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You searched for subject:( SULT2A1). Showing records 1 – 2 of 2 total matches.

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University of Guelph

1. Desnoyer, Jillian Eve. The formation of androstenone conjugates from testes tissue of the mature boar.

Degree: 2011, University of Guelph

The accumulation of androstenone in the fat of mature boars results in boar taint; the conjugation of androstenone would decrease this important meat quality problem by decreasing the accumulation and increasing the excretion of androstenone. Leydig cells and testis microsomes from mature boars were incubated with radiolabeled pregnenolone, and the free and conjugated metabolites were examined by HPLC. Sulfated androstenone with a mass of 367 m/z was directly identified by MS, with a novel tentative structure of 3-keto-4- sulfoxy-androstenone. Addition of enolase to the microsomal incubations increased the formation of 3-keto-4-sulfoxy-androstenone. Overexpression of SULT2A1 in HEK cells resulted in the sulfoconjugation of dehydroepiandrosterone, but not androstenone, suggesting that SULT2A1 may not be involved in sulfoconjugation of androstenone. This thesis describes the novel direct characterization of androstenone sulfate and the importance of enolase in its formation. The relevance to boar taint metabolism is discussed. Advisors/Committee Members: Squires, E.J (advisor).

Subjects/Keywords: androstenone; conjugate; SULT2A1; boar taint; androstene; cloning; enolase; HPLC; Leydig cell; sulfoconjugation; sulfation; adipocytes; porcine; pig; metabolism

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APA (6th Edition):

Desnoyer, J. E. (2011). The formation of androstenone conjugates from testes tissue of the mature boar. (Thesis). University of Guelph. Retrieved from https://atrium.lib.uoguelph.ca/xmlui/handle/10214/3165

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Chicago Manual of Style (16th Edition):

Desnoyer, Jillian Eve. “The formation of androstenone conjugates from testes tissue of the mature boar. ” 2011. Thesis, University of Guelph. Accessed July 15, 2019. https://atrium.lib.uoguelph.ca/xmlui/handle/10214/3165.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

MLA Handbook (7th Edition):

Desnoyer, Jillian Eve. “The formation of androstenone conjugates from testes tissue of the mature boar. ” 2011. Web. 15 Jul 2019.

Vancouver:

Desnoyer JE. The formation of androstenone conjugates from testes tissue of the mature boar. [Internet] [Thesis]. University of Guelph; 2011. [cited 2019 Jul 15]. Available from: https://atrium.lib.uoguelph.ca/xmlui/handle/10214/3165.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Council of Science Editors:

Desnoyer JE. The formation of androstenone conjugates from testes tissue of the mature boar. [Thesis]. University of Guelph; 2011. Available from: https://atrium.lib.uoguelph.ca/xmlui/handle/10214/3165

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation


University of Florida

2. Ambadapadi, Sriram. Modulation of Steroid Sulfonation by Small Molecules That Interact with Sulfotransferases and Sulfatases.

Degree: PhD, Pharmaceutical Sciences - Medicinal Chemistry, 2012, University of Florida

Sulfonation, a major phase-II conjugation reaction turns otherwisehighly lipophilic compounds water soluble and makes them amenable to excretionvia the kidneys. Sulfonated forms of compounds such as 17ß-Estradiol (17ß-E2) also act as transport formswhich are made available to various tissues by the plasma. Several smallmolecules interact with sulfotransferases to alter their activity. In thisstudy, interaction of two compounds, celecoxib and triclosan, were explored atthe molecular level. It was observed previously that 17ß-E2 which, upon sulfotransferase2A1 (SULT2A1) catalysis forms 17ß-E2 3-sulfate as the major productand also forms 17ß-E217-sulfate as the minor product, switches its sulfonation pattern in thepresence of the cox-2 inhibitor, celecoxib to form more 17ß-E2 17-sulfate in human livercytosol. To investigate the reason for this switching at the molecular level,steroids analogous to 17ß-E2were selected for the study of their sulfonation by SULT2A1 in the presence ofcelecoxib. Enzyme kinetic data when coupled with in silico ligand docking studies suggests that celecoxib binds inthe large binding site of SULT2A1 and, while prohibiting the normal binding ofthe substrates facilitates, for appropriately shaped substrates, a binding modethat allows more 17-sulfonation. The effect of celecoxib on the sheep and rat liver cytosolswas also tested in vitro with 17ß-E2 to see if they replicate thehuman model. There was inhibition of sulfonation but no switching in femalesheep and male rat. In female rat there was no observable effect of celecoxib,but it was interesting to note that 17ß-E217-sulfate was the major product of 17ß-E2sulfonation. Triclosan, an antibacterial used in preparations such soapsand tooth pastes has been shown to interact with off-target proteins.  Since it is shown to be excreted mainly asits conjugates, studies were undertaken to identify the major isoforms ofsulfotransferase enzymes bringing about this biotransformation. SULT1B1 andSULT1A1 with Vmax/Km values of 820 and 320 ml/min/mg arethe most active isoforms. Triclosan also was inhibitory towards the activitiesof other major human sulfotransferase and sulfatase enzymes. ( en ) Advisors/Committee Members: James, Margaret O (committee chair), Sloan, Kenneth B (committee member), Luesch, Hendrik (committee member), Dunn, Ben M (committee member).

Subjects/Keywords: Breast cancer; Enzymes; Estrogens; Ligands; Liver; Molecules; Rats; Sheep; Steroids; Sulfates; 17a-estradiol  – 17b-dihydroequilenin  – 17b-dihydroequilin  – 17b-estradiol  – 2-hydroxyestradiol  – 3-methoxyestradiol  – 4-hydroxyestradiol  – 4-methylumbelliferone-sulfate  – 6-dehydroestradiol  – 9-dehydroestradiol  – androstenediol  – catechol-estrogens  – celecoxib  – dehydroepiandrosterone  – epitestosterone  – estradiol  – estradiol-17-sulfate  – estradiol-3-sulfate  – estrone  – homology-modeling  – ligand-docking  – molecular-modeling  – st-60  – sulfatase  – sulfation  – sulfonation  – sulfotransferase  – sult1a1  – sult1a3  – sult1b1  – sult1e1  – sult2a1  – testosterone  – triclosan

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APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6th Edition):

Ambadapadi, S. (2012). Modulation of Steroid Sulfonation by Small Molecules That Interact with Sulfotransferases and Sulfatases. (Doctoral Dissertation). University of Florida. Retrieved from http://ufdc.ufl.edu/UFE0044990

Chicago Manual of Style (16th Edition):

Ambadapadi, Sriram. “Modulation of Steroid Sulfonation by Small Molecules That Interact with Sulfotransferases and Sulfatases.” 2012. Doctoral Dissertation, University of Florida. Accessed July 15, 2019. http://ufdc.ufl.edu/UFE0044990.

MLA Handbook (7th Edition):

Ambadapadi, Sriram. “Modulation of Steroid Sulfonation by Small Molecules That Interact with Sulfotransferases and Sulfatases.” 2012. Web. 15 Jul 2019.

Vancouver:

Ambadapadi S. Modulation of Steroid Sulfonation by Small Molecules That Interact with Sulfotransferases and Sulfatases. [Internet] [Doctoral dissertation]. University of Florida; 2012. [cited 2019 Jul 15]. Available from: http://ufdc.ufl.edu/UFE0044990.

Council of Science Editors:

Ambadapadi S. Modulation of Steroid Sulfonation by Small Molecules That Interact with Sulfotransferases and Sulfatases. [Doctoral Dissertation]. University of Florida; 2012. Available from: http://ufdc.ufl.edu/UFE0044990

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