Journal of steroid biochemistry最新文献

{"title":"Altered steroidogenic pattern of human granulosa-lutein cells in relation to cumulus cell culture morphology","authors":"Hela Gitay-Goren ,&nbsp;Joseph M. Brandes ,&nbsp;Shalom Bar-Ami","doi":"10.1016/0022-4731(90)90088-A","DOIUrl":"10.1016/0022-4731(90)90088-A","url":null,"abstract":"<div><p>It has been reported that human cumulus-oocyte complexes (COC) retrieved at a stimulated cycle manifest an asynchrony between oocyte meiotic maturation and cumulus mucification. However, when mature COC were subdivided into subtypes marked by the culture morphology of their cumulus cells following 3 days' culture, successful fertilization and cleavage were approximately 1.5-fold lower in mature COC yielding cumulus cells aggregated into clumps (type A and B COC) than in mature COC yielding homogeneously spread cells (type C-D COC). To determine whether the existing relationship between cumulus culture morphology and oocyte functionality in the various COC types (A-D) could be extended to another follicular compartment—the granulosa-lutein (G-L) cells—basal steroid secretion by the corresponding G-L cells was evaluated within 5 days of culture. Over the first 3 days of culture, secretion of progesterone was 3-fold lower and secretion of testosterone (T) was 2.5-fold higher in cultures of G-L cells from follicles yielding type A COC than in type C-D COC. During days 4 and 5 of culture, G-L cells were incubated with or without 10⁻⁷M 3β-hydroxy-5-pregnen-20-one (pregnenolone), dehydroepiandrosterone (DHA), 4-androstene-3,17-dione (androstenedione), or T. The pattern of progesterone level noted over the first 3 days of culture was not altered in the presence of pregnanolone, DHA, androstenedione, or T. Addition of pregnenolone, DHA, androstenedione, or T increased T level 2.5-, 5.6-, 7.3-, and 17.7-fold, respectively, in cultures of G-L cells from follicles yielding type A COC, but did not significantly alter T level in cultures of G-L cells from follicles yielding type C-D COC. In cultures of G-L cells from follicles yielding type A COC, addition of androgens unsaturated at position 4 preferentially increased oestradiol-17β (E₂) level, whereas in cultures of G-L cells of type C-D COC, DHA and androstenedione preferentially increased E₂ level. Taken together, the asynchrony between oocyte and cumulus activity could be diminished when the activity of various follicular cell compartments is evaluated according to cumulus culture morphology rather than cumulus expansion and mucification. The present study suggests that follicles yielding mature COC represent a non-homogeneous population in which G-L cells from follicles yielding type A-B COC manifest a less luteinized state than those from follicles yielding type C-D COC.</p></div>","PeriodicalId":17138,"journal":{"name":"Journal of steroid biochemistry","volume":"36 5","pages":"Pages 457-464"},"PeriodicalIF":0.0,"publicationDate":"1990-08-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0022-4731(90)90088-A","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13299807","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Multiplicity of in vitro glucuronidation of 2-hydroxyestriol","authors":"Tadashi Ohkubo,&nbsp;Ayako Takahashi,&nbsp;Toshio Nambara","doi":"10.1016/0022-4731(90)90094-9","DOIUrl":"10.1016/0022-4731(90)90094-9","url":null,"abstract":"<div><p><em>In vitro</em> glucuronidation of 2-hydroxyestriol has been investigated by means of HPLC with dual-electrode coulometric detection. When incubated with rat or dog liver microsomal preparation in the presence of UDPGA, 2-hydroxyestriol was transformed into the 2-glucuronide together with a small amount of 16- and/or 17-glucuronides. In contrast, incubation of 2-hydroxyestriol with guinea-pig liver microsomal preparation yielded the 3-glucuronide and a trace amount of the 2-glucuronide, but no ring D glucuronides. Upon pretreatment with 3-methylcholanthrene male rat liver exhibited a marked increase in both 2-and 3-glucuronidation activities, whereas female rat liver showed an elevation only in 2-glucuronidation. On the other hand, in male and female rats pretreatment with phenobarbital caused a relatively small increase in the glucuronidation activity of the liver. In the male guinea-pig, glucuronidation was not affected by pretreatment with either of the two compounds. The present result demonstrates the multiplicity of hepatic 2-hydroxyestriol UDP-glucuronyl-transferase in the rat, guinea-pig and dog.