Monoamine oxidase activity and triiodothyronine biosynthesis in human cultured thyroid cells
1 The proposal that monoamine oxidase (MAO) is a source of peroxide in thyroid hormone biosynthesis has been examined by use of isolated cultured human thyroid cells which retain the ability to secrete triiodothyronine (T3) in response to thyroid stimulating hormone (TSH). 2 The results demonstrated...
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| Veröffentlicht in: | British journal of pharmacology 1989-02, Vol.96 (2), p.465-469 |
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| container_title | British journal of pharmacology |
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| creator | Kraiem, Z. Sadeh, O. Youdim, M.B.H. |
| description | 1
The proposal that monoamine oxidase (MAO) is a source of peroxide in thyroid hormone biosynthesis has been examined by use of isolated cultured human thyroid cells which retain the ability to secrete triiodothyronine (T3) in response to thyroid stimulating hormone (TSH).
2
The results demonstrated the presence of MAO A and B in human thyroid cells which oxidized 5‐hydroxytryptamine and 2‐phenylethylamine, respectively, and were selectively inhibited by the MAO inhibitors clorgyline and (−)‐deprenyl.
3
Addition of propylthiouracil to the culture system induced a 61% reduction in TSH‐stimulated T3 secretion, indicating that the bulk of such secretion apparently derives from de novo iodothyronine synthesis.
4
The MAO A and B substrate, tyramine, was ineffective in stimulating T3 secretion.
5
The selective MAO inhibitors, clorgyline and (−)‐deprenyl, alone and in combination, and in the presence and absence of tyramine, failed to inhibit basal as well as TSH‐stimulated T3 secretion in cultured human thyrocytes.
6
It is therefore apparent that even though thyroid MAO A and B enzyme reactions result in the generation of H202, this H202 does not seem to play a significant role in T3 biosynthesis. |
| doi_str_mv | 10.1111/j.1476-5381.1989.tb11839.x |
| format | Article |
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The proposal that monoamine oxidase (MAO) is a source of peroxide in thyroid hormone biosynthesis has been examined by use of isolated cultured human thyroid cells which retain the ability to secrete triiodothyronine (T3) in response to thyroid stimulating hormone (TSH).
2
The results demonstrated the presence of MAO A and B in human thyroid cells which oxidized 5‐hydroxytryptamine and 2‐phenylethylamine, respectively, and were selectively inhibited by the MAO inhibitors clorgyline and (−)‐deprenyl.
3
Addition of propylthiouracil to the culture system induced a 61% reduction in TSH‐stimulated T3 secretion, indicating that the bulk of such secretion apparently derives from de novo iodothyronine synthesis.
4
The MAO A and B substrate, tyramine, was ineffective in stimulating T3 secretion.
5
The selective MAO inhibitors, clorgyline and (−)‐deprenyl, alone and in combination, and in the presence and absence of tyramine, failed to inhibit basal as well as TSH‐stimulated T3 secretion in cultured human thyrocytes.
