Comparison of 3α-hydroxysteroid dehydrogenase activities in the microsomal fractions of hyperplastic, malignant and normal human prostatic tissues

The conversion of dihydrotestosterone (DHT) to 3α-androstanediol (3α-adiol) was studied using the microsomal fractions of 15 hyperplastic, 5 malignant and 6 normal human prostatic tissues. Standard assay conditions were: 0.2 μ M DHT, 1.0 mM NADPH, 1.0 mM NADH, 2.0 mM EDTA and the microsomal fraction...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Veröffentlicht in:Journal of steroid biochemistry 1984-04, Vol.20 (4), p.829-833
1. Verfasser: Hudson, Robert W.
Format: Artikel
Sprache:eng
Schlagworte:
Online-Zugang:Volltext
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
container_end_page 833
container_issue 4
container_start_page 829
container_title Journal of steroid biochemistry
container_volume 20
creator Hudson, Robert W.
description The conversion of dihydrotestosterone (DHT) to 3α-androstanediol (3α-adiol) was studied using the microsomal fractions of 15 hyperplastic, 5 malignant and 6 normal human prostatic tissues. Standard assay conditions were: 0.2 μ M DHT, 1.0 mM NADPH, 1.0 mM NADH, 2.0 mM EDTA and the microsomal fractions equivalent to 200 mg of prostatic tissue, in 0.1 M MES buffer, pH 6.5. Under the conditions of this assay, the back-conversion of 3α-adiol to DHT or the conversion of DHT to androstanediol were negligible. Optimum enzyme activity was achieved under standard assay conditions. In the absence of EDTA: enzyme activity was 65% of the standard assay; activity was diminished further by 2mM Ca 2+ and virtually eliminated by 2 mM Mg 2+ or 2 μM Zn 2+. Activity in the absence of either NADPH or NADH was only 50% of the activities seen in the presence of both cofactors. The pH optimum of the enzyme was between 6.0 and 6.5. The apparent K m values of the enzymes in hyperplastic, malignant and normal tissues were 0.03, 0.02 and 0.03μM, respectively. The V max values for these tissues were 6.0 ± 2.1, 1.6 ± 0.5 and 14.0 ± 3.0 pmol/mg protein/20 min incubation, respectively. The results of these experiments offer further explanation for the differences in DHT and 3α-adiol levels seen in the 3 prostatic tissues.
doi_str_mv 10.1016/0022-4731(84)90391-1
format Article
fullrecord <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_81002673</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>0022473184903911</els_id><sourcerecordid>81002673</sourcerecordid><originalsourceid>FETCH-LOGICAL-c386t-d3ff0c9cfe899fc6ed5640a4b1913bee88570fb1abee17ec31feb9bfc3eed1b43</originalsourceid><addsrcrecordid>eNp9kM-OFCEQhzlo1nX1DTThYIwmtkLDdDeXTczEf8kmXvRMaCh2MN3QUszGeQ6fxBfxmaR3JnP0BKnfV0XxEfKMs7ec8e4dY23byF7wV4N8rZhQvOEPyOW5_Ig8RvzBGFeDbC_IRdcy1rPNJfm9TfNicsAUafJU_P3T7A4up18HLJBTcNTBfeEWokGgxpZwF0oApCHSsgM6B5sTptlM1Oc1ThHXUbvDAnmZDJZg39Aah9toYqEmOhpTXvndfjaRLrW9mErREhD3gE_IQ28mhKen84p8__jh2_Zzc_P105ft-5vGiqErjRPeM6ush0Epbztwm04yI0euuBgBhmHTMz9yU--8Byu4h1GN3goAx0cprsjL49y6wc_6btFzQAvTZCKkPeqBV39dLyooj-D6U8zg9ZLDbPJBc6ZX_3oVrVfRepD63r_mte35af5-nMGdm07ya_7ilBu0Zqr2og14xlTPlFRtxa6PGFQXdwGyRhsgWnAhgy3apfD_Pf4BZp6p2A</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>81002673</pqid></control><display><type>article</type><title>Comparison of 3α-hydroxysteroid dehydrogenase activities in the microsomal fractions of hyperplastic, malignant and normal human prostatic tissues</title><source>MEDLINE</source><source>Alma/SFX Local Collection</source><creator>Hudson, Robert W.</creator><creatorcontrib>Hudson, Robert W.