| First Author | Phopin K | Year | 2012 |
| Journal | Mol Reprod Dev | Volume | 79 |
| Issue | 3 | Pages | 208-17 |
| PubMed ID | 22231989 | Mgi Jnum | J:182706 |
| Mgi Id | MGI:5316351 | Doi | 10.1002/mrd.22016 |
| Citation | Phopin K, et al. (2012) Distribution, crypticity, stability, and localization of alpha-L-fucosidase of mouse cauda epididymal sperm. Mol Reprod Dev 79(3):208-17 |
| abstractText | Sperm-associated and semen-specific isoforms of alpha-L-fucosidase are thought to function in fertilization in numerous organisms. Here, we report the localization, distribution, crypticity, and stability of this enzyme in mouse cauda epididymal sperm and cauda fluid. Western analysis revealed that the sperm-associated alpha-L-fucosidase is present as two isoforms (Mr approximately 49 and 56 kDa), whereas the cauda fluid alpha-L-fucosidase shows a single band at 50 kDa. alpha-L-Fucosidase activity was detected using the fluorogenic substrate 4-MU-FUC. Of the total alpha-L-fucosidase activity recovered in the cauda epididymal contents, 74% was found in the cell-free cauda fluid and about 7% was found in sperm cells. During capacitation or permeabilization, cryptic intracellular stores of soluble enzyme were released to the supernatant, while leaving bound enzyme concentrated within the small volume of sperm. Moreover, membrane-associated enzyme activity was still detectable in acrosome-reacted cells. Immunofluorescence studies support the presence of alpha-L-fucosidase (originally localizing at the acrosomal area) at the equatorial segment after the acrosome reaction. alpha-L-Fucosidase activity of both cauda fluid and sperm at 37 degrees C, 5% CO(2) was relatively stable and detectable up to 72 hr. The stability and appearance of mouse sperm-associated alpha-L-fucosidase in the equatorial segment after the acrosome reaction suggest that alpha-L-fucosidase may be involved in sperm-egg interaction. |
