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Regulation of Phosphorylation of Glycogen Synthase Kinase 3α and the Correlation with Sperm Motility in Human.
Park, Seung Hyun; Kim, Young-Pil; Lee, Jeong Min; Park, Dong-Wook; Seo, Ju Tae; Gye, Myung Chan.
Afiliación
  • Park SH; Department of Life Science and Institute for Natural Sciences, Hanyang University, Seoul, Korea.
  • Kim YP; Department of Life Science and Institute for Natural Sciences, Hanyang University, Seoul, Korea.
  • Lee JM; Department of Life Science and Institute for Natural Sciences, Hanyang University, Seoul, Korea.
  • Park DW; Graduate School of Global Pharmaceutical Industry and Clinical Pharmacy, Ajou University, Suwon, Korea.
  • Seo JT; JTS Urology Medical Center, Seoul, Korea.
  • Gye MC; Department of Life Science and Institute for Natural Sciences, Hanyang University, Seoul, Korea. mcgye@hanyang.ac.kr.
World J Mens Health ; 42(2): 373-383, 2024 Apr.
Article en En | MEDLINE | ID: mdl-37635337
PURPOSE: To unravel the mechanism regulating the phosphorylation of glycogen synthase kinase 3 (GSK3) and the correlation between the inhibitory phosphorylation of GSK3α and sperm motility in human. MATERIALS AND METHODS: The phosphorylation and priming phosphorylated substrate-specific kinase activity of GSK3 were examined in human spermatozoa with various motility conditions. RESULTS: In human spermatozoa, GSK3α/ß was localized in the head, midpiece, and principal piece of tail and p-GSK3α(Ser21) was enriched in the midpiece. The ratio of p-GSK3α(Ser21)/GSK3α was positively coupled with normal sperm motility criteria of World Health Organization. In high-motility spermatozoa, p-GSK3α(Ser21) phosphotyrosine (p-Tyr) proteins but p-GSK3α(Tyr279) markedly increased together with decreased kinase activity of GSK3 after incubation in Ca2+ containing medium. In high-motility spermatozoa, p-GSK3α(Ser21) levels were negatively coupled with kinase activity of GSK3, and which was deregulated in low-motility spermatozoa. In high-motility spermatozoa, 6-bromo-indirubin-3'-oxime, an inhibitor of kinase activity of GSK3 increased p-GSK3α(Ser21) and p-Tyr proteins. p-GSK3α(Ser21) and p-Tyr protein levels were decreased by inhibition of PKA and Akt. Calyculin A, a protein phosphatase-1/2A inhibitor, markedly increased the p-GSK3α(Ser21) and p-Tyr proteins, and significantly increased the motility of low-motility human spermatozoa. CONCLUSIONS: Down regulation of kinase activity of GSK3α by inhibitory phosphorylation was positively coupled with human sperm motility, and which was regulated by Ca2+, PKA, Akt, and PP1. Small-molecule inhibitors of GSK3 and PP1 can be considered to potentiate human sperm motility.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Idioma: En Revista: World J Mens Health Año: 2024 Tipo del documento: Article Pais de publicación: Corea del Sur
Texto completo
Añadir a Mi BVS
Imprimir
XML
PubMed Links
Buscar en Google

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Idioma: En Revista: World J Mens Health Año: 2024 Tipo del documento: Article Pais de publicación: Corea del Sur