</creatorcontrib><description>The conversion of dihydrotestosterone (DHT) to 3α-androstanediol (3α-adiol) was studied using the microsomal fractions of 15 hyperplastic, 5 malignant and 6 normal human prostatic tissues. Standard assay conditions were: 0.2 μ M DHT, 1.0 mM NADPH, 1.0 mM NADH, 2.0 mM EDTA and the microsomal fractions equivalent to 200 mg of prostatic tissue, in 0.1 M MES buffer, pH 6.5. Under the conditions of this assay, the back-conversion of 3α-adiol to DHT or the conversion of DHT to androstanediol were negligible. Optimum enzyme activity was achieved under standard assay conditions. In the absence of EDTA: enzyme activity was 65% of the standard assay; activity was diminished further by 2mM Ca 2+ and virtually eliminated by 2 mM Mg 2+ or 2 μM Zn 2+. Activity in the absence of either NADPH or NADH was only 50% of the activities seen in the presence of both cofactors. The pH optimum of the enzyme was between 6.0 and 6.5. The apparent K m values of the enzymes in hyperplastic, malignant and normal tissues were 0.03, 0.02 and 0.03μM, respectively. The V max values for these tissues were 6.0 ± 2.1, 1.6 ± 0.5 and 14.0 ± 3.0 pmol/mg protein/20 min incubation, respectively. The results of these experiments offer further explanation for the differences in DHT and 3α-adiol levels seen in the 3 prostatic tissues.</description><identifier>ISSN: 0022-4731</identifier><identifier>DOI: 10.1016/0022-4731(84)90391-1</identifier><identifier>PMID: 6200705</identifier><identifier>CODEN: JSTBBK</identifier><language>eng</language><publisher>Oxford: Elsevier B.V</publisher><subject>3-alpha-Hydroxysteroid Dehydrogenase (B-Specific) ; 3-Hydroxysteroid Dehydrogenases - metabolism ; Biological and medical sciences ; Cations, Divalent ; Edetic Acid - pharmacology ; Humans ; Kinetics ; Male ; Medical sciences ; Microsomes - enzymology ; Nephrology. Urinary tract diseases ; Prostate - enzymology ; Prostatic Hyperplasia - enzymology ; Prostatic Neoplasms - enzymology ; Reference Values ; Tumors of the urinary system ; Urinary tract. Prostate gland</subject><ispartof>Journal of steroid biochemistry, 1984-04, Vol.20 (4), p.829-833</ispartof><rights>1984</rights><rights>1984 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c386t-d3ff0c9cfe899fc6ed5640a4b1913bee88570fb1abee17ec31feb9bfc3eed1b43</citedby><cites>FETCH-LOGICAL-c386t-d3ff0c9cfe899fc6ed5640a4b1913bee88570fb1abee17ec31feb9bfc3eed1b43</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&amp;idt=9709492$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/6200705$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Hudson, Robert W.</creatorcontrib><title>Comparison of 3α-hydroxysteroid dehydrogenase activities in the microsomal fractions of hyperplastic, malignant and normal human prostatic tissues</title><title>Journal of steroid biochemistry</title><addtitle>J Steroid Biochem</addtitle><description>The conversion of dihydrotestosterone (DHT) to 3α-androstanediol (3α-adiol) was studied using the microsomal fractions of 15 hyperplastic, 5 malignant and 6 normal human prostatic tissues. Standard assay conditions were: 0.2 μ M DHT, 1.0 mM NADPH, 1.0 mM NADH, 2.0 mM EDTA and the microsomal fractions equivalent to 200 mg of prostatic tissue, in 0.1 M MES buffer, pH 6.5. Under the conditions of this assay, the back-conversion of 3α-adiol to DHT or the conversion of DHT to androstanediol were negligible. Optimum enzyme activity was achieved under standard assay conditions. In the absence of EDTA: enzyme activity was 65% of the standard assay; activity was diminished further by 2mM Ca 