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ADAM7 is associated with epididymosomes and integrated into sperm plasma membrane
- Source :
- Molecules and Cells. 28:441-446
- Publication Year :
- 2009
- Publisher :
- Springer Science and Business Media LLC, 2009.
-
Abstract
- 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.
- Subjects :
- Male
endocrine system
Fluorescent Antibody Technique
Mice
medicine
Disintegrin
Animals
Secretion
Molecular Biology
reproductive and urinary physiology
Sperm plasma membrane
Epididymis
Metalloproteinase
biology
urogenital system
Chemistry
Vesicle
Cell Membrane
Cytoplasmic Vesicles
Membrane Proteins
Cell Biology
General Medicine
Spermatozoa
Sperm
Cell biology
ADAM Proteins
medicine.anatomical_structure
Immunology
biology.protein
ADAM7
Protein Binding
Subjects
Details
- ISSN :
- 02191032 and 10168478
- Volume :
- 28
- Database :
- OpenAIRE
- Journal :
- Molecules and Cells
- Accession number :
- edsair.doi.dedup.....b631cdf51986679e409d53a970d447a6