First Author | Gyamera-Acheampong C | Year | 2010 |
Journal | Fertil Steril | Volume | 93 |
Issue | 4 | Pages | 1112-23 |
PubMed ID | 19342015 | Mgi Jnum | J:233577 |
Mgi Id | MGI:5784984 | Doi | 10.1016/j.fertnstert.2008.12.013 |
Citation | Gyamera-Acheampong C, et al. (2010) PCSK4-null sperm display enhanced protein tyrosine phosphorylation and ADAM2 proteolytic processing during in vitro capacitation. Fertil Steril 93(4):1112-23 |
abstractText | OBJECTIVE: To study the molecular basis for the accelerated capacitation rate in PCSK4-null sperm. DESIGN: Comparative and controlled experimental research study. SETTING: Academic medical institute. ANIMAL(S): Male mice C57BL/6J wild-type or null congenics for the Pcsk4 allele. INTERVENTION(S): Cauda and epididymal sperm were capacitated for varying times. MAIN OUTCOME MEASURE(S): Differences in sperm protein tyrosine phosphorylation and proteolytic processing of sperm-egg ligands ADAM2 and ADAM3. RESULT(S): The PCSK4-null sperm proteins are hyper-tyrosine phosphorylated during capacitation. This hyperphosphorylation is dependent on protein kinase A (PKA), albumin, and calcium. There is also more ADAM2 proteolytic processing from a 46-kDa form of ADAM2 to a 27-kDa form in PCSK4-null sperm than in wild-type sperm. This processing is dependent on cholesterol efflux. CONCLUSION(S): Lack of PCSK4 is associated with quantitative changes in the phosphorylation and proteolysis of sperm proteins during capacitation; therefore, alterations in signal transduction and proteolytic processing during capacitation may underlie the fertilization incompetence of PCSK4-null sperm. More investigation is needed to determine how and to what extent these changes might contribute to the loss of fertilizing ability of PCSK4-null sperm. |