Epididymosome‐Mediated Acquisition of MMSDH, an Androgen‐Dependent and Developmentally Regulated Epididymal Sperm Protein

: A differential proteomics approach led to the identification of several novel epididymal sperm proteins. One of the novel proteins was methylmalonate‐semialdehyde dehydrogenase (MMSDH). In the present study, we carried out an in‐depth characterization to study its regulation by androgen, its appea...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Veröffentlicht in:Journal of andrology 2012-09, Vol.33 (5), p.963-974
Hauptverfasser: Suryawanshi, Amol R., Khan, Shagufta A., Joshi, Chetanchandra S., Khole, Vrinda V.
Format: Artikel
Sprache:eng
Schlagworte:
Online-Zugang:Volltext
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
Beschreibung
Zusammenfassung:: A differential proteomics approach led to the identification of several novel epididymal sperm proteins. One of the novel proteins was methylmalonate‐semialdehyde dehydrogenase (MMSDH). In the present study, we carried out an in‐depth characterization to study its regulation by androgen, its appearance during ontogeny, and the mechanism of its interaction with and acquisition by the sperm. Western blotting and immunohistochemical studies suggest that the protein is present in both tissue and sperm from all regions of the epididymis, indicating synthesis as well as acquisition of the protein in these regions. Androgen depletion resulted in reduction of the MMSDH protein level in the epididymis, which completely disappeared 1 week after castration. The protein reappeared after testosterone propionate injection, indicating that the protein is regulated by androgens. Ontogeny studies indicated that the protein appeared from day 10 postnatal with a gradual increase at day 30, which maximized at day 50, indicating that the protein is developmentally regulated and is probably involved in epididymal development. Sequential extraction of sperm proteins indicated that MMSDH exists both as a peripheral and integral form on the plasma membrane. We also found that the protein can be transferred from the epididymosomes to testicular sperm in vitro. The study provides evidence regarding the acquisition of this multidomain androgen and developmentally regulated protein in the epididymis via the epididymosomes. The molecule has generated enough interest and deserves to be investigated further for its physiological relevance.
ISSN:0196-3635
1939-4640
DOI:10.2164/jandrol.111.014753