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Development of WEE2 kinase inhibitors as novel non-hormonal female contraceptives that target meiosis†.
Hanna, Carol B; Mudaliar, Deepti; John, Kristen; Allen, C Leigh; Sun, Luxin; Hawkinson, Jon E; Schönbrunn, Ernst; Georg, Gunda I; Jensen, Jeffrey T.
Afiliação
  • Hanna CB; Oregon National Primate Research Center, Beaverton, Division of Reproductive & Developmental Sciences OR, USA.
  • Mudaliar D; University of Minnesota, Department of Obstetrics & Gynecology, Minneapolis, MN, USA.
  • John K; University of Minnesota, Department of Obstetrics & Gynecology, Minneapolis, MN, USA.
  • Allen CL; University of Minnesota, Department of Obstetrics & Gynecology, Minneapolis, MN, USA.
  • Sun L; Moffitt Cancer Center, Drug Discovery Department, Tampa, FL, USA.
  • Hawkinson JE; University of Minnesota, Department of Obstetrics & Gynecology, Minneapolis, MN, USA.
  • Schönbrunn E; Moffitt Cancer Center, Drug Discovery Department, Tampa, FL, USA.
  • Georg GI; University of Minnesota, Department of Obstetrics & Gynecology, Minneapolis, MN, USA.
  • Jensen JT; Oregon National Primate Research Center, Beaverton, Division of Reproductive & Developmental Sciences OR, USA.
Biol Reprod ; 103(2): 368-377, 2020 08 04.
Article em En | MEDLINE | ID: mdl-32667031
WEE2 oocyte meiosis inhibiting kinase is a well-conserved oocyte specific kinase with a dual regulatory role during meiosis. Active WEE2 maintains immature, germinal vesicle stage oocytes in prophase I arrest prior to the luteinizing hormone surge and facilitates exit from metaphase II arrest at fertilization. Spontaneous mutations at the WEE2 gene locus in women have been linked to total fertilization failure indicating that selective inhibitors to this kinase could function as non-hormonal contraceptives. Employing co-crystallization with WEE1 G2 checkpoint kinase inhibitors, we revealed the structural basis of action across WEE kinases and determined type I inhibitors were not selective to WEE2 over WEE1. In response, we performed in silico screening by FTMap/FTSite and Schrodinger SiteMap analysis to identify potential allosteric sites, then used an allosterically biased activity assay to conduct high-throughput screening of a 26 000 compound library containing scaffolds of known allosteric inhibitors. Resulting hits were validated and a selective inhibitor that binds full-length WEE2 was identified, designated GPHR-00336382, along with a fragment-like inhibitor that binds the kinase domain, GPHR-00355672. Additionally, we present an in vitro testing workflow to evaluate biological activity of candidate WEE2 inhibitors including; (1) enzyme-linked immunosorbent assays measuring WEE2 phosphorylation activity of cyclin dependent kinase 1 (CDK1; also known as cell division cycle 2 kinase, CDC2), (2) in vitro fertilization of bovine ova to determine inhibition of metaphase II exit, and (3) cell-proliferation assays to look for off-target effects against WEE1 in somatic (mitotic) cells.
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Proteínas Tirosina Quinases / Proteínas de Ciclo Celular / Anticoncepcionais Femininos / Inibidores de Proteínas Quinases / Meiose Limite: Animals / Humans Idioma: En Revista: Biol Reprod Ano de publicação: 2020 Tipo de documento: Article

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Proteínas Tirosina Quinases / Proteínas de Ciclo Celular / Anticoncepcionais Femininos / Inibidores de Proteínas Quinases / Meiose Limite: Animals / Humans Idioma: En Revista: Biol Reprod Ano de publicação: 2020 Tipo de documento: Article