{"id":{"repo_id":"uiuc","oai_identifier":"oai:www.ideals.illinois.edu:2142/84230"},"canonical_url":"https://search.dev.ndltd.org/etd/uiuc/oai:www.ideals.illinois.edu:2142/84230","repository":{"repo_id":"uiuc","name":"University of Illinois - Urbana-Champaign","base_url":"https://www.ideals.illinois.edu/oai-pmh"},"display":{"title":"Imaging Prostate Cancer: Design, Synthesis, and in Vivo Testing of Steroidal and Non-Steroidal Androgen Selective PET Radiopharmaceuticals","abstract":"In addition to our non-steroidal work, we have designed and synthesized some high affinity steroidal compounds to probe the mechanism of androgen delivery to the cellular AR transcription mechanism. Sex hormone binding globulin (SHBG) binds testosterone, the principal circulating androgen, in high affinity and is believed to be directly involved in delivery of the hormone to cytoplasmic AR. Other high-affinity AR compounds, such as nor-testosterone, do not bind SHBG and their potential as imaging agents is not clear. We have prepared two classes of high affinity AR, 18F-labeled steroidal compounds, one of which also binds with high affinity to SHBG. In addition, we have studied their distribution in rat models in hope to elucidate the role that SHBG plays in radiopharmaceutical delivery.","abstract_html":"In addition to our non-steroidal work, we have designed and synthesized some high affinity steroidal compounds to probe the mechanism of androgen delivery to the cellular AR transcription mechanism. Sex hormone binding globulin (SHBG) binds testosterone, the principal circulating androgen, in high affinity and is believed to be directly involved in delivery of the hormone to cytoplasmic AR. Other high-affinity AR compounds, such as nor-testosterone, do not bind SHBG and their potential as imaging agents is not clear. We have prepared two classes of high affinity AR, 18F-labeled steroidal compounds, one of which also binds with high affinity to SHBG. In addition, we have studied their distribution in rat models in hope to elucidate the role that SHBG plays in radiopharmaceutical delivery.","abstract_has_math":false,"creators":["Parent, Ephraim Edward"],"institution":"University of Illinois at Urbana-Champaign","degree_name":"Ph.D.","degree_level":"Dissertation","degree_discipline":"Chemistry","degree_department":null,"school":null,"contributors":["Katzenellenbogen, John A."],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2015,"date_issued":"2015-09-25T22:13:34Z","date_published":"2015-09-25T22:13:34Z","updated_at":"2026-07-22T22:26:22Z","subjects":["Health Sciences, Radiology"],"languages":["eng"],"rights":[],"rights_urls":[],"identifier_entries":[{"key":"dc:identifier","label":"Identifier","values":["(MiAaPQ)AAI3223685"],"render_values":[{"text":"(MiAaPQ)AAI3223685","href":null,"code":true}]}]},"links":{"outbound_url":"http://hdl.handle.net/2142/84230","outbound_label":"Handle","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor","label":"Contributor","values":["Katzenellenbogen, John A."]},{"key":"dc:creator","label":"Author","values":["Parent, Ephraim Edward"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date","label":"Dc Date","values":["2015-09-25T22:13:34Z","10000-01-01","2006"]},{"key":"dc:type","label":"Dc Type","values":["text"]},{"key":"thesis:degree_discipline","label":"Discipline","values":["Chemistry"]},{"key":"thesis:degree_level","label":"Degree Level","values":["Dissertation"]},{"key":"thesis:degree_name","label":"Degree Name","values":["Ph.D."]},{"key":"thesis:institution_name","label":"Thesis Institution Name","values":["University of Illinois at Urbana-Champaign"]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["Health Sciences, Radiology"]}]},{"id":"language_rights","label":"Language and Rights","entries":[{"key":"dc:language","label":"Dc Language","values":["eng"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier","label":"Identifier","values":["http://hdl.handle.net/2142/84230","(MiAaPQ)AAI3223685"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description","label":"Description","values":["In addition to our non-steroidal work, we have designed and synthesized some high affinity steroidal compounds to probe the mechanism of androgen delivery to the cellular AR transcription mechanism. 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Sex hormone binding globulin (SHBG) binds testosterone, the principal circulating androgen, in high affinity and is believed to be directly involved in delivery of the hormone to cytoplasmic AR. Other high-affinity AR compounds, such as nor-testosterone, do not bind SHBG and their potential as imaging agents is not clear. We have prepared two classes of high affinity AR, 18F-labeled steroidal compounds, one of which also binds with high affinity to SHBG. In addition, we have studied their distribution in rat models in hope to elucidate the role that SHBG plays in radiopharmaceutical delivery.","Made available in DSpace on 2015-09-25T22:13:34Z (GMT). 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