</p></div>","PeriodicalId":17138,"journal":{"name":"Journal of steroid biochemistry","volume":"36 5","pages":"Pages 501-503"},"PeriodicalIF":0.0,"publicationDate":"1990-08-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0022-4731(90)90094-9","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13323700","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"American Society of Andrology 16th annual meeting and postgraduate course","authors":"","doi":"10.1016/0022-4731(90)90103-Y","DOIUrl":"https://doi.org/10.1016/0022-4731(90)90103-Y","url":null,"abstract":"","PeriodicalId":17138,"journal":{"name":"Journal of steroid biochemistry","volume":"36 5","pages":"Page IV"},"PeriodicalIF":0.0,"publicationDate":"1990-08-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0022-4731(90)90103-Y","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"136433653","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Animal growth regulation","authors":"","doi":"10.1016/0022-4731(90)90098-D","DOIUrl":"https://doi.org/10.1016/0022-4731(90)90098-D","url":null,"abstract":"","PeriodicalId":17138,"journal":{"name":"Journal of steroid biochemistry","volume":"36 5","pages":"Page 508"},"PeriodicalIF":0.0,"publicationDate":"1990-08-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0022-4731(90)90098-D","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"136465869","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Effects of progesterone, epipregnanolone and RU 38486 on potassium uptake in cultured cortical neurons","authors":"H.C. Bauer ,&nbsp;H. Bauer","doi":"10.1016/0022-4731(90)90216-F","DOIUrl":"10.1016/0022-4731(90)90216-F","url":null,"abstract":"<div><p>It was previously reported that progesterone and its metabolites influence electrical properties of the CNS in many different ways. In the present study we elicited the effects of progesterone, its 5β reduced metabolite epipregnanolone and the anti-progestin compound RU 38486 on potassium uptake in cultured cortical neurons. K⁺ was substituted by the tracer substance ⁸⁶Rb. When hormone treatment (10⁻⁹−10⁻⁷ M/1) was performed for 3 days, addition of progesterone and epipregnanolone led to a significant decrease of ⁸⁶Rb uptake whereas treatment with RU 38486 markedly increased ⁸⁶Rb uptake. The effect of the anti-progestin could be reversed by the addition of increasing amounts of progesterone. Hormone actions were dose-dependent and most distinct when performed from the very first day of culture. Short-term (15min) hormone treatment of neurons did not significantly alter ⁸⁶Rb uptake. These findings suggest a specific receptor mediated progestin action which, in a long-term course, controls potassium uptake across excitable membranes.</p></div>","PeriodicalId":17138,"journal":{"name":"Journal of steroid biochemistry","volume":"36 4","pages":"Pages 269-272"},"PeriodicalIF":0.0,"publicationDate":"1990-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0022-4731(90)90216-F","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13322351","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Antagonism of estrogen- and antiestrogen-induced uterine complement component C3 expression by ICI 164,384","authors":"Matthew S. Galman,&nbsp;Susan A. Sundstrom,&nbsp;C.Richard Lyttle","doi":"10.1016/0022-4731(90)90218-H","DOIUrl":"10.1016/0022-4731(90)90218-H","url":null,"abstract":"<div><p>The uterus of the immature rat synthesizes and secretes complement component C3 in response to estradiol treatment. This response occurs in the uterine epithelial cells and is also stimulated by several antiestrogens including tamoxifen and LY117018. The administration of a new antiestrogen ICI 164,384 blocked the estradiol as well as the antiestrogen-stimulated increases in uterine weight, epithelial cell height, C3 synthesis and C3 mRNA. ICI 164,384 demonstrated no agonist properties in terms of epithelial cell response as determined by C3 expression.</p></div>","PeriodicalId":17138,"journal":{"name":"Journal of steroid biochemistry","volume":"36 4","pages":"Pages 281-286"},"PeriodicalIF":0.0,"publicationDate":"1990-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0022-4731(90)90218-H","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13540121","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Estrogen synthetase (aromatase). Affinity purification of antibody against the cytochrome P450 component","authors":"Kandan Sethumadhavan ,&nbsp;Francis L. Bellino","doi":"10.1016/0022-4731(90)90220-M","DOIUrl":"10.1016/0022-4731(90)90220-M","url":null,"abstract":"<div><p>To procure an affinity gel capable of purifying antibody against the cytochrome <em>P</em>450 component of estrogen synthetase (<em>P</em>450_ES), we coupled purified <em>P</em>450_ES to agarose supports. Our purpose was to compare two differently-activated agarose gels (Affi-Gel 15 and Tresyl-activated Sepharose) with the same <em>P</em>450_ES preparation to compare the efficiency of coupling and the yield of purified antibody. Using supplier-directed protocols to covalently attach <em>P</em>450_ES to each of the supports, and identical procedures to bind and elute anti-<em>P</em>450_ES, we reached the following conclusions. Tresyl-activated Sepharose bound greater amounts of antigen than Affi-Gel 15 based on the amount of residual antigen after the coupling procedure and the amount of bound antigen detected by an ELISA-type method. However, both ligand-coupled supports yielded comparable amounts of purified anti-<em>P</em>450_ES at a 48-fold purification relative to the starting IgG preparation.