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Mol. Cells 2009; 28(5): 441-446

Published online October 21, 2009

https://doi.org/10.1007/s10059-009-0140-x

© The Korean Society for Molecular and Cellular Biology

ADAM7 Is Associated with Epididymosomes and
Integrated into Sperm Plasma Membrane

Jeong Su Oh, Cecil Han, and Chunghee Cho

Received: July 6, 2009; Accepted: September 1, 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.

Keywords disintegrin, epididymis, epididymosomes, fertilization, metalloprotease, sperm

Article

Research Article

Mol. Cells 2009; 28(5): 441-446

Published online November 30, 2009 https://doi.org/10.1007/s10059-009-0140-x

Copyright © The Korean Society for Molecular and Cellular Biology.

ADAM7 Is Associated with Epididymosomes and
Integrated into Sperm Plasma Membrane

Jeong Su Oh, Cecil Han, and Chunghee Cho

Received: July 6, 2009; Accepted: September 1, 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.

Keywords: disintegrin, epididymis, epididymosomes, fertilization, metalloprotease, sperm

Mol. Cells
Nov 30, 2023 Vol.46 No.11, pp. 655~725
COVER PICTURE
Kim et al. (pp. 710-724) demonstrated that a pathogen-derived Ralstonia pseudosolanacearum type III effector RipL delays flowering time and enhances susceptibility to bacterial infection in Arabidopsis thaliana. Shown is the RipL-expressing Arabidopsis plant, which displays general dampening of the transcriptional program during pathogen infection, grown in long-day conditions.

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