A Seminal Vesicle Autoantigen of Mouse Is Able to Suppress Sperm Capacitation-Related Events Stimulated by Serum Albumin

• Published in: Biology of reproduction 2000-11, Vol.63 (5), p.1562-1566
• Main Authors: HUANG, Yen-Hua, CHU, Sin-Tak, CHEN, Yee-Hsiung
• Format: Article
• Language: English
• Subjects: Animals; Autoantigens - pharmacology; Biological and medical sciences; Epididymis - drug effects; Epididymis - metabolism; Fundamental and applied biological sciences. Psychology; In Vitro Techniques; Male; Mammalian male genital system; Mice; Morphology. Physiology; Phosphorylation; Phosphotyrosine - metabolism; Protein Tyrosine Phosphatases - metabolism; Seminal Vesicles - immunology; Serum Albumin - antagonists & inhibitors; Serum Albumin - pharmacology; Sperm Capacitation - drug effects; Vertebrates: reproduction; Zinc - physiology
• ISSN: 0006-3363; 1529-7268
• DOI: 10.1095/biolreprod63.5.1562

We studied the effect of a mouse seminal vesicle autoantigen (SVA) on BSA-stimulated functions of mouse sperm. Uncapacitated, capacitated, and acrosome-reacted stages of sperm were morphologically scored, and the cellular zinc content was examined cytologically in a modified Tyrode solution at 37°C for 80 min. More than 85% of control cells remained uncapacitated. Addition of 0.3% SVA to the cell incubation did not affect the cell status. Approximately 65% of cells were capacitated in the incubation medium containing 0.3% BSA. Only 30% of the cells became capacitated after incubation with 0.3% BSA and 0.3% SVA together. The decapacitation effect by 0.3% SVA could be subdued by more than 3% BSA in the cell incubation. Whereas BSA did, SVA did not cause removal of Zn 2+ from sperm, but SVA could suppress the BSA effect. The tyrosine phosphorylated proteins in sperm were detected after incubation in a modified HEPES medium containing 0.3% BSA and/or 0.3% SVA at 37°C for 90 min. Whereas BSA enhanced greatly, SVA did not cause phosphorylation of proteins in the range of M r 40 000–120 000. The BSA-stimulated protein tyrosine phosphorylation could be suppressed by SVA in the cell incubation.