</p></div>","PeriodicalId":17138,"journal":{"name":"Journal of steroid biochemistry","volume":"36 4","pages":"Pages 295-299"},"PeriodicalIF":0.0,"publicationDate":"1990-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0022-4731(90)90220-M","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13540122","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Molecular endocrinology and steroid hormone action","authors":"","doi":"10.1016/0022-4731(90)90234-J","DOIUrl":"https://doi.org/10.1016/0022-4731(90)90234-J","url":null,"abstract":"","PeriodicalId":17138,"journal":{"name":"Journal of steroid biochemistry","volume":"36 4","pages":"Page 383"},"PeriodicalIF":0.0,"publicationDate":"1990-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0022-4731(90)90234-J","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"136498332","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Direct effect of plasma sex hormone binding globulin (SHBG) on the metabolic clearance rate of 17β-estradiol in the primate","authors":"Stephen R. Plymate ,&nbsp;Pearl C. Namkung ,&nbsp;Louis A. Metej ,&nbsp;Philip H. Petra","doi":"10.1016/0022-4731(90)90223-F","DOIUrl":"10.1016/0022-4731(90)90223-F","url":null,"abstract":"<div><p>Sex hormone binding globulin (SHBG) has been shown to be a major determinant of testosterone clearance in the primate. It has also been suggested that SHBG would also be a determinant of estradiol clearance (MCR-E₂). However, published studies have suggested that the MCR-E₂ do not always vary with changes in the level of SHBG. Therefore, the present study was undertaken to address this issue. The baseline MCR-E₂ was determined in adult male pigtail macaques (<em>Macaca nemestrina</em>). Following the baseline determination of MCR-E₂ the animals were infused with either purified human (h)SHBG or antibody against hSHBG, which also has a high degree of cross-reactivity with primate SHBG. Following the infusions of either hSHBG or anti-SHBG, MCR-E₂ was again determined. In addition, luteinizing hormone (LH) was measured using a mouse Leydig cell bioassay. Following the infusion of hSHBG, a marked increase in serum SHBG was noted and the MCR-E₂ decreased. Associated with the increase in SHBG, the SHBG bound T levels decreased and LH increased. Following the infusion of antibody, serum SHBG decreased, and the MCR-E₂ also decreased. With the decrease in SHBG following the antibody infusion, non-SHBG bound T increased and serum LH fell. This study demonstrates that an increase in the serum SHBG levels is associated with a decrease in MCR-E₂, however, an acute decrease in serum SHBG also decreases the MCR-E₂. This later result demonstrates that factors in addition to serum SHBG binding may be important in determining the MCR-E₂.</p></div>","PeriodicalId":17138,"journal":{"name":"Journal of steroid biochemistry","volume":"36 4","pages":"Pages 311-317"},"PeriodicalIF":0.0,"publicationDate":"1990-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0022-4731(90)90223-F","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13540125","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Effect of atp on the regulation of the steroid binding activity of the oestradiol receptor","authors":"Hooshang Lahooti,&nbsp;Thor Thorsen,&nbsp;Asbjørn Aakvaag","doi":"10.1016/0022-4731(90)90226-I","DOIUrl":"10.1016/0022-4731(90)90226-I","url":null,"abstract":"<div><p>We have observed that ATP induces a second type of oestradiol binding site with slightly lower affinity (<em>K</em>_<em>a</em> 3.3 × 10⁸M⁻¹) and lower sedimentation coefficient (4S) in cytosol from immature lamb uterus and MCF-7 cells. A factor isolated from immature lamb uterine nuclear extract was found to decrease the steroid binding activity of oestradiol receptor that had been purified by heparin Sepharose and oestradiol-Sepharose chromatography. Inhibition of this factor by known phosphatase inhibitors, indicated that this factor may be a phosphatase. Another factor isolated from immature lamb uterine cytosol was found to enhance the effect of ATP on receptor binding in cytosol from immature lamb uterus and MCF-7 cells. The ability of this factor to phosphorylate a partially purified cytosol receptor from immature lamb uterus when incubated with [γ³²P]ATP, indicates that this factor is a phosphokinase. The phosphorylated products after labeling with [³H]tamoxifen aziridine were characterized by sodium dodecyl sulphate-polyacrylamide gel electrophoresis. Three phosphorylated proteins with molecular weights 150, 97, and 67 kDa bound [³H]tamoxifen aziridine. Ammonium sulphate precipitated cytosol oestradiol receptor from immature lamb uterus was inactivated with receptor inactivating factor and then reactivated with receptor activating factor in the presence of [γ³²P]ATP and subsequently affinity labelled with [³H]tamoxifen aziridine. The affinity labelled oestradiol receptor was immunopurified with the monoclonal antibody JS 34/32. Three proteins with molecular weights 67, 50 and 43 kDa specifically bound [³H]tamoxifen aziridine and only 43 kDa receptor fragment was phosphorylated. The relevance of inactivation/reactivation of oestradiol receptor to the dephosphorylation/phosphorylation of receptor is discussed.</p></div>","PeriodicalId":17138,"journal":{"name":"Journal of steroid biochemistry","volume":"36 4","pages":"Pages 333-343"},"PeriodicalIF":0.0,"publicationDate":"1990-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0022-4731(90)90226-I","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13322352","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}