6
It is therefore apparent that even though thyroid MAO A and B enzyme reactions result in the generation of H202, this H202 does not seem to play a significant role in T3 biosynthesis.</description><identifier>ISSN: 0007-1188</identifier><identifier>EISSN: 1476-5381</identifier><identifier>DOI: 10.1111/j.1476-5381.1989.tb11839.x</identifier><identifier>PMID: 2924086</identifier><identifier>CODEN: BJPCBM</identifier><language>eng</language><publisher>Oxford, UK: Blackwell Publishing Ltd</publisher><subject>Biological and medical sciences ; Cells, Cultured ; Fundamental and applied biological sciences. Psychology ; Hormones. Regulation ; Humans ; Monoamine Oxidase - metabolism ; Monoamine Oxidase Inhibitors - pharmacology ; thyroid ; Thyroid Gland - drug effects ; Thyroid Gland - enzymology ; Thyroid Gland - metabolism ; Thyroid. Parathyroid. Ultimobranchial body ; triiodothyronine ; Triiodothyronine - biosynthesis ; Vertebrates: endocrinology</subject><ispartof>British journal of pharmacology, 1989-02, Vol.96 (2), p.465-469</ispartof><rights>1989 British Pharmacological Society</rights><rights>1989 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5389-cb2ad71d0053af57d26551bcd6bd96eb1134fc86899e154cffae7c911f1d54fa3</citedby><cites>FETCH-LOGICAL-c5389-cb2ad71d0053af57d26551bcd6bd96eb1134fc86899e154cffae7c911f1d54fa3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC1854370/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC1854370/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,723,776,780,881,27903,27904,53770,53772</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=7299673$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/2924086$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kraiem, Z.</creatorcontrib><creatorcontrib>Sadeh, O.</creatorcontrib><creatorcontrib>Youdim, M.B.H.</creatorcontrib><title>Monoamine oxidase activity and triiodothyronine biosynthesis in human cultured thyroid cells</title><title>British journal of pharmacology</title><addtitle>Br J Pharmacol</addtitle><description>1
The proposal that monoamine oxidase (MAO) is a source of peroxide in thyroid hormone biosynthesis has been examined by use of isolated cultured human thyroid cells which retain the ability to secrete triiodothyronine (T3) in response to thyroid stimulating hormone (TSH).
2
The results demonstrated the presence of MAO A and B in human thyroid cells which oxidized 5‐hydroxytryptamine and 2‐phenylethylamine, respectively, and were selectively inhibited by the MAO inhibitors clorgyline and (−)‐deprenyl.
3
Addition of propylthiouracil to the culture system induced a 61% reduction in TSH‐stimulated T3 secretion, indicating that the bulk of such secretion apparently derives from de novo iodothyronine synthesis.
4
The MAO A and B substrate, tyramine, was ineffective in stimulating T3 secretion.
5
The selective MAO inhibitors, clorgyline and (−)‐deprenyl, alone and in combination, and in the presence and absence of tyramine, failed to inhibit basal as well as TSH‐stimulated T3 secretion in cultured human thyrocytes.
6
It is therefore apparent that even though thyroid MAO A and B enzyme reactions result in the generation of H202, this H202 does not seem to play a significant role in T3 biosynthesis.</description><subject>Biological and medical sciences</subject><subject>Cells, Cultured</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Hormones. Regulation</subject><subject>Humans</subject><subject>Monoamine Oxidase - metabolism</subject><subject>Monoamine Oxidase Inhibitors - pharmacology</subject><subject>thyroid</subject><subject>Thyroid Gland - drug effects</subject><subject>Thyroid Gland - enzymology</subject><subject>Thyroid Gland - metabolism</subject><subject>Thyroid. Parathyroid. Ultimobranchial body</subject><subject>triiodothyronine</subject><subject>Triiodothyronine - biosynthesis</subject><subject>Vertebrates: endocrinology</subject><issn>0007-1188</issn><issn>1476-5381</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1989</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqVkdFr1TAYxYMo8276JwhFZG_tkqZpEh_EOeYmTPRB34SQJqk3lzaZSTpv_3tTb7nok5iXL3B-3-F8HABeIlih_C52FWpoWxLMUIU441XqEGKYV_tHYHOUHoMNhJCWWWJPwWmMOwizSMkJOKl53UDWbsC3j955OVpnCr-3WkZTSJXsg01zIZ0uUrDWa5-2c_BuoTrr4-zS1kQbC-uK7TRKV6hpSFMwmV9AqwtlhiE-A096OUTzfJ1n4Ov76y9Xt-Xdp5sPV5d3pco5eam6WmqKNIQEy55QXbeEoE7pttO8Nfk23PSKtYxzg0ij-l4aqjhCPdKk6SU-A28OvvdTNxqtjEtBDuI-2FGGWXhpxd-Ks1vx3T8IxEiDKcwG56tB8D8mE5MYbVxOkM74KQrKGMMENv8EEcF105DF8fUBVMHHGEx_TIOgWEoUO7E0JZamxFKiWEsU-7z84s97jqtra1l_teoyKjn0QTpl4xGjNectxRl7e8B-2sHM_xFAvPt8-_uLfwFue72_</recordid><startdate>198902</startdate><enddate>198902</enddate><creator>Kraiem, Z.