Stallion epididymal fluid proteome: qualitative and quantitative characterization; secretion and dynamic changes of major proteins.
Abstract: Proteins present in and secreted into the lumen of various regions of the stallion epididymis were characterized qualitatively and quantitatively by two-dimensional electrophoresis. Using this proteomic approach, 201 proteins were found in the lumen and 117 were found that were secreted by the epithelium in various parts of the organ. Eighteen proteins made up 92.6% of the total epididymal secretory activity, lactoferrin (41.2%) and clusterin (24.8%) being the most abundant. Procathepsin D, HE1/CTP (cholesterol transfer protein), GPX (glutathione peroxidase), beta-N-acetyl-hexosaminidase, and PGDS (prostaglandin D2 synthase) were the other major compounds secreted. The most abundant proteins found in the luminal fluid were albumin and the secreted proteins: lactoferrin, PGDS, GPX, HE1/CTP, and hexosaminidase. Three main secretory epididymal regions were identified from the protein pattern, i.e., regions E0-E2, E3-E5, and E6-E9. Region E0-E2 was characterized by the secretion of clusterin (53%), PGDS (44%), and GPX (6%). Region E3-E5 had the highest number of secreted proteins, the highest protein concentrations (60-80 mg/ml), and the highest spermatocrit value (85%). Lactoferrin (60% in E4), clusterin (29% in E3), hexosaminidase (10% in E3), and procathepsin D (6.9% in E4) were the most abundant proteins in this region. Region E6-E9, in which few region-specific secreted compounds were found, was characterized by a high quantity of lactoferrin in the luminal fluid (2-14 mg/ml). Comparison between the secretion of the major proteins and their concentrations in the lumen throughout the organ showed that the behavior of each protein is specific, in particular for the three isoforms of clusterin.
Publication Date: 2000-05-20 PubMed ID: 10819784DOI: 10.1095/biolreprod62.6.1790Google Scholar: Lookup
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- Journal Article
- Research Support
- Non-U.S. Gov't
Summary
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The research investigates the different proteins found in the lumen and those secreted by the epithelium in various regions of the stallion epididymis. It identifies 201 proteins in the lumen and 117 secreted ones, with lactoferrin and clusterin being the most prevalent. The study also outlines the varying protein concentrations in different epididymal regions.
Methodology
- The study uses two-dimensional electrophoresis for the qualitative and quantitative characterization of proteins in the lumen and proteins secreted into the lumen by the epithelium in various regions of the stallion epididymis.
- Through this proteomic approach, the researchers were able to identify 201 proteins in the lumen and 117 secreted by the epithelium.
Main Findings
- The researchers discovered that of all the proteins secreted, eighteen predominated, accounting for 92.6% of the total secretory activity in the epididymis. The most abundant of these were lactoferrin (41.2%) and clusterin (24.8%).
- Other major compounds secreted included procathepsin D, HE1/CTP (cholesterol transfer protein), GPX (glutathione peroxidase), beta-N-acetyl-hexosaminidase, and PGDS (prostaglandin D2 synthase).
- The luminal fluid’s most abundant proteins were albumin and the secreted proteins: lactoferrin, PGDS, GPX, HE1/CTP, and hexosaminidase.
The Protein Pattern in Different Epididymal Regions
- The study revealed a differentiation in the protein pattern across the epididymis, identifying three main secretory regions: E0-E2, E3-E5, and E6-E9.
- In region E0-E2, clusterin (53%), PGDS (44%), and GPX (6%) were the defining secreted proteins.
- Region E3-E5 was identified as having the greatest number of secreted proteins, the highest protein concentrations, and the highest spermatocrit value. Notably, the most abundant proteins in this region included lactoferrin, clusterin, hexosaminidase, and procathepsin D.
- The final region, E6-E9, which had few region-specific secreted compounds, was characterized by a high quantity of lactoferrin in the luminal fluid.
Behavior of Major Proteins
- By comparing the secretion and concentration of the major proteins across the organ, the study revealed protein-specific behavior patterns. This was particularly evident for the three isoforms of clusterin.
Cite This Article
APA
Fouchécourt S, Métayer S, Locatelli A, Dacheux F, Dacheux JL.
(2000).
Stallion epididymal fluid proteome: qualitative and quantitative characterization; secretion and dynamic changes of major proteins.
Biol Reprod, 62(6), 1790-1803.
https://doi.org/10.1095/biolreprod62.6.1790 Publication
Researcher Affiliations
- Station de Physiologie de la Reproduction des Mammifères Domestiques, URA INRA-CNRS 1291, 37380 Nouzilly, France.
MeSH Terms
- Amino Acid Sequence
- Animals
- Body Fluids / chemistry
- Carrier Proteins
- Cathepsin D / analysis
- Cathepsin D / chemistry
- Cathepsin D / metabolism
- Clusterin
- Electrophoresis, Gel, Two-Dimensional
- Epididymis / anatomy & histology
- Epididymis / metabolism
- Epithelium / metabolism
- Glutathione Peroxidase / analysis
- Glutathione Peroxidase / chemistry
- Glutathione Peroxidase / metabolism
- Glycoproteins / analysis
- Glycoproteins / chemistry
- Glycoproteins / metabolism
- Horses / anatomy & histology
- Horses / metabolism
- Intramolecular Oxidoreductases / analysis
- Intramolecular Oxidoreductases / metabolism
- Lactoferrin / analysis
- Lactoferrin / metabolism
- Lipocalins
- Male
- Molecular Chaperones
- Molecular Sequence Data
- Proteins / analysis
- Proteins / metabolism
- Proteome
- Sequence Analysis, Protein
- Sperm Count
- Vesicular Transport Proteins
- beta-N-Acetylhexosaminidases / analysis
- beta-N-Acetylhexosaminidases / chemistry
- beta-N-Acetylhexosaminidases / metabolism
Citations
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