Distribution and possible metabolic role of class III alcohol dehydrogenase in the human brain
In human brain, the sole alcohol dehydrogenase (ADH) present in significant quantity has been shown to be Class III (χ) ADH and this ADH is ineffective in generating potentially toxic and reactive acetaldehyde from ethanol at concentrations attainable in living brain tissue. We have extended this fi...
Gespeichert in:
Veröffentlicht in: | Brain research 1989-02, Vol.481 (1), p.131-141 |
---|---|
Hauptverfasser: | , , , |
Format: | Artikel |
Sprache: | eng |
Schlagworte: | |
Online-Zugang: | Volltext |
Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
container_end_page | 141 |
---|---|
container_issue | 1 |
container_start_page | 131 |
container_title | Brain research |
container_volume | 481 |
creator | Rathna Giri, P. Linnoila, M. Blanche O'Neill, J. Goldman, D. |
description | In human brain, the sole alcohol dehydrogenase (ADH) present in significant quantity has been shown to be Class III (χ) ADH and this ADH is ineffective in generating potentially toxic and reactive acetaldehyde from ethanol at concentrations attainable in living brain tissue. We have extended this finding to show that Class I ADH potentially present is undetectable even when concentrated several hundred-fold. Purified Class III ADH from human brain is identical in its pattern of tryptic peptides and in other properties to Class III ADH from human liver. Immunohistochemical staining and western immunoblots using polyclonal antibodies reveal that Class III ADH is widely distributed in brain and most concentrated in the subependymal layer and perivascular areas. Class III ADH closely resembles ω-hydroxyfatty acid dehydrogenase and a possible role for the brain enzyme is in the oxidization of long chain fatty alcohols and ω-hydroxyfatty acids. |
doi_str_mv | 10.1016/0006-8993(89)90493-9 |
format | Article |
fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_15328060</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>0006899389904939</els_id><sourcerecordid>15328060</sourcerecordid><originalsourceid>FETCH-LOGICAL-c512t-233a3243d2e3d1163ad6b0be6ae6fad5ba094c951c935e64aa137ac8f1dae0333</originalsourceid><addsrcrecordid>eNp9kEtrHDEMgE1oSbdp_0EKPpTSHqbxY8Y7vgRK-loI9JJeazS2JuvgsTf2TCH_vt7sssdeJIQ-Cekj5JKzz5xxdcUYU02vtfzY60-atVo2-oyseL8WjRIte0FWJ-QVeV3KQy2l1OycnAvVsZ7JFfnz1Zc5-2GZfYoUoqO7VIofAtIJZxhS8JbmVMs0UhugFLrZbCgEm7YpUIfbJ5fTPUYoSH2k8xbpdpkg0iGDj2_IyxFCwbfHfEF-f_92d_Ozuf31Y3Pz5baxHRdzI6QEKVrpBErHuZLg1MAGVIBqBNcNwHRrdcetlh2qFoDLNdh-5A6w_iQvyIfD3l1OjwuW2Uy-WAwBIqalGN5J0TPFKtgeQJvrnxlHs8t-gvxkODN7rWbvzOyd1WCetRpdx94d9y_DhO40dPRY---PfSgWwpghWl9O2FronglVsesDhtXFX4_ZFOsxWnQ-o52NS_7_d_wDonqUEw</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>15328060</pqid></control><display><type>article</type><title>Distribution and possible metabolic role of class III alcohol dehydrogenase in the human brain</title><source>MEDLINE</source><source>ScienceDirect Journals (5 years ago - present)</source><creator>Rathna Giri, P. ; Linnoila, M. ; Blanche O'Neill, J. ; Goldman, D.</creator><creatorcontrib>Rathna Giri, P. ; Linnoila, M. ; Blanche O'Neill, J. ; Goldman, D.</creatorcontrib><description>In human brain, the sole alcohol dehydrogenase (ADH) present in significant quantity has been shown to be Class III (χ) ADH and this ADH is ineffective in generating potentially toxic and reactive acetaldehyde from ethanol at concentrations attainable in living brain tissue. We have extended this finding to show that Class I ADH potentially present is undetectable even when concentrated several hundred-fold. Purified Class III ADH from human brain is identical in its pattern of tryptic peptides and in other properties to Class III ADH from human liver. Immunohistochemical staining and western immunoblots using polyclonal antibodies reveal that Class III ADH is widely distributed in brain and most concentrated in the subependymal layer and perivascular areas. Class III ADH closely resembles ω-hydroxyfatty acid dehydrogenase and a possible role for the brain enzyme is in the oxidization of long chain fatty alcohols and ω-hydroxyfatty acids.