Flavonoid glucuronides are substrates for human liver β‐glucuronidase
Quercetin glucuronides are the main circulating metabolites of quercetin in humans. We hypothesise that the potential availability of the aglycone within tissues depends on the substrate specificity of the deconjugating enzyme β‐glucuronidase towards circulating flavonoid glucuronides. Human tissues...
Gespeichert in:
| Veröffentlicht in: | FEBS letters 2001-08, Vol.503 (1), p.103-106 |
|---|---|
| Hauptverfasser: | , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 106 |
|---|---|
| container_issue | 1 |
| container_start_page | 103 |
| container_title | FEBS letters |
| container_volume | 503 |
| creator | O'Leary, Karen A Day, Andrea J Needs, Paul W Sly, William S O'Brien, Nora M Williamson, Gary |
| description | Quercetin glucuronides are the main circulating metabolites of quercetin in humans. We hypothesise that the potential availability of the aglycone within tissues depends on the substrate specificity of the deconjugating enzyme β‐glucuronidase towards circulating flavonoid glucuronides. Human tissues (small intestine, liver and neutrophils) exhibited β‐glucuronidase against quercetin glucuronides. The various quercetin glucuronides were deconjugated at similar rates, but liver cell‐free extracts were the most efficient and the activity was completely inhibited by saccharo‐1,4‐lactone (a β‐glucuronidase inhibitor). Furthermore, pure recombinant human β‐glucuronidase hydrolysed various flavonoid glucuronides, with a 20‐fold variation in catalytic efficiency (k
cat/K
m=1.3×103 M−1 s−1 for equol‐7‐O‐glucuronide and 26×103 M−1 s−1 for kaempferol‐3‐O‐glucuronide). Similar catalytic efficiencies were obtained for quercetin O‐glucuronides substituted at different positions. These results show that flavonoid glucuronides can be deconjugated by microsomal β‐glucuronidase from various human cells. |
| doi_str_mv | 10.1016/S0014-5793(01)02684-9 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_71107630</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>71107630</sourcerecordid><originalsourceid>FETCH-LOGICAL-c4179-5b725b568daa2747e8b318ee644abc2209e977999a7fbe37811de75a9f87085b3</originalsourceid><addsrcrecordid>eNqNkEFOwzAQRS0EoqVwBFBWCBYBTxzH9hKqliJVYgGsLTuZQFDSFLsp6o4jcBYOwiE4CWlawZbVaGben5EeIcdAL4BCcnlPKcQhF4qdUTinUSLjUO2QPkjBQhYncpf0f5EeOfD-hba9BLVPegAcmExYn0zGpVnWs7rIgqeySRtXz4oMfWAcBr6xfuHMom3z2gXPTWVmQVks0QVfn9_vH38B4_GQ7OWm9Hi0rQPyOB49DCfh9O7mdng1DdMYhAq5FRG3PJGZMZGIBUrLQCImcWxsGkVUoRJCKWVEbpEJCZCh4EblUlDJLRuQ083duatfG_QLXRU-xbI0M6wbrwUAFQmjLcg3YOpq7x3meu6KyriVBqrXCnWnUK_9aAq6U6hVmzvZPmhshdlfauusBSYb4K0ocfW_q3o8uo66zXpBoRsr9gO1dII6</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>71107630</pqid></control><display><type>article</type><title>Flavonoid glucuronides are substrates for human liver β‐glucuronidase</title><source>Wiley Online Library - AutoHoldings Journals</source><source>MEDLINE</source><source>Elsevier ScienceDirect Journals Complete</source><source>Wiley Free Content</source><source>EZB-FREE-00999 freely available EZB journals</source><source>Alma/SFX Local Collection</source><creator>O'Leary, Karen A ; Day, Andrea J ; Needs, Paul W ; Sly, William S ; O'Brien, Nora M ; Williamson, Gary</creator><creatorcontrib>O'Leary, Karen A ; Day, Andrea J ; Needs, Paul W ; Sly, William S ; O'Brien, Nora M ; Williamson, Gary</creatorcontrib><description>Quercetin glucuronides are the main circulating metabolites of quercetin in humans. We hypothesise that the potential availability of the aglycone within tissues depends on the substrate specificity of the deconjugating enzyme β‐glucuronidase towards circulating flavonoid glucuronides. Human tissues (small intestine, liver and neutrophils) exhibited β‐glucuronidase against quercetin glucuronides. The various quercetin glucuronides were deconjugated at similar rates, but liver cell‐free extracts were the most efficient and the activity was completely inhibited by saccharo‐1,4‐lactone (a β‐glucuronidase inhibitor). Furthermore, pure recombinant human β‐glucuronidase hydrolysed various flavonoid glucuronides, with a 20‐fold variation in catalytic efficiency (k
cat/K
