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Part 1: Document Description
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Citation |
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Title: |
Regulation of Phosphorylation of Glycogen Synthase Kinase 3α and the Correlation with Sperm Motility in Human |
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Identification Number: |
doi:10.7910/DVN/5FTZAP |
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Distributor: |
Harvard Dataverse |
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Date of Distribution: |
2023-08-08 |
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Version: |
1 |
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Bibliographic Citation: |
Myung Chan Gye, 2023, "Regulation of Phosphorylation of Glycogen Synthase Kinase 3α and the Correlation with Sperm Motility in Human", https://doi.org/10.7910/DVN/5FTZAP, Harvard Dataverse, V1 |
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Citation |
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Title: |
Regulation of Phosphorylation of Glycogen Synthase Kinase 3α and the Correlation with Sperm Motility in Human |
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Identification Number: |
doi:10.7910/DVN/5FTZAP |
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Authoring Entity: |
Myung Chan Gye (Department of Life Science and Institute for Natural Sciences, Hanyang University) |
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Distributor: |
Harvard Dataverse |
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Access Authority: |
Myung Chan Gye |
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Depositor: |
Park, Hyun Jun |
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Date of Deposit: |
2023-08-08 |
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Holdings Information: |
https://doi.org/10.7910/DVN/5FTZAP |
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Study Scope |
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Keywords: |
Medicine, Health and Life Sciences |
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Abstract: |
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/β 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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Related Publications |
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Citation |
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Bibliographic Citation: |
pISSN: 2287-4208 / eISSN: 2287-4690 World J Mens Health Published online, 2023 https://doi.org/10.5534/wjmh.230004 |
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Label: |
WJMH-23-0004R1 data.xlsx |
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Notes: |
application/vnd.openxmlformats-officedocument.spreadsheetml.sheet |