2+ and virtually eliminated by 2 mM Mg 2+ or 2 μM Zn 2+. Activity in the absence of either NADPH or NADH was only 50% of the activities seen in the presence of both cofactors. The pH optimum of the enzyme was between 6.0 and 6.5. The apparent K m values of the enzymes in hyperplastic, malignant and normal tissues were 0.03, 0.02 and 0.03μM, respectively. The V max values for these tissues were 6.0 ± 2.1, 1.6 ± 0.5 and 14.0 ± 3.0 pmol/mg protein/20 min incubation, respectively. The results of these experiments offer further explanation for the differences in DHT and 3α-adiol levels seen in the 3 prostatic tissues.</description><subject>3-alpha-Hydroxysteroid Dehydrogenase (B-Specific)</subject><subject>3-Hydroxysteroid Dehydrogenases - metabolism</subject><subject>Biological and medical sciences</subject><subject>Cations, Divalent</subject><subject>Edetic Acid - pharmacology</subject><subject>Humans</subject><subject>Kinetics</subject><subject>Male</subject><subject>Medical sciences</subject><subject>Microsomes - enzymology</subject><subject>Nephrology. Urinary tract diseases</subject><subject>Prostate - enzymology</subject><subject>Prostatic Hyperplasia - enzymology</subject><subject>Prostatic Neoplasms - enzymology</subject><subject>Reference Values</subject><subject>Tumors of the urinary system</subject><subject>Urinary tract. Prostate gland</subject><issn>0022-4731</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1984</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kM-OFCEQhzlo1nX1DTThYIwmtkLDdDeXTczEf8kmXvRMaCh2MN3QUszGeQ6fxBfxmaR3JnP0BKnfV0XxEfKMs7ec8e4dY23byF7wV4N8rZhQvOEPyOW5_Ig8RvzBGFeDbC_IRdcy1rPNJfm9TfNicsAUafJU_P3T7A4up18HLJBTcNTBfeEWokGgxpZwF0oApCHSsgM6B5sTptlM1Oc1ThHXUbvDAnmZDJZg39Aah9toYqEmOhpTXvndfjaRLrW9mErREhD3gE_IQ28mhKen84p8__jh2_Zzc_P105ft-5vGiqErjRPeM6ush0Epbztwm04yI0euuBgBhmHTMz9yU--8Byu4h1GN3goAx0cprsjL49y6wc_6btFzQAvTZCKkPeqBV39dLyooj-D6U8zg9ZLDbPJBc6ZX_3oVrVfRepD63r_mte35af5-nMGdm07ya_7ilBu0Zqr2og14xlTPlFRtxa6PGFQXdwGyRhsgWnAhgy3apfD_Pf4BZp6p2A</recordid><startdate>198404</startdate><enddate>198404</enddate><creator>Hudson, Robert W.</creator><general>Elsevier B.V</general><general>Pergamon</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>7X8</scope></search><sort><creationdate>198404</creationdate><title>Comparison of 3α-hydroxysteroid dehydrogenase activities in the microsomal fractions of hyperplastic, malignant and normal human prostatic tissues</title><author>Hudson, Robert W.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c386t-d3ff0c9cfe899fc6ed5640a4b1913bee88570fb1abee17ec31feb9bfc3eed1b43</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1984</creationdate><topic>3-alpha-Hydroxysteroid Dehydrogenase (B-Specific)</topic><topic>3-Hydroxysteroid Dehydrogenases - metabolism</topic><topic>Biological and medical sciences</topic><topic>Cations, Divalent</topic><topic>Edetic Acid - pharmacology</topic><topic>Humans</topic><topic>Kinetics</topic><topic>Male</topic><topic>Medical sciences</topic><topic>Microsomes - enzymology</topic><topic>Nephrology. Urinary tract diseases</topic><topic>Prostate - enzymology</topic><topic>Prostatic Hyperplasia - enzymology</topic><topic>Prostatic Neoplasms - enzymology</topic><topic>Reference Values</topic><topic>Tumors of the urinary system</topic><topic>Urinary tract. Prostate gland</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Hudson, Robert 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>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of steroid biochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Hudson, Robert W.