</creator><creator>Sadeh, O.</creator><creator>Youdim, M.B.H.</creator><general>Blackwell Publishing Ltd</general><general>Nature Publishing</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>8FD</scope><scope>FR3</scope><scope>M7Z</scope><scope>P64</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>198902</creationdate><title>Monoamine oxidase activity and triiodothyronine biosynthesis in human cultured thyroid cells</title><author>Kraiem, Z. ; Sadeh, O. ; Youdim, M.B.H.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5389-cb2ad71d0053af57d26551bcd6bd96eb1134fc86899e154cffae7c911f1d54fa3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1989</creationdate><topic>Biological and medical sciences</topic><topic>Cells, Cultured</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Hormones. Regulation</topic><topic>Humans</topic><topic>Monoamine Oxidase - metabolism</topic><topic>Monoamine Oxidase Inhibitors - pharmacology</topic><topic>thyroid</topic><topic>Thyroid Gland - drug effects</topic><topic>Thyroid Gland - enzymology</topic><topic>Thyroid Gland - metabolism</topic><topic>Thyroid. Parathyroid. Ultimobranchial body</topic><topic>triiodothyronine</topic><topic>Triiodothyronine - biosynthesis</topic><topic>Vertebrates: endocrinology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kraiem, Z.</creatorcontrib><creatorcontrib>Sadeh, O.</creatorcontrib><creatorcontrib>Youdim, M.B.H.</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>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biochemistry Abstracts 1</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>British journal of pharmacology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kraiem, Z.</au><au>Sadeh, O.</au><au>Youdim, M.B.H.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Monoamine oxidase activity and triiodothyronine biosynthesis in human cultured thyroid cells</atitle><jtitle>British journal of pharmacology</jtitle><addtitle>Br J Pharmacol</addtitle><date>1989-02</date><risdate>1989</risdate><volume>96</volume><issue>2</issue><spage>465</spage><epage>469</epage><pages>465-469</pages><issn>0007-1188</issn><eissn>1476-5381</eissn><coden>BJPCBM</coden><abstract>1
The proposal that monoamine oxidase (MAO) is a source of peroxide in thyroid hormone biosynthesis has been examined by use of isolated cultured human thyroid cells which retain the ability to secrete triiodothyronine (T3) in response to thyroid stimulating hormone (TSH).
2
The results demonstrated the presence of MAO A and B in human thyroid cells which oxidized 5‐hydroxytryptamine and 2‐phenylethylamine, respectively, and were selectively inhibited by the MAO inhibitors clorgyline and (−)‐deprenyl.
3
Addition of propylthiouracil to the culture system induced a 61% reduction in TSH‐stimulated T3 secretion, indicating that the bulk of such secretion apparently derives from de novo iodothyronine synthesis.
4
The MAO A and B substrate, tyramine, was ineffective in stimulating T3 secretion.
5
The selective MAO inhibitors, clorgyline and (−)‐deprenyl, alone and in combination, and in the presence and absence of tyramine, failed to inhibit basal as well as TSH‐stimulated T3 secretion in cultured human thyrocytes.
6
It is therefore apparent that even though thyroid MAO A and B enzyme reactions result in the generation of H202, this H202 does not seem to play a significant role in T3 biosynthesis.</abstract><cop>Oxford, UK</cop><pub>Blackwell Publishing Ltd</pub><pmid>2924086</pmid><doi>10.1111/j.1476-5381.1989.tb11839.x</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; PubMed Central; Alma/SFX Local Collection |
| subjects | Biological and medical sciences Cells, Cultured Fundamental and applied biological sciences. Psychology Hormones. Regulation Humans Monoamine Oxidase - metabolism Monoamine Oxidase Inhibitors - pharmacology thyroid Thyroid Gland - drug effects Thyroid Gland - enzymology Thyroid Gland - metabolism Thyroid. Parathyroid. Ultimobranchial body triiodothyronine Triiodothyronine - biosynthesis Vertebrates: endocrinology |
| title | Monoamine oxidase activity and triiodothyronine biosynthesis in human cultured thyroid cells |
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