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1.
Biol. Res ; 44(2): 119-124, 2011. ilus
Article in English | LILACS | ID: lil-602966

ABSTRACT

The current knowledge about teleost fish egg envelope is summarized. The paper analyzes the organization and deposition process of the protein composition and genes involved in the synthesis of teleost fish egg envelopes and their role in gamete interaction during fertilization. Pelagic and demersal species that our research group is working with are especially considered. The vertebrate ZP family of proteins, the evolution and relationship among the different genes and their expression are taken into account. We consider fish envelope as a possible biomonitor for ecological contaminants. The biotechnological applications for aquaculture and genomic and post-genomic approaches are auspicious.


Subject(s)
Animals , Female , Male , Egg Proteins/analysis , Fishes/physiology , Sperm-Ovum Interactions/physiology , Biomarkers/analysis , Environmental Monitoring , Egg Proteins/genetics , Egg Proteins/ultrastructure , Fishes/genetics , Microscopy, Electron, Transmission , Sperm-Ovum Interactions/genetics
2.
Article in English | IMSEAR | ID: sea-135861

ABSTRACT

Background & objectives: An inability or decreased ability of spermatozoa to bind to the zona pellucida (ZP), an extracellular glycoproteinaceous matrix surrounding egg, is one of the plausible causes of idiopathic infertility. It will be clinically useful to distinguish this condition from other causes of infertility. An assay system, investigating binding of human sperm with ZP glycoprotein may prove useful in this regard. We attempted to develop a simple assay system to analyse the binding of capacitated human spermatozoa to human zona pellucida glycoprotein-3 (ZP3) using baculovirus-expressed recombinant human ZP3 coated beads. Methods: Recombinant baculovirus-expressed ZP3 was purified, labelled with biotin and coated on streptavidin sepharose beads. An in vitro assay system was optimized to study binding of capacitated human sperm to ZP3 coated beads. Results: A higher percentage of baculovirus-expressed recombinant human ZP3 coated beads showed significant (P<0.05) binding of capacitated human sperm as compared to beads coated with fetuin. An inhibition in the binding of sperm to ZP3 coated beads was observed in presence of cold recombinant human ZP3. Further, prior incubation of ZP3 coated beads with monoclonal antibodies (MAbs) against ZP3 but not against ZP2 resulted in the decrease in number of sperm bound to bead. Interpretation & conclusion: An in vitro assay system to study the binding of human sperm to ZP3- primary sperm receptor was established, which may be useful to determine the functional competence of spermatozoa.


Subject(s)
Egg Proteins/genetics , Egg Proteins/metabolism , Humans , Male , Membrane Glycoproteins/genetics , Membrane Glycoproteins/metabolism , Protein Binding , Receptors, Cell Surface/genetics , Receptors, Cell Surface/metabolism , Recombinant Fusion Proteins/genetics , Recombinant Fusion Proteins/metabolism , Sperm Capacitation/physiology , Spermatozoa/cytology , Spermatozoa/metabolism , Zona Pellucida/metabolism , alpha-Fetoproteins/metabolism
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