Comparative protein profiles: potential molecular markers from spermatozoa of Acipenseriformes (Chondrostei, Pisces).
Identifieur interne : 000374 ( PubMed/Curation ); précédent : 000373; suivant : 000375Comparative protein profiles: potential molecular markers from spermatozoa of Acipenseriformes (Chondrostei, Pisces).
Auteurs : Ping Li [République tchèque] ; Martin Hulak ; Marek Rodina ; Miroslav Sulc ; Zhi-Hua Li ; Otomar LinhartSource :
- Comparative biochemistry and physiology. Part D, Genomics & proteomics [ 1878-0407 ] ; 2010.
English descriptors
- KwdEn :
- Animals, Biomarkers (metabolism), Electrophoresis, Gel, Two-Dimensional (methods), Fishes (classification), Fishes (genetics), Fishes (metabolism), Fructose-Bisphosphate Aldolase (genetics), Fructose-Bisphosphate Aldolase (metabolism), Glycerolphosphate Dehydrogenase (genetics), Glycerolphosphate Dehydrogenase (metabolism), Isoelectric Focusing (methods), Isoenzymes (genetics), Isoenzymes (metabolism), Male, Mississippi, Peptide Mapping (methods), Peptides (genetics), Peptides (metabolism), Phosphoglycerate Kinase (genetics), Phosphoglycerate Kinase (metabolism), Phosphopyruvate Hydratase (genetics), Phosphopyruvate Hydratase (metabolism), Proteomics (methods), Siberia, Species Specificity, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization (methods), Spermatozoa (metabolism).
- MESH :
- chemical , genetics : Fructose-Bisphosphate Aldolase, Glycerolphosphate Dehydrogenase, Isoenzymes, Peptides, Phosphoglycerate Kinase, Phosphopyruvate Hydratase.
- chemical , metabolism : Biomarkers, Fructose-Bisphosphate Aldolase, Glycerolphosphate Dehydrogenase, Isoenzymes, Peptides, Phosphoglycerate Kinase, Phosphopyruvate Hydratase.
- geographic : Mississippi, Siberia.
- classification : Fishes.
- genetics : Fishes.
- metabolism : Fishes, Spermatozoa.
- methods : Electrophoresis, Gel, Two-Dimensional, Isoelectric Focusing, Peptide Mapping, Proteomics, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization.
- Animals, Male, Species Specificity.
Abstract
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.
DOI: 10.1016/j.cbd.2010.08.003
PubMed: 20869341
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pubmed:20869341Le document en format XML
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<front><div type="abstract" xml:lang="en">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.</div>
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<Abstract><AbstractText>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.</AbstractText>
<CopyrightInformation>Copyright © 2010 Elsevier Inc. All rights reserved.</CopyrightInformation>
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