Comparative protein profiles: potential molecular markers from spermatozoa of Acipenseriformes (Chondrostei, Pisces)
Language English Country Netherlands Media print
Document type Comparative Study, Journal Article, Research Support, Non-U.S. Gov't
PubMed
20869341
DOI
10.1016/j.cbd.2010.08.003
PII: S1744-117X(10)00076-6
Knihovny.cz E-resources
- MeSH
- Electrophoresis, Gel, Two-Dimensional methods MeSH
- Fructose-Bisphosphate Aldolase genetics metabolism MeSH
- Biomarkers metabolism MeSH
- Species Specificity MeSH
- Phosphoglycerate Kinase genetics metabolism MeSH
- Phosphopyruvate Hydratase genetics metabolism MeSH
- Glycerolphosphate Dehydrogenase genetics metabolism MeSH
- Isoelectric Focusing methods MeSH
- Isoenzymes genetics metabolism MeSH
- Peptide Mapping methods MeSH
- Peptides genetics metabolism MeSH
- Proteomics methods MeSH
- Fishes classification genetics metabolism MeSH
- Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization methods MeSH
- Spermatozoa metabolism MeSH
- Animals MeSH
- Check Tag
- Male MeSH
- Animals MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Comparative Study MeSH
- Geographicals
- Mississippi MeSH
- Siberia MeSH
- Names of Substances
- Fructose-Bisphosphate Aldolase MeSH
- Biomarkers MeSH
- Phosphoglycerate Kinase MeSH
- Phosphopyruvate Hydratase MeSH
- Glycerolphosphate Dehydrogenase MeSH
- Isoenzymes MeSH
- Peptides MeSH
Sturgeon and paddlefish (Acipenseriformes), the source of roe consumed as caviar, are a unique and commercially valuable group of ancient fishes. In this study, comparative proteomics was used to analyze protein profiles of spermatozoa from five sturgeon species and one paddlefish: Siberian sturgeon (Acipenser baerii), sterlet (A. ruthenus), Russian sturgeon (A. gueldenstaedtii), starry sturgeon (A. stellatus), beluga (Huso huso), and Mississippi paddlefish (Polyodon spathula). Protein profiles of spermatozoa were determined by isoelectric focusing and two-dimensional electrophoresis (2-DE) high-resolution gels. The peptides, previously selected by 2-DE analysis as potentially species-specific, were obtained by "in-gel" tryptic digestion, followed by matrix-associated laser desorption/ionization time-of-flight/mass spectrometry (MALDI-TOF/MS). Among the 23 protein spots selected, 14 were identified as isoforms of enolase B present in all species, but with different isoelectric points or molecular mass. Exceptions were A. ruthenus and H. huso, species with a close phylogenetic relationship. Glycerol-3-phosphate dehydrogenase was detected exclusively in P. spathula. Phosphoglycerate kinase was detected only in A. ruthenus and H. huso, and 3 additional proteins (fructose bisphosphate aldolase A-2, glycogen phosphorylase type IV and glyceraldehyde-3-phosphate dehydrogenase) were found exclusively in A. gueldenstaedtii and H. huso. This study points to the application of proteomics for differential characterization and comparative studies of acipenseriform species at the molecular level.
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