Enhancement of mouse sperm motility by trophinin-binding peptide.

BACKGROUND:Trophinin is an intrinsic membrane protein that forms a complex in the cytoplasm with bystin and tastin, linking it microtubule-associated motor dynein (ATPase) in some cell types. Previously, we found that human sperm tails contain trophinin, bystin and tastin proteins, and that trophinin-binding (glycine, tryptophan, arginine, glutamine) peptide enhanced motility of human sperm. METHODS:Immunohistochemistry was employed to determine trophinin protein in mouse spermatozoa from wild type mouse, by using spermatozoa from trophinin null mutant mice as a negative control. Multivalent 8-branched GWduanyu1745 (glycine, tryptophan, arginine, glutamine) peptide or was chemically synthesized, purified by HPLC and its structure was confirmed by MALDI-TOF mass spectrometry. Effect of on mouse spermatozoa from wild type and trophinin null mutant was assessed by a computer-assisted semen analyzer (CASA). RESULTS:Anti-trophinin antibody stained the principal (central) piece of the tail of wild type mouse sperm, whereas the antibody showed no staining on trophinin null sperm. Phage particles displaying GWduanyu1745 bound to the principal piece of sperm tail from wild type but not trophinin null mice. GWduanyu1745-MAPS enhanced motility of spermatozoa from wild type but not trophinin null mice. CASA showed that GWduanyu1745-MAPS enhanced both progressive motility and rapid motility in wild type mouse sperm. CONCLUSIONS:Present study established the expression of trophinin in the mouse sperm tail and trophinin-dependent effect of GWduanyu1745-MAPS on sperm motility. GWduanyu1745 causes a significant increase in sperm motility.

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