</description><identifier>ISSN: 0006-8993</identifier><identifier>EISSN: 1872-6240</identifier><identifier>DOI: 10.1016/0006-8993(89)90493-9</identifier><identifier>PMID: 2650803</identifier><identifier>CODEN: BRREAP</identifier><language>eng</language><publisher>London: Elsevier B.V</publisher><subject>Alcohol Oxidoreductases - analysis ; Alcohol Oxidoreductases - classification ; Alcohol Oxidoreductases - metabolism ; Alcoholism ; Amino Acids - analysis ; Biochemistry and metabolism ; Biological and medical sciences ; Brain - enzymology ; Central nervous system ; Class III alcohol dehydrogenase ; Fundamental and applied biological sciences. Psychology ; Humans ; Hydrogen-Ion Concentration ; Kinetics ; Vertebrates: nervous system and sense organs ; ω-Hydroxyfatty acid</subject><ispartof>Brain research, 1989-02, Vol.481 (1), p.131-141</ispartof><rights>1989 Elsevier Science Publishers B.V. (Biomedical Division)</rights><rights>1989 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c512t-233a3243d2e3d1163ad6b0be6ae6fad5ba094c951c935e64aa137ac8f1dae0333</citedby><cites>FETCH-LOGICAL-c512t-233a3243d2e3d1163ad6b0be6ae6fad5ba094c951c935e64aa137ac8f1dae0333</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/0006-8993(89)90493-9$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=7298026$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/2650803$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Rathna Giri, P.</creatorcontrib><creatorcontrib>Linnoila, M.</creatorcontrib><creatorcontrib>Blanche O'Neill, J.</creatorcontrib><creatorcontrib>Goldman, D.</creatorcontrib><title>Distribution and possible metabolic role of class III alcohol dehydrogenase in the human brain</title><title>Brain research</title><addtitle>Brain Res</addtitle><description>In human brain, the sole alcohol dehydrogenase (ADH) present in significant quantity has been shown to be Class III (χ) ADH and this ADH is ineffective in generating potentially toxic and reactive acetaldehyde from ethanol at concentrations attainable in living brain tissue. We have extended this finding to show that Class I ADH potentially present is undetectable even when concentrated several hundred-fold. Purified Class III ADH from human brain is identical in its pattern of tryptic peptides and in other properties to Class III ADH from human liver. Immunohistochemical staining and western immunoblots using polyclonal antibodies reveal that Class III ADH is widely distributed in brain and most concentrated in the subependymal layer and perivascular areas. Class III ADH closely resembles ω-hydroxyfatty acid dehydrogenase and a possible role for the brain enzyme is in the oxidization of long chain fatty alcohols and ω-hydroxyfatty acids.</description><subject>Alcohol Oxidoreductases - analysis</subject><subject>Alcohol Oxidoreductases - classification</subject><subject>Alcohol Oxidoreductases - metabolism</subject><subject>Alcoholism</subject><subject>Amino Acids - analysis</subject><subject>Biochemistry and metabolism</subject><subject>Biological and medical sciences</subject><subject>Brain - enzymology</subject><subject>Central nervous system</subject><subject>Class III alcohol dehydrogenase</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Humans</subject><subject>Hydrogen-Ion Concentration</subject><subject>Kinetics</subject><subject>Vertebrates: nervous system and sense organs</subject><subject>ω-Hydroxyfatty acid</subject><issn>0006-8993</issn><issn>1872-6240</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1989</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kEtrHDEMgE1oSbdp_0EKPpTSHqbxY8Y7vgRK-loI9JJeazS2JuvgsTf2TCH_vt7sssdeJIQ-Cekj5JKzz5xxdcUYU02vtfzY60-atVo2-oyseL8WjRIte0FWJ-QVeV3KQy2l1OycnAvVsZ7JFfnz1Zc5-2GZfYoUoqO7VIofAtIJZxhS8JbmVMs0UhugFLrZbCgEm7YpUIfbJ5fTPUYoSH2k8xbpdpkg0iGDj2_IyxFCwbfHfEF-f_92d_Ozuf31Y3Pz5baxHRdzI6QEKVrpBErHuZLg1MAGVIBqBNcNwHRrdcetlh2qFoDLNdh-5A6w_iQvyIfD3l1OjwuW2Uy-WAwBIqalGN5J0TPFKtgeQJvrnxlHs8t-gvxkODN7rWbvzOyd1WCetRpdx94d9y_DhO40dPRY---PfSgWwpghWl9O2FronglVsesDhtXFX4_ZFOsxWnQ-o52NS_7_d_wDonqUEw</recordid><startdate>19890227</startdate><enddate>19890227</enddate><creator>Rathna Giri, P.</creator><creator>Linnoila, M.</creator><creator>Blanche O'Neill, J.</creator><creator>Goldman, D.</creator><general>Elsevier B.V</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>7TK</scope></search><sort><creationdate>19890227</creationdate><title>Distribution and possible metabolic role of class III alcohol dehydrogenase in the human brain</title><author>Rathna Giri, P. ; Linnoila, M. ; Blanche O'Neill, J. ; Goldman, D.