Related Experiment Video
Updated: Apr 20, 2026

Medium-throughput Screening Assays for Assessment of Effects on Ca2+-Signaling and Acrosome Reaction in Human Sperm
Published on: March 1, 2019
Emodin inhibits human sperm functions by reducing sperm [Ca(2+)]i and tyrosine phosphorylation
Tao Luo1, Na Li1, Yuan-qiao He1
1Institute of Life Science, Nanchang University, Nanchang, Jiangxi 330031, PR China.
Abstract:
Emodin, a bioactive anthraquinone widely used in Chinese traditional medicine, disrupts mouse testicular gene expression in vivo. In this study, we investigated the toxicity of emodin to human sperm in vitro. Different doses of emodin (25, 50, 100, 200 and 400μM) were applied to ejaculated human sperm. The results indicated that 100, 200 and 400μM emodin significantly inhibited the total motility, progressive motility and linear velocity of human sperm. In addition, sperm's ability to penetrate viscous medium together with progesterone induced capacitation and acrosome reaction was also adversely affected by emodin. In contrast, emodin did not affect sperm viability. Furthermore, intracellular Ca(2+) concentration ([Ca(2+)]i) and tyrosine phosphorylation, which serve as key regulators of sperm function, were dose-dependently reduced by emodin (50-400μM). These results suggest that emodin inhibits human sperm functions by reducing sperm [Ca(2+)]i and suppressing tyrosine phosphorylation in vitro.
More Related Videos
19:26Measuring Intracellular Ca2+ Changes in Human Sperm using Four Techniques: Conventional Fluorometry, Stopped Flow Fluorometry, Flow Cytometry and Single Cell Imaging
Published on: May 24, 2013
09:47Recording Electrical Currents across the Plasma Membrane of Mammalian Sperm Cells
Published on: February 14, 2021
Related Concept Videos
Feedback Regulation of Calcium Concentration
Various transmembrane receptors, such as G protein-coupled receptors (GPCRs), elicit a response to extracellular signals by increasing cytosolic calcium. Activated GPCRs...
Spermatogenesis
Infertility in Males
Calmodulin-dependent Signaling
The Ca2+-CaM complex does not have enzymatic activity by itself. Instead, the complex binds downstream target proteins, including membrane proteins or enzymes,...
Fertilization
Sperm Structure and Semen Composition