{"title":"雌激素和羟基类固醇硫转移酶在人乳腺癌中的特性","authors":"J.B. Adams, N.S. Phillips","doi":"10.1016/0022-4731(90)90190-4","DOIUrl":null,"url":null,"abstract":"<div><p>Partial purification (~ χ 140-fold) of estrogen sulphotransferase (EC 2.8.2.4) in human mammary estrogen receptor positive cancer tissue was achieved by affinity chromatography on adenosine-3',5'-diphosphate-agarose. It had a <em>M</em><sub><em>r</em></sub>, of approximately 70,000 by gel filtration and upon electrophoresis on concave gradient polyacrylamide gels, showed a major (<em>M</em><sub><em>r</em></sub> 70,000) and a minor (<em>M</em><sub><em>r</em></sub> 200,000) peak of activity. Kinetics of this preparation (estradiol-17β and estrone as substrates), and also that of hydroxysteroid sulphotransferase (EC 2.8.2.2) contained in the cytosol of human mammary cancer MCF-7 cells (5-androstene-3β,17β-diol and dehydroepiandrosterone as substrates), were compared. The enzymes showed very similar behaviour, characterized by high affinity for their steroid substrates (low nM range) and co-operativity in their binding. For hydroxysteroid sulphotransferase, the adrenal-derived estrogen 5-androstene-3β,17β-diol was the preferred substrate compared to dehydro-epiandrosterone in the 0–40 nM concentration range. Such properties of the enzymes might be designed to limit the exposure of nuclear receptor to free ligand. Alternatively, a defined subcellular location would perhaps involve the enzymes in the elimination of estrogen after processing of the ligand-bound receptor.</p></div>","PeriodicalId":17138,"journal":{"name":"Journal of steroid biochemistry","volume":null,"pages":null},"PeriodicalIF":0.0000,"publicationDate":"1990-08-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0022-4731(90)90190-4","citationCount":"20","resultStr":"{\"title\":\"Properties of estrogen and hydroxysteroid sulphotransferases in human mammary cancer\",\"authors\":\"J.B. Adams, N.S. Phillips\",\"doi\":\"10.1016/0022-4731(90)90190-4\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p>Partial purification (~ χ 140-fold) of estrogen sulphotransferase (EC 2.8.2.4) in human mammary estrogen receptor positive cancer tissue was achieved by affinity chromatography on adenosine-3',5'-diphosphate-agarose. It had a <em>M</em><sub><em>r</em></sub>, of approximately 70,000 by gel filtration and upon electrophoresis on concave gradient polyacrylamide gels, showed a major (<em>M</em><sub><em>r</em></sub> 70,000) and a minor (<em>M</em><sub><em>r</em></sub> 200,000) peak of activity. Kinetics of this preparation (estradiol-17β and estrone as substrates), and also that of hydroxysteroid sulphotransferase (EC 2.8.2.2) contained in the cytosol of human mammary cancer MCF-7 cells (5-androstene-3β,17β-diol and dehydroepiandrosterone as substrates), were compared. The enzymes showed very similar behaviour, characterized by high affinity for their steroid substrates (low nM range) and co-operativity in their binding. For hydroxysteroid sulphotransferase, the adrenal-derived estrogen 5-androstene-3β,17β-diol was the preferred substrate compared to dehydro-epiandrosterone in the 0–40 nM concentration range. Such properties of the enzymes might be designed to limit the exposure of nuclear receptor to free ligand. Alternatively, a defined subcellular location would perhaps involve the enzymes in the elimination of estrogen after processing of the ligand-bound receptor.</p></div>\",\"PeriodicalId\":17138,\"journal\":{\"name\":\"Journal of steroid biochemistry\",\"volume\":null,\"pages\":null},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1990-08-28\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1016/0022-4731(90)90190-4\",\"citationCount\":\"20\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Journal of steroid biochemistry\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/0022473190901904\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Journal of steroid biochemistry","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/0022473190901904","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Properties of estrogen and hydroxysteroid sulphotransferases in human mammary cancer
Partial purification (~ χ 140-fold) of estrogen sulphotransferase (EC 2.8.2.4) in human mammary estrogen receptor positive cancer tissue was achieved by affinity chromatography on adenosine-3',5'-diphosphate-agarose. It had a Mr, of approximately 70,000 by gel filtration and upon electrophoresis on concave gradient polyacrylamide gels, showed a major (Mr 70,000) and a minor (Mr 200,000) peak of activity. Kinetics of this preparation (estradiol-17β and estrone as substrates), and also that of hydroxysteroid sulphotransferase (EC 2.8.2.2) contained in the cytosol of human mammary cancer MCF-7 cells (5-androstene-3β,17β-diol and dehydroepiandrosterone as substrates), were compared. The enzymes showed very similar behaviour, characterized by high affinity for their steroid substrates (low nM range) and co-operativity in their binding. For hydroxysteroid sulphotransferase, the adrenal-derived estrogen 5-androstene-3β,17β-diol was the preferred substrate compared to dehydro-epiandrosterone in the 0–40 nM concentration range. Such properties of the enzymes might be designed to limit the exposure of nuclear receptor to free ligand. Alternatively, a defined subcellular location would perhaps involve the enzymes in the elimination of estrogen after processing of the ligand-bound receptor.