m=1.3×103 M−1 s−1 for equol‐7‐O‐glucuronide and 26×103 M−1 s−1 for kaempferol‐3‐O‐glucuronide). Similar catalytic efficiencies were obtained for quercetin O‐glucuronides substituted at different positions. These results show that flavonoid glucuronides can be deconjugated by microsomal β‐glucuronidase from various human cells.</description><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1016/S0014-5793(01)02684-9</identifier><identifier>PMID: 11513863</identifier><language>eng</language><publisher>England</publisher><subject>Chromatography, High Pressure Liquid ; ER, endoplasmic reticulum ; Flavonoid ; Flavonoids - metabolism ; Glucuronidase - metabolism ; Glucuronide ; Glucuronides - metabolism ; Human ; Humans ; Kinetics ; Liver - enzymology ; p-NPGlcA, p-nitrophenol glucuronide ; Quercetin ; Recombinant Proteins - metabolism ; Substrate Specificity ; Turnover ; UDPGA, uridine-diphosphate-glucuronic acid ; UGT, uridine-diphosphate-glucuronosyltransferase ; β-Glucuronidase</subject><ispartof>FEBS letters, 2001-08, Vol.503 (1), p.103-106</ispartof><rights>FEBS Letters 503 (2001) 1873-3468 © 2015 Federation of European Biochemical Societies</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4179-5b725b568daa2747e8b318ee644abc2209e977999a7fbe37811de75a9f87085b3</citedby><cites>FETCH-LOGICAL-c4179-5b725b568daa2747e8b318ee644abc2209e977999a7fbe37811de75a9f87085b3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1016%2FS0014-5793%2801%2902684-9$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1016%2FS0014-5793%2801%2902684-9$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,780,784,1416,1432,27922,27923,45572,45573,46407,46831</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11513863$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>O'Leary, Karen A</creatorcontrib><creatorcontrib>Day, Andrea J</creatorcontrib><creatorcontrib>Needs, Paul W</creatorcontrib><creatorcontrib>Sly, William S</creatorcontrib><creatorcontrib>O'Brien, Nora M</creatorcontrib><creatorcontrib>Williamson, Gary</creatorcontrib><title>Flavonoid glucuronides are substrates for human liver β‐glucuronidase</title><title>FEBS letters</title><addtitle>FEBS Lett</addtitle><description>Quercetin glucuronides are the main circulating metabolites of quercetin in humans. We hypothesise that the potential availability of the aglycone within tissues depends on the substrate specificity of the deconjugating enzyme β‐glucuronidase towards circulating flavonoid glucuronides. Human tissues (small intestine, liver and neutrophils) exhibited β‐glucuronidase against quercetin glucuronides. The various quercetin glucuronides were deconjugated at similar rates, but liver cell‐free extracts were the most efficient and the activity was completely inhibited by saccharo‐1,4‐lactone (a β‐glucuronidase inhibitor). Furthermore, pure recombinant human β‐glucuronidase hydrolysed various flavonoid glucuronides, with a 20‐fold variation in catalytic efficiency (k
cat/K
m=1.3×103 M−1 s−1 for equol‐7‐O‐glucuronide and 26×103 M−1 s−1 for kaempferol‐3‐O‐glucuronide). Similar catalytic efficiencies were obtained for quercetin O‐glucuronides substituted at different positions. These results show that flavonoid glucuronides can be deconjugated by microsomal β‐glucuronidase from various human cells.</description><subject>Chromatography, High Pressure Liquid</subject><subject>ER, endoplasmic reticulum</subject><subject>Flavonoid</subject><subject>Flavonoids - metabolism</subject><subject>Glucuronidase - metabolism</subject><subject>Glucuronide</subject><subject>Glucuronides - metabolism</subject><subject>Human</subject><subject>Humans</subject><subject>Kinetics</subject><subject>Liver - enzymology</subject><subject>p-NPGlcA, p-nitrophenol glucuronide</subject><subject>Quercetin</subject><subject>Recombinant Proteins - metabolism</subject><subject>Substrate Specificity</subject><subject>Turnover</subject><subject>UDPGA, uridine-diphosphate-glucuronic acid</subject><subject>UGT, uridine-diphosphate-glucuronosyltransferase</subject><subject>β-Glucuronidase</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2001</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkEFOwzAQRS0EoqVwBFBWCBYBTxzH9hKqliJVYgGsLTuZQFDSFLsp6o4jcBYOwiE4CWlawZbVaGben5EeIcdAL4BCcnlPKcQhF4qdUTinUSLjUO2QPkjBQhYncpf0f5EeOfD-hba9BLVPegAcmExYn0zGpVnWs7rIgqeySRtXz4oMfWAcBr6xfuHMom3z2gXPTWVmQVks0QVfn9_vH38B4_GQ7OWm9Hi0rQPyOB49DCfh9O7mdng1DdMYhAq5FRG3PJGZMZGIBUrLQCImcWxsGkVUoRJCKWVEbpEJCZCh4EblUlDJLRuQ083duatfG_QLXRU-xbI0M6wbrwUAFQmjLcg3YOpq7x3meu6KyriVBqrXCnWnUK_9aAq6U6hVmzvZPmhshdlfauusBSYb4K0ocfW_q3o8uo66zXpBoRsr9gO1dII6</recordid><startdate>20010810</startdate><enddate>20010810</enddate><creator>O'Leary, Karen A</creator><creator>Day, Andrea J</creator><creator>Needs, Paul W</creator><creator>Sly, William S</creator><creator>O'Brien, Nora M</creator><creator>Williamson, Gary</creator><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>20010810</creationdate><title>Flavonoid glucuronides are substrates for human liver β‐glucuronidase</title><author>O'Leary, Karen