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Comparison of 3α-hydroxysteroid dehydrogenase activities in the microsomal fractions of hyperplastic, malignant and normal human prostatic tissues</atitle><jtitle>Journal of steroid biochemistry</jtitle><addtitle>J Steroid Biochem</addtitle><date>1984-04</date><risdate>1984</risdate><volume>20</volume><issue>4</issue><spage>829</spage><epage>833</epage><pages>829-833</pages><issn>0022-4731</issn><coden>JSTBBK</coden><abstract>The conversion of dihydrotestosterone (DHT) to 3α-androstanediol (3α-adiol) was studied using the microsomal fractions of 15 hyperplastic, 5 malignant and 6 normal human prostatic tissues. Standard assay conditions were: 0.2 μ M DHT, 1.0 mM NADPH, 1.0 mM NADH, 2.0 mM EDTA and the microsomal fractions equivalent to 200 mg of prostatic tissue, in 0.1 M MES buffer, pH 6.5. Under the conditions of this assay, the back-conversion of 3α-adiol to DHT or the conversion of DHT to androstanediol were negligible. Optimum enzyme activity was achieved under standard assay conditions. In the absence of EDTA: enzyme activity was 65% of the standard assay; activity was diminished further by 2mM Ca 2+ and virtually eliminated by 2 mM Mg 2+ or 2 μM Zn 2+. Activity in the absence of either NADPH or NADH was only 50% of the activities seen in the presence of both cofactors. The pH optimum of the enzyme was between 6.0 and 6.5. The apparent K m values of the enzymes in hyperplastic, malignant and normal tissues were 0.03, 0.02 and 0.03μM, respectively. The V max values for these tissues were 6.0 ± 2.1, 1.6 ± 0.5 and 14.0 ± 3.0 pmol/mg protein/20 min incubation, respectively. The results of these experiments offer further explanation for the differences in DHT and 3α-adiol levels seen in the 3 prostatic tissues.</abstract><cop>Oxford</cop><cop>New York, NY</cop><pub>Elsevier B.V</pub><pmid>6200705</pmid><doi>10.1016/0022-4731(84)90391-1</doi><tpages>5</tpages></addata></record>
fulltext fulltext
identifier ISSN: 0022-4731
ispartof Journal of steroid biochemistry, 1984-04, Vol.20 (4), p.829-833
issn 0022-4731
language eng
recordid cdi_proquest_miscellaneous_81002673
source MEDLINE; Alma/SFX Local Collection
subjects 3-alpha-Hydroxysteroid Dehydrogenase (B-Specific)
3-Hydroxysteroid Dehydrogenases - metabolism
Biological and medical sciences
Cations, Divalent
Edetic Acid - pharmacology
Humans
Kinetics
Male
Medical sciences
Microsomes - enzymology
Nephrology. Urinary tract diseases
Prostate - enzymology
Prostatic Hyperplasia - enzymology
Prostatic Neoplasms - enzymology
Reference Values
Tumors of the urinary system
Urinary tract. Prostate gland
title Comparison of 3α-hydroxysteroid dehydrogenase activities in the microsomal fractions of hyperplastic, malignant and normal human prostatic tissues
url https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-24T20%3A09%3A40IST&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=Comparison%20of%203%CE%B1-hydroxysteroid%20dehydrogenase%20activities%20in%20the%20microsomal%20fractions%20of%20hyperplastic,%20malignant%20and%20normal%20human%20prostatic%20tissues&rft.jtitle=Journal%20of%20steroid%20biochemistry&rft.au=Hudson,%20Robert%20W.&rft.date=1984-04&rft.volume=20&rft.issue=4&rft.spage=829&rft.epage=833&rft.pages=829-833&rft.issn=0022-4731&rft.coden=JSTBBK&rft_id=info:doi/10.1016/0022-4731(84)90391-1&rft_dat=%3Cproquest_cross%3E81002673%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=81002673&rft_id=info:pmid/6200705&rft_els_id=0022473184903911&rfr_iscdi=true