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a Division of Research, Department of Obstetrics and Gynecology, Medical College of Ohio, Toledo, Ohio 43614
The involvement of serine and threonine phosphorylation in human sperm capacitation was investigated. Anti-phosphoserine monoclonal antibody (mAb) recognized six protein bands in the 43–55-kDa, 94 ± 2-kDa, 110-kDa, and 190-kDa molecular regions, in addition to a faint band each in the 18-kDa and 35-kDa regions. Anti-phosphothreonine mAb recognized protein bands in six similar regions, except that the 18-kDa, 35-kDa, and 94 ± 2-kDa protein bands were sharper and thicker, and an additional band was observed in the 110-kDa molecular region. In the 43–55-kDa molecular region, there was a well-characterized glycoprotein, designated fertilization antigen, that showed a further increase in serine/threonine phosphorylation after exposure to solubilized human zona pellucida. In a cell-free in vitro kinase assay carried out on beads or in solution, four to eight proteins belonging to similar molecular regions, namely 20 ± 2 kDa, 43–55 kDa, 94 ± 2 kDa, and 110 ± 10 kDa, as well as in 80 ± 4 and 210 ± 10 kDa regions, were phosphorylated at dual residues (serine/tyrosine and threonine/tyrosine). Capacitation increased the intensity of serine/threonine phosphorylation per sperm cell, increased the number of sperm cells that were phosphorylated, and induced a subcellular shift in the serine/threonine-specific fluorescence. These findings indicate that protein serine/threonine phosphorylation is involved and may have a physiological role in sperm capacitation.
2 Correspondence: Rajesh K. Naz, Division of Research, Health Education Building, Rm 211, Medical College of Ohio, 3055 Arlington Avenue, Toledo, OH 43614-5806. FAX: 419 383 4473; rnaz{at}mco.edu
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