Document Detail


Proteomics-based study on asthenozoospermia: differential expression of proteasome alpha complex.
MedLine Citation:
PMID:  20304782     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
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.
Authors:
Archana Bharadwaj Siva; Duvvuri Butchi Kameshwari; Vaibhav Singh; Kadupu Pavani; Curam Sreenivasacharlu Sundaram; Nandini Rangaraj; Mamata Deenadayal; Sisinthy Shivaji
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2010-03-18
Journal Detail:
Title:  Molecular human reproduction     Volume:  16     ISSN:  1460-2407     ISO Abbreviation:  Mol. Hum. Reprod.     Publication Date:  2010 Jul 
Date Detail:
Created Date:  2010-06-10     Completed Date:  2010-09-07     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  9513710     Medline TA:  Mol Hum Reprod     Country:  England    
Other Details:
Languages:  eng     Pagination:  452-62     Citation Subset:  IM    
Affiliation:
Centre for Cellular and Molecular Biology, Uppal Road, Hyderabad 500 007, India.
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MeSH Terms
Descriptor/Qualifier:
Animals
Asthenozoospermia / metabolism*
Electrophoresis, Gel, Two-Dimensional
Electrophoresis, Polyacrylamide Gel
Gene Expression Regulation*
Humans
Immunoblotting
Male
Proteasome Endopeptidase Complex / metabolism*
Proteomics*
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
Spermatozoa / metabolism
Tandem Mass Spectrometry
Chemical
Reg. No./Substance:
EC 3.4.25.1/Proteasome Endopeptidase Complex

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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