ADAM7 is associated with epididymosomes and integrated into sperm plasma membrane.
During epididymal transit, mammalian sperm acquire selected proteins secreted by the epididymis. We previously showed that a disintegrin and metalloprotease (ADAM) 7 is expressed specifically in the epididymis and transferred to the sperm surface during epididymal transit. Here, we show that mouse ADAM7 secreted to the epididymal lumen is associated with membranous vesicles known as epididymosomes. Furthermore, we found that ADAM7 can be transferred directly from epididymal vesicles to sperm and that it is an integral plasma membrane protein in sperm. Thus, our study provides new information regarding the unique mode of secretion and interaction of ADAM7 during the epididymis-to-sperm transfer process.
Department of Life Science, Gwangju Institute of Science and Technology, Gwangju 500-712, Korea.
Jeong Su
JS
Oh
Cecil
C
Han
Chunghee
C
Cho
D051722:ADAM Proteins / Q000378:metabolism*; D000818:Animals; D002462:Cell Membrane / Q000378:metabolism*; D022162:Cytoplasmic Vesicles / Q000378:metabolism*; D004822:Epididymis / Q000166:cytology / Q000378:metabolism*; D005455:Fluorescent Antibody Technique; D008297:Male; D008565:Membrane Proteins / Q000378:metabolism*; D051379:Mice; D011485:Protein Binding; D013094:Spermatozoa / Q000166:cytology* / Q000378:metabolism*
D008565:Membrane Proteins; D051722:ADAM Proteins; C484106:Adam7 protein, mouse