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c512t-233a3243d2e3d1163ad6b0be6ae6fad5ba094c951c935e64aa137ac8f1dae0333</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1989</creationdate><topic>Alcohol Oxidoreductases - analysis</topic><topic>Alcohol Oxidoreductases - classification</topic><topic>Alcohol Oxidoreductases - metabolism</topic><topic>Alcoholism</topic><topic>Amino Acids - analysis</topic><topic>Biochemistry and metabolism</topic><topic>Biological and medical sciences</topic><topic>Brain - enzymology</topic><topic>Central nervous system</topic><topic>Class III alcohol dehydrogenase</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Humans</topic><topic>Hydrogen-Ion Concentration</topic><topic>Kinetics</topic><topic>Vertebrates: nervous system and sense organs</topic><topic>ω-Hydroxyfatty acid</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Rathna Giri, P.</creatorcontrib><creatorcontrib>Linnoila, M.</creatorcontrib><creatorcontrib>Blanche O'Neill, J.</creatorcontrib><creatorcontrib>Goldman, D.</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>Neurosciences Abstracts</collection><jtitle>Brain research</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Rathna Giri, P.</au><au>Linnoila, M.</au><au>Blanche O'Neill, J.</au><au>Goldman, D.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Distribution and possible metabolic role of class III alcohol dehydrogenase in the human brain</atitle><jtitle>Brain research</jtitle><addtitle>Brain Res</addtitle><date>1989-02-27</date><risdate>1989</risdate><volume>481</volume><issue>1</issue><spage>131</spage><epage>141</epage><pages>131-141</pages><issn>0006-8993</issn><eissn>1872-6240</eissn><coden>BRREAP</coden><abstract>In human brain, the sole alcohol dehydrogenase (ADH) present in significant quantity has been shown to be Class III (χ) ADH and this ADH is ineffective in generating potentially toxic and reactive acetaldehyde from ethanol at concentrations attainable in living brain tissue. We have extended this finding to show that Class I ADH potentially present is undetectable even when concentrated several hundred-fold. Purified Class III ADH from human brain is identical in its pattern of tryptic peptides and in other properties to Class III ADH from human liver. Immunohistochemical staining and western immunoblots using polyclonal antibodies reveal that Class III ADH is widely distributed in brain and most concentrated in the subependymal layer and perivascular areas. Class III ADH closely resembles ω-hydroxyfatty acid dehydrogenase and a possible role for the brain enzyme is in the oxidization of long chain fatty alcohols and ω-hydroxyfatty acids.</abstract><cop>London</cop><cop>Amsterdam</cop><cop>New York, NY</cop><pub>Elsevier B.V</pub><pmid>2650803</pmid><doi>10.1016/0006-8993(89)90493-9</doi><tpages>11</tpages></addata></record> |
fulltext | fulltext |
identifier | ISSN: 0006-8993 |
ispartof | Brain research, 1989-02, Vol.481 (1), p.131-141 |
issn | 0006-8993 1872-6240 |
language | eng |
recordid | cdi_proquest_miscellaneous_15328060 |
source | MEDLINE; ScienceDirect Journals (5 years ago - present) |
subjects | Alcohol Oxidoreductases - analysis Alcohol Oxidoreductases - classification Alcohol Oxidoreductases - metabolism Alcoholism Amino Acids - analysis Biochemistry and metabolism Biological and medical sciences Brain - enzymology Central nervous system Class III alcohol dehydrogenase Fundamental and applied biological sciences. Psychology Humans Hydrogen-Ion Concentration Kinetics Vertebrates: nervous system and sense organs ω-Hydroxyfatty acid |
title | Distribution and possible metabolic role of class III alcohol dehydrogenase in the human brain |
url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-07T23%3A00%3A10IST&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=Distribution%20and%20possible%20metabolic%20role%20of%20class%20III%20alcohol%20dehydrogenase%20in%20the%20human%20brain&rft.jtitle=Brain%20research&rft.au=Rathna%20Giri,%20P.&rft.date=1989-02-27&rft.volume=481&rft.issue=1&rft.spage=131&rft.epage=141&rft.pages=131-141&rft.issn=0006-8993&rft.eissn=1872-6240&rft.coden=BRREAP&rft_id=info:doi/10.1016/0006-8993(89)90493-9&rft_dat=%3Cproquest_cross%3E15328060%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=15328060&rft_id=info:pmid/2650803&rft_els_id=0006899389904939&rfr_iscdi=true |