Lectin binding sites on the plasma membranes of Orthoptera Tettigonioidea spermatodesms. 2020

Roberta Pecoraro, and Maria Elena Scalisi, and Maria Violetta Brundo
Department of Biological, Geological and Environmental Science, University of Catania, Catania, Italy.

In many Vertebrate and invertebrate, the interaction mechanisms among gametes are based on a high affinity and specificity of recognition and link between specific saccharidic residues and receptors present on the surface of gametes. Literature data also suggest that Insects could use this strategy. In particular, Orthoptera Tettigoniidae spermatodesms and sperms undergo radical changes passing through the male to the female genital tracts that may be interpreted as well as a capacitation process. These changes could also concern the presence and distribution of surface glycoconjugates. Our study aims to highlight the presence and distribution of saccharide residues on the spermatozoa surface in five species of Orthoptera Tettigoniidae using a battery of lectins Fluorescein Isothiocyanate Conjugated and Gold Conjugated. The results of this investigation have shown that on the surface of the male gametes are present saccharide residues whose nature and distribution are species-specific, during their transfer to the female genital tract, they significantly undergo a change. These results let us hypothesize that also for this group of Insects, the glycoconjugates play a significant role in the process of interaction between gametes.

UI MeSH Term Description Entries
D008297 Male Males
D009987 Orthoptera An order of insects comprising two suborders: Caelifera and Ensifera. They consist of GRASSHOPPERS, locusts, and crickets (GRYLLIDAE). Caelifera,Ensifera,Caeliferas,Ensiferas,Orthopteras
D002462 Cell Membrane The lipid- and protein-containing, selectively permeable membrane that surrounds the cytoplasm in prokaryotic and eukaryotic cells. Plasma Membrane,Cytoplasmic Membrane,Cell Membranes,Cytoplasmic Membranes,Membrane, Cell,Membrane, Cytoplasmic,Membrane, Plasma,Membranes, Cell,Membranes, Cytoplasmic,Membranes, Plasma,Plasma Membranes
D005260 Female Females
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D001665 Binding Sites The parts of a macromolecule that directly participate in its specific combination with another molecule. Combining Site,Binding Site,Combining Sites,Site, Binding,Site, Combining,Sites, Binding,Sites, Combining
D013094 Spermatozoa Mature male germ cells derived from SPERMATIDS. As spermatids move toward the lumen of the SEMINIFEROUS TUBULES, they undergo extensive structural changes including the loss of cytoplasm, condensation of CHROMATIN into the SPERM HEAD, formation of the ACROSOME cap, the SPERM MIDPIECE and the SPERM TAIL that provides motility. Sperm,Spermatozoon,X-Bearing Sperm,X-Chromosome-Bearing Sperm,Y-Bearing Sperm,Y-Chromosome-Bearing Sperm,Sperm, X-Bearing,Sperm, X-Chromosome-Bearing,Sperm, Y-Bearing,Sperm, Y-Chromosome-Bearing,Sperms, X-Bearing,Sperms, X-Chromosome-Bearing,Sperms, Y-Bearing,Sperms, Y-Chromosome-Bearing,X Bearing Sperm,X Chromosome Bearing Sperm,X-Bearing Sperms,X-Chromosome-Bearing Sperms,Y Bearing Sperm,Y Chromosome Bearing Sperm,Y-Bearing Sperms,Y-Chromosome-Bearing Sperms
D037102 Lectins Proteins that share the common characteristic of binding to carbohydrates. Some ANTIBODIES and carbohydrate-metabolizing proteins (ENZYMES) also bind to carbohydrates, however they are not considered lectins. PLANT LECTINS are carbohydrate-binding proteins that have been primarily identified by their hemagglutinating activity (HEMAGGLUTININS). However, a variety of lectins occur in animal species where they serve diverse array of functions through specific carbohydrate recognition. Animal Lectin,Animal Lectins,Isolectins,Lectin,Isolectin,Lectin, Animal,Lectins, Animal

Related Publications

Roberta Pecoraro, and Maria Elena Scalisi, and Maria Violetta Brundo
August 1975, The Journal of cell biology,
Roberta Pecoraro, and Maria Elena Scalisi, and Maria Violetta Brundo
August 1998, Tissue & cell,
Roberta Pecoraro, and Maria Elena Scalisi, and Maria Violetta Brundo
December 1999, The Journal of biological chemistry,
Roberta Pecoraro, and Maria Elena Scalisi, and Maria Violetta Brundo
January 1984, Histochemistry,
Roberta Pecoraro, and Maria Elena Scalisi, and Maria Violetta Brundo
June 1993, The Histochemical journal,
Roberta Pecoraro, and Maria Elena Scalisi, and Maria Violetta Brundo
January 2000, Folia biologica,
Roberta Pecoraro, and Maria Elena Scalisi, and Maria Violetta Brundo
January 2007, Zhurnal evoliutsionnoi biokhimii i fiziologii,
Roberta Pecoraro, and Maria Elena Scalisi, and Maria Violetta Brundo
September 1977, The Journal of cell biology,
Roberta Pecoraro, and Maria Elena Scalisi, and Maria Violetta Brundo
January 1984, General pharmacology,
Roberta Pecoraro, and Maria Elena Scalisi, and Maria Violetta Brundo
January 1994, Ukrainskii biokhimicheskii zhurnal (1978),
Copied contents to your clipboard!