Proteomics-based study on asthenozoospermia: differential expression of proteasome alpha complex

With a view to understand the molecular basis of sperm motility, we have tried to establish the human sperm proteome by two-dimensional PAGE MALDI MS/MS analysis. We report identification of 75 different proteins in the human spermatozoa. Comparative proteome analysis was carried out for asthenozoos...

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Published inMolecular human reproduction Vol. 16; no. 7; pp. 452 - 462
Main Authors Siva, Archana Bharadwaj, Kameshwari, Duvvuri Butchi, Singh, Vaibhav, Pavani, Kadupu, Sundaram, Curam Sreenivasacharlu, Rangaraj, Nandini, Deenadayal, Mamata, Shivaji, Sisinthy
Format Journal Article
LanguageEnglish
Published Oxford Oxford University Press 01.07.2010
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Summary:With a view to understand the molecular basis of sperm motility, we have tried to establish the human sperm proteome by two-dimensional PAGE MALDI MS/MS analysis. We report identification of 75 different proteins in the human spermatozoa. Comparative proteome analysis was carried out for asthenozoospermic and normozoospermic patients to understand the molecular basis of sperm motility. Analysis revealed eight proteins (including one unidentified) with altered intensity between the groups. Differential proteins distributed into three functional groups: ‘energy and metabolism’ (triose-phosphate isomerase, glycerol kinase 2, testis specific isoform and succinyl-CoA:3-ketoacid co-enzyme A transferase 1, mitochondrial precursor); ‘movement and organization’ (tubulin beta 2C and tektin 1) and ‘protein turnover, folding and stress response’ (proteasome alpha 3 subunit and heat shock-related 70 kDa protein 2). It was interesting to note that although the proteins falling in the functional group of ‘energy and metabolism’ are higher in the asthenozoospermic patients, the other two functional groups contain proteins, which are higher in the normozoospermic samples. Validation of results carried out for proteasome alpha 3 subunit by immunoblotting and confocal microscopy, confirmed significant changes in intensity of proteasome alpha 3 subunit in asthenozoospermic samples when compared with normozoospermic controls. Significant positive correlation too was found between proteasome alpha 3 subunit levels and rapid, linear progressive motility of the spermatozoa. In our understanding, this data would contribute appreciably to the presently limited information available about the proteins implicated in human sperm motility.
Bibliography:istex:F12A4EB49CA42D8C127832C127116F7658E60F1D
ArticleID:gaq009
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ISSN:1360-9947
1460-2407
DOI:10.1093/molehr/gaq009