Inhibitory Effects of Condensed Tannins on Angiotensin Converting Enzyme
Effects of condensed tannins isolated from Rhei Rhizoma on the activities of angiotensin converting enzyme (ACE) and various proteases were examined in vitro. Among the various condensed tannins tested, procyanidin B-5 3,3’-di-O-gallate and procyanidin C-1 3,3’,3”-tri-O-gallate strongly inhibited th...
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| Veröffentlicht in: | Japanese Journal of Pharmacology 1987, Vol.43 (2), p.242-246 |
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| container_title | Japanese Journal of Pharmacology |
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| creator | UCHIDA, Shinji IKARI, Nobuhiko OHTA, Hisashi NIWA, Masami NONAKA, Gen-ichiro NISHIOKA, Itsuo OZAKI, Masayori |
| description | Effects of condensed tannins isolated from Rhei Rhizoma on the activities of angiotensin converting enzyme (ACE) and various proteases were examined in vitro. Among the various condensed tannins tested, procyanidin B-5 3,3’-di-O-gallate and procyanidin C-1 3,3’,3”-tri-O-gallate strongly inhibited the activity of ACE. The concentration of procyanidin B-5 3,3’-di-O-gallate required for 50% inhibition of ACE was 1.3×10-6 M. The inhibition of ACE by condensed tannins was reversible and non-competitive, according to dialysis and to Dixon plots. However, over one hundred times the concentration was required to inhibit activities of other proteases such as trypsin, chymotrypsin, leucine aminopeptidase, carboxypeptidase A and urinary kallikrein. These results suggest that the inhibitory effects of condensed tannins on the activities of ACE are specific. |
| doi_str_mv | 10.1016/S0021-5198(19)43547-6 |
| format | Article |
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Among the various condensed tannins tested, procyanidin B-5 3,3’-di-O-gallate and procyanidin C-1 3,3’,3”-tri-O-gallate strongly inhibited the activity of ACE. The concentration of procyanidin B-5 3,3’-di-O-gallate required for 50% inhibition of ACE was 1.3×10-6 M. The inhibition of ACE by condensed tannins was reversible and non-competitive, according to dialysis and to Dixon plots. However, over one hundred times the concentration was required to inhibit activities of other proteases such as trypsin, chymotrypsin, leucine aminopeptidase, carboxypeptidase A and urinary kallikrein. These results suggest that the inhibitory effects of condensed tannins on the activities of ACE are specific.</description><identifier>ISSN: 0021-5198</identifier><identifier>EISSN: 1347-3506</identifier><identifier>DOI: 10.1016/S0021-5198(19)43547-6</identifier><identifier>PMID: 3033368</identifier><identifier>CODEN: JJPAAZ</identifier><language>eng</language><publisher>Kyoto: The Japanese Pharmacological Society</publisher><subject>Angiotensin-Converting Enzyme Inhibitors ; Animals ; Biflavonoids ; Biological and medical sciences ; Catechin ; Cattle ; Dialysis ; Kinetics ; Medical sciences ; Miscellaneous ; Pharmacology. Drug treatments ; Proanthocyanidins ; Swine ; Tannins - pharmacology</subject><ispartof>Japanese Journal of Pharmacology, 1987, Vol.43 (2), p.242-246</ispartof><rights>1987 Elsevier B.V.</rights><rights>1987 INIST-CNRS</rights><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c3906-333a8f2a7112565d2c909a7eb9a54de93d06cf96e3deea897fd026a29a1901a23</citedby><cites>FETCH-LOGICAL-c3906-333a8f2a7112565d2c909a7eb9a54de93d06cf96e3deea897fd026a29a1901a23</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,4024,27923,27924,27925</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=8345637$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/3033368$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>UCHIDA, Shinji</creatorcontrib><creatorcontrib>IKARI, Nobuhiko</creatorcontrib><creatorcontrib>OHTA, Hisashi</creatorcontrib><creatorcontrib>NIWA, Masami</creatorcontrib><creatorcontrib>NONAKA, Gen-ichiro</creatorcontrib><creatorcontrib>NISHIOKA, Itsuo</creatorcontrib><creatorcontrib>OZAKI, Masayori</creatorcontrib><creatorcontrib>School of Medicine</creatorcontrib><creatorcontrib>Department of Pharmacology</creatorcontrib><creatorcontrib>Faculty of Pharmaceutical Sciences</creatorcontrib><creatorcontrib>Kyushu University</creatorcontrib><creatorcontrib>Nagasaki University</creatorcontrib><title>Inhibitory Effects of Condensed Tannins on Angiotensin Converting Enzyme</title><title>Japanese Journal of Pharmacology</title><addtitle>Jpn J Pharmacol</addtitle><description>Effects of condensed tannins isolated from Rhei Rhizoma on the activities of angiotensin converting enzyme (ACE) and various proteases were examined in vitro. Among the various condensed tannins tested, procyanidin B-5 3,3’-di-O-gallate and procyanidin C-1 3,3’,3”-tri-O-gallate strongly inhibited the activity of ACE. The concentration of procyanidin B-5 3,3’-di-O-gallate required for 50% inhibition of ACE was 1.3×10-6 M. The inhibition of ACE by condensed tannins was reversible and non-competitive, according to dialysis and to Dixon plots. However, over one hundred times the concentration was required to inhibit activities of other proteases such as trypsin, chymotrypsin, leucine aminopeptidase, carboxypeptidase A and urinary kallikrein. These results suggest that the inhibitory effects of condensed tannins on the activities of ACE are specific.