ADAM7 Is Associated with Epididymosomes and Integrated into Sperm Plasma Membrane

• Published in: Molecules and cells Vol. 28; no. 5; pp. 441 - 446
• Main Authors: Su Oh, Jeong, Han, Cecil, Cho, Chunghee
• Format: Journal Article
• Language: English
• Published: Springer Elsevier Inc 01.11.2009; Korean Society for Molecular and Cellular Biology; 한국분자세포생물학회
• Subjects: ADAM Proteins - metabolism; Animals; Biochemistry; Biomedical and Life Sciences; Biomedicine; Biotechnology; Cell Biology; Cell Membrane - metabolism; Cytoplasmic Vesicles - metabolism; disintegrin; epididymis; Epididymis - cytology; Epididymis - metabolism; epididymosomes; FECONDATION; FECUNDACION; FERTILIZATION; Fluorescent Antibody Technique; Life Sciences; Male; Membrane Proteins - metabolism; metalloprotease; Mice; Protein Binding; SEMEN; sperm; Spermatozoa - cytology; Spermatozoa - metabolism; SPERME; TESTES; TESTICULE; TESTICULOS; 생물학; disintegrin; sperm; metalloprotease; epididymis; fertilization; epididymosomes
• ISSN: 1016-8478; 0219-1032
• DOI: 10.1007/s10059-009-0140-x

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.