A ; Day, Andrea J ; Needs, Paul W ; Sly, William S ; O'Brien, Nora M ; Williamson, Gary</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4179-5b725b568daa2747e8b318ee644abc2209e977999a7fbe37811de75a9f87085b3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2001</creationdate><topic>Chromatography, High Pressure Liquid</topic><topic>ER, endoplasmic reticulum</topic><topic>Flavonoid</topic><topic>Flavonoids - metabolism</topic><topic>Glucuronidase - metabolism</topic><topic>Glucuronide</topic><topic>Glucuronides - metabolism</topic><topic>Human</topic><topic>Humans</topic><topic>Kinetics</topic><topic>Liver - enzymology</topic><topic>p-NPGlcA, p-nitrophenol glucuronide</topic><topic>Quercetin</topic><topic>Recombinant Proteins - metabolism</topic><topic>Substrate Specificity</topic><topic>Turnover</topic><topic>UDPGA, uridine-diphosphate-glucuronic acid</topic><topic>UGT, uridine-diphosphate-glucuronosyltransferase</topic><topic>β-Glucuronidase</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>O'Leary, Karen A</creatorcontrib><creatorcontrib>Day, Andrea J</creatorcontrib><creatorcontrib>Needs, Paul W</creatorcontrib><creatorcontrib>Sly, William S</creatorcontrib><creatorcontrib>O'Brien, Nora M</creatorcontrib><creatorcontrib>Williamson, Gary</creatorcontrib><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>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>O'Leary, Karen A</au><au>Day, Andrea J</au><au>Needs, Paul W</au><au>Sly, William S</au><au>O'Brien, Nora M</au><au>Williamson, Gary</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Flavonoid glucuronides are substrates for human liver β‐glucuronidase</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>2001-08-10</date><risdate>2001</risdate><volume>503</volume><issue>1</issue><spage>103</spage><epage>106</epage><pages>103-106</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><abstract>Quercetin glucuronides are the main circulating metabolites of quercetin in humans. We hypothesise that the potential availability of the aglycone within tissues depends on the substrate specificity of the deconjugating enzyme β‐glucuronidase towards circulating flavonoid glucuronides. Human tissues (small intestine, liver and neutrophils) exhibited β‐glucuronidase against quercetin glucuronides. The various quercetin glucuronides were deconjugated at similar rates, but liver cell‐free extracts were the most efficient and the activity was completely inhibited by saccharo‐1,4‐lactone (a β‐glucuronidase inhibitor). Furthermore, pure recombinant human β‐glucuronidase hydrolysed various flavonoid glucuronides, with a 20‐fold variation in catalytic efficiency (k
cat/K
m=1.3×103 M−1 s−1 for equol‐7‐O‐glucuronide and 26×103 M−1 s−1 for kaempferol‐3‐O‐glucuronide). Similar catalytic efficiencies were obtained for quercetin O‐glucuronides substituted at different positions. These results show that flavonoid glucuronides can be deconjugated by microsomal β‐glucuronidase from various human cells.</abstract><cop>England</cop><pmid>11513863</pmid><doi>10.1016/S0014-5793(01)02684-9</doi><tpages>4</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0014-5793 |
| ispartof | FEBS letters, 2001-08, Vol.503 (1), p.103-106 |
| issn | 0014-5793 1873-3468 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_71107630 |
| source | Wiley Online Library - AutoHoldings Journals; MEDLINE; Elsevier ScienceDirect Journals Complete; Wiley Free Content; EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
| subjects | Chromatography, High Pressure Liquid ER, endoplasmic reticulum Flavonoid Flavonoids - metabolism Glucuronidase - metabolism Glucuronide Glucuronides - metabolism Human Humans Kinetics Liver - enzymology p-NPGlcA, p-nitrophenol glucuronide Quercetin Recombinant Proteins - metabolism Substrate Specificity Turnover UDPGA, uridine-diphosphate-glucuronic acid UGT, uridine-diphosphate-glucuronosyltransferase β-Glucuronidase |
| title | Flavonoid glucuronides are substrates for human liver β‐glucuronidase |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-14T03%3A18%3A20IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Flavonoid%20glucuronides%20are%20substrates%20for%20human%20liver%20%CE%B2%E2%80%90glucuronidase&rft.jtitle=FEBS%20letters&rft.au=O'Leary,%20Karen%20A&rft.date=2001-08-10&rft.volume=503&rft.issue=1&rft.spage=103&rft.epage=106&rft.pages=103-106&rft.issn=0014-5793&rft.eissn=1873-3468&rft_id=info:doi/10.1016/S0014-5793(01)02684-9&rft_dat=%3Cproquest_cross%3E71107630%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=71107630&rft_id=info:pmid/11513863&rfr_iscdi=true |