membranes - enzymology Leukotriene LTC4 synthase Membrane photolabel Microsomes - enzymology Molecular Weight Monocytes - enzymology PBS phosphate-buffered saline Photochemistry SDS sodium dodecyl sulfate Solubility Taurocholic Acid Transferases |
| title | Photoaffinity labelling of human leukotriene C4 synthase in THP‐1 cell membranes |
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