</description><subject>Angiotensin-Converting Enzyme Inhibitors</subject><subject>Animals</subject><subject>Biflavonoids</subject><subject>Biological and medical sciences</subject><subject>Catechin</subject><subject>Cattle</subject><subject>Dialysis</subject><subject>Kinetics</subject><subject>Medical sciences</subject><subject>Miscellaneous</subject><subject>Pharmacology. Drug treatments</subject><subject>Proanthocyanidins</subject><subject>Swine</subject><subject>Tannins - pharmacology</subject><issn>0021-5198</issn><issn>1347-3506</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1987</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkUtvEzEUhS0EKqHwEyrNAiFYDFw_Z7xCVZTSSpVYUNaW47kujiZ2sCeV0l-Pp4myZePH9XfPsY8JuaLwlQJV334BMNpKqvvPVH8RXIquVa_IgvK64BLUa7I4I2_Ju1I2ddsDFRfkggPnXPULcnsX_4R1mFI-NCvv0U2lSb5ZpjhgLDg0DzbGEGsxNtfxMaSplkOcgSfMU4iPzSo-H7b4nrzxdiz44TRfkt83q4flbXv_88fd8vq-dVyDaqut7T2zHaVMKjkwp0HbDtfaSjGg5gMo57VCPiDaXnd-AKYs05ZqoJbxS_LpqLvL6e8ey2S2oTgcRxsx7YvpOgnAGVRQHkGXUykZvdnlsLX5YCiYOUHzkqCZ4zFUm5cEjap9VyeD_XqLw7nrFFk9_3g6t8XZ0WcbXShnrOdCKt5V7OaIVY1QuRTHENFs0j7Hmo9xXm02aTdW674zAIIDM1DvAUyweVCd6AWb_b4fhbCm-hQwm-ICRldlc_0uM6Twnxf9A5u-olM</recordid><startdate>1987</startdate><enddate>1987</enddate><creator>UCHIDA, Shinji</creator><creator>IKARI, Nobuhiko</creator><creator>OHTA, Hisashi</creator><creator>NIWA, Masami</creator><creator>NONAKA, Gen-ichiro</creator><creator>NISHIOKA, Itsuo</creator><creator>OZAKI, Masayori</creator><general>The Japanese Pharmacological Society</general><general>Japanese Pharmacological Society</general><scope>6I.</scope><scope>AAFTH</scope><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>7X8</scope></search><sort><creationdate>1987</creationdate><title>Inhibitory Effects of Condensed Tannins on Angiotensin Converting Enzyme</title><author>UCHIDA, Shinji ; IKARI, Nobuhiko ; OHTA, Hisashi ; NIWA, Masami ; NONAKA, Gen-ichiro ; NISHIOKA, Itsuo ; OZAKI, Masayori</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3906-333a8f2a7112565d2c909a7eb9a54de93d06cf96e3deea897fd026a29a1901a23</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1987</creationdate><topic>Angiotensin-Converting Enzyme Inhibitors</topic><topic>Animals</topic><topic>Biflavonoids</topic><topic>Biological and medical sciences</topic><topic>Catechin</topic><topic>Cattle</topic><topic>Dialysis</topic><topic>Kinetics</topic><topic>Medical sciences</topic><topic>Miscellaneous</topic><topic>Pharmacology. 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Among the various condensed tannins tested, procyanidin B-5 3,3’-di-O-gallate and procyanidin C-1 3,3’,3”-tri-O-gallate strongly inhibited the activity of ACE. The concentration of procyanidin B-5 3,3’-di-O-gallate required for 50% inhibition of ACE was 1.3×10-6 M. The inhibition of ACE by condensed tannins was reversible and non-competitive, according to dialysis and to Dixon plots. However, over one hundred times the concentration was required to inhibit activities of other proteases such as trypsin, chymotrypsin, leucine aminopeptidase, carboxypeptidase A and urinary kallikrein. These results suggest that the inhibitory effects of condensed tannins on the activities of ACE are specific.</abstract><cop>Kyoto</cop><pub>The Japanese Pharmacological Society</pub><pmid>3033368</pmid><doi>10.1016/S0021-5198(19)43547-6</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Japanese Journal of Pharmacology, 1987, Vol.43 (2), p.242-246 |
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| source | MEDLINE; J-STAGE日本語サイト (Free Access); Free Full-Text Journals in Chemistry; EZB* |
| subjects | Angiotensin-Converting Enzyme Inhibitors Animals Biflavonoids Biological and medical sciences Catechin Cattle Dialysis Kinetics Medical sciences Miscellaneous Pharmacology. Drug treatments Proanthocyanidins Swine Tannins - pharmacology |
| title | Inhibitory Effects of Condensed Tannins on Angiotensin Converting Enzyme |
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