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a Department of Cell Biology and Human Anatomy, University of California, Davis School of Medicine, Davis, California 95616
b Veterans Affairs Medical Center and Oregon Health Sciences University, Portland, Oregon 97201
The signal transduction pathways involved in the progesterone (P4)-initiated mammalian sperm acrosome reaction (AR) are not fully understood. To investigate the role of the protein kinase A (PKA) pathway in the P4-initiated AR, we probed this pathway by pretreating capacitated human sperm with reagents designed to either inhibit PKA activation or disrupt PKA/A kinase anchoring protein (AKAP) interactions. Preincubation with the stearated (membrane permeable) PKA inhibitor, PKI 
5-24 (S-PKI 5-24), significantly inhibited the P4-initiated AR at 10 µM as compared to stearated control peptide. In contrast, preincubation with 100 µM nonstearated PKI 5-24 did not significantly inhibit versus solvent control. Preincubation with the PKA inhibitor Rp-8-Br-cAMP at 500 µM and 150 µM significantly inhibited the P4-initiated AR versus 8-Br-cAMP and versus solvent. Preincubation with the anchoring inhibitory peptide S-Ht-31 significantly stimulated the P4-initiated AR at 10, 3, and 1 µM versus inactive control peptide. The stimulation of the P4-initiated AR by 3 µM S-Ht31 was significantly inhibited by the addition of 30 µM S-PKI 5-24 prior to the addition of S-Ht31. Preincubation with S-PKI 5-24 (30 µM) partially inhibited the ionomycin (50 µM)-initiated AR. A role for PKA in the P4-initiated AR may exist both upstream and downstream of Ca2+ entry. Our studies present the first evidence for the participation of PKA in the P4-initiated AR and also suggest that AKAPs are involved in the PKA-mediated events.
1 This research was supported by NIH grant HD-36408 to D.W.C. and HD-23098 to S.M.
2 Correspondence: Stanley Meizel, Department of Cell Biology and Human Anatomy, Rm. 3301 Tupper Hall, University of California, Davis, Davis, CA 95616. FAX: 530 752 8520; smeizel{at}ucdavis.edu
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