Aberrant Distribution of Adam3 in Sperm from Both Angiotensin-converting Enzyme (Ace)- and Calmegin (Clgn)-deficient Mice.
From: Genome Information Research Center, Pharmaceutical Sciences, Research Institute for Microbial Diseases, Osaka University, Osaka, 565-0871, Japan.
Biology of reproduction
- Publish Date: Nov 2006
- ISSN: 0006-3363
- Volume: 75
- Issue: 5
- Pages: 760-6
- Medium: Print
- Language: English
- Citation (JAMA): Yamaguchi Ryo, Yamagata Kazuo, Ikawa Masahito, et al. Aberrant Distribution of Adam3 in Sperm from Both Angiotensin-converting Enzyme (Ace)- and Calmegin (Clgn)-deficient Mice.. Biol. Reprod. Nov 2006;75:760-6
Abstract
Male mice deficient for the calmegin (Clgn) or the angiotensin-converting enzyme (Ace) gene show impaired sperm migration into the oviduct and loss of sperm-zona pellucida binding ability in vitro. Since CLGN is a molecular chaperone for membrane transport of target proteins and ACE is a membrane protein, we looked for ACE on the sperm membranes from Clgn-/- mice. ACE was present and showed normal activity, indicating that CLGN is not involved in transporting ACE to the sperm membranes. The ablation of the Adam2 and Adam3 genes generated animals whose sperm did not bind the zona pellucida, which led us to examine the presence of ADAM2 and ADAM3 in Clgn-/- and Ace-/- sperm. ADAM3 was absent from Clgn-/- sperm. In the Ace-/- mice, while ADAM2 was found normally in the sperm, ADAM3 disappeared from the Triton X-114 detergent-enriched phase after phase separation, which suggests that ACE is involved in distributing ADAM3 to a location where it can participate in sperm-zona pellucida binding. This diminished amount of ADAM3 in the Triton X-114 detergent-enriched phase may explain the inability of Clgn-/- and Ace-/- sperm to bind to the zona pellucida.
Mesh Headings (Keywords): ADAM Proteins, Animals, Calcium-Binding Proteins, Male, Membrane Glycoproteins, Mice, Molecular Chaperones, Peptidyl-Dipeptidase A, Sperm-Ovum Interactions, Spermatozoa, Testis, Zona Pellucida
Check for Full Text / PubMed Unique Identifier (PMID): 16870943
This abstract is part of PubMed, a service of the U.S. National Library of Medicine. PubMed includes more than 17 million citations from MEDLINE and other life science journals for biomedical articles. See Copyright and Disclaimers.
Linked medical terms appearing on this page are added by Healia to help readers find more information and are not part of the original PubMed document.
The data herein was last updated on July 8th, 2008 and may not reflect the most current and accurate data available from NLM.
