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Avian gametes present specific features related to their internal long-term mode of fertilization. Among other central actors of energetic metabolism control, 5'-AMP-activated protein kinase (AMPK) has been suspected to influence sperm functions and thus to play a key role in fertilization success. In the present work, we studied AMPK localization and function in chicken sperm incubated in vitro. Effects of the pharmacological AMPK activators (AICAR, Metformin) and the AMPK inhibitor Compound C were assessed by evaluating AMPKalpha (Thr(172)) phosphorylation (Western blotting), semen quality (viability, motility, ability to perform acrosome reaction), and energetic metabolism indicators (lactate, ATP). Localization of AMPK in the subcellular sperm compartments was evaluated by immunocytochemistry. Total AMPK was found in all compartments except the nucleus but the phosphorylated form, phospho-Thr(172)-AMPK, was essentially localized in the flagellum and the acrosome. The AMPK activators significantly improved AMPK phosphorylation, sperm motility (increase by 40% of motile, 90% of progressive and 60% of rapid sperm), acrosome reaction and lactate production (increase by 40%) and viability. The AMPK inhibitor significantly reduced AMPK phosphorylation and percentages of motile (decrease by 25%), progressive (decrease by 35%), and rapid sperm (decrease by 30%), acrosome reaction, lactate production, and ATP release. The two activators differed in their effect on ATP concentration: AICAR stimulated ATP formation whereas Metformin did not. Our results indicate that AMPK plays a key role in the regulation of chicken sperm functions and metabolism. This action differs from the one suggested in mammals, mainly by its crucial involvement in the acrosome reaction process

Central Role of 5′-AMP-Activated Protein Kinase in Chicken Sperm Functions1