Biochemical characterization of stallion prostasomes and comparison to their human counterparts.
Abstract: Release of nanometer-sized prostasomes into human and equine semen suggests essential functions in their relationships with sperm cells and the fertilization process. The two types of prostasomes displayed ultrastructural similarities, albeit the human prostasomes were somewhat larger than the stallion prostasomes. A high ratio of saturated fatty acids was characteristic for the two prostasome types. Electrophoretic separation systems revealed an equine prostasomal pattern different from that of human. The 21 distinctive low molecular weight protein spots in the 2D-gel (with no counterparts in human prostasomes) were identified via peptide mass fingerprinting, several of which may be different isoforms. Out of the three high molecular weight bands characteristic for human prostasomes (CD10, CD13, and CD26), CD10 and CD13 were retrieved in equine prostasomes. We present some new proteins of horse prostasomes not found in their human counterparts. Further studies are warranted to reveal the function of these proteins.
Publication Date: 2013-08-02 PubMed ID: 23909385DOI: 10.3109/19396368.2013.822612Google Scholar: Lookup
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- Comparative Study
- Journal Article
- Research Support
- Non-U.S. Gov't
Summary
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The research article focuses on the biochemical analysis of stallion prostasomes (membrane-vesicles produced by the prostate gland), comparing them to human prostasomes to better understand their roles in sperm functionality and fertility.
Comparison of Prostasomes
- The researchers examined human and equine (horse) prostasomes, noting that both types were released into semen and are therefore assumed to play a crucial role in sperm behavior and the fertilization process.
- Structurally, both types of prostasomes were found to be similar. However, human prostasomes were somewhat larger than equine prostasomes.
Nature of Prostasomes
- Both types of prostasomes exhibited a high concentration of saturated fatty acids. This is worth noting because the biochemistry of prostasomes can play a significant role in their functional interactions within the body.
Protein Composition of Prostasomes
- Electrophoretic separation technology was utilized to identify the protein profile of the equine prostasomes, comparing it to that of human prostasomes.
- These techniques revealed the presence of 21 distinctive low molecular weight proteins in the stallion prostasomes that were not observed in the human equivalents. These proteins were then identified using peptide mass fingerprinting. It was suggested that some of these proteins may exist in different isoforms (variants).
- Of the three high molecular weight protein bands that are traditionally seen in human prostasomes (CD10, CD13, and CD26), only CD10 and CD13 were found in horse prostasomes.
Future Studies
- The research team identified several new proteins in horse prostasomes that are not typically found in human prostasomes. The potential function of these proteins in the context of their role in reproduction is unknown and the authors call for further research to understand these differences.
Cite This Article
APA
Ronquist GK, Ek B, Ronquist G, Morrell J, Carlsson L, Larsson A.
(2013).
Biochemical characterization of stallion prostasomes and comparison to their human counterparts.
Syst Biol Reprod Med, 59(6), 297-303.
https://doi.org/10.3109/19396368.2013.822612 Publication
Researcher Affiliations
- Department of Medical Sciences, Clinical Chemistry , University Hospital , Uppsala , Sweden.
MeSH Terms
- Animals
- Chromatography, Gas
- Electrophoresis, Gel, Two-Dimensional
- Electrophoresis, Polyacrylamide Gel
- Fatty Acids / metabolism
- Horses
- Humans
- Male
- Microscopy, Electron
- Prostate / metabolism
- Prostate / ultrastructure
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