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The envelopes of amphibian oocytes: physiological modifications in Bufo arenarum

A characterization of the Amphibian Bufo arenarum oocyte envelope is presented. It was made in different functional conditions of the oocyte: 1) when it has been released into the coelomic cavity during ovulation (surrounded by the coelomic envelope, (CE), 2) after it has passed through the oviduct...

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Autores principales: Barisone, Gustavo A, Albertali, Isabel E, Sánchez, Mercedes, Cabada, Marcelo O
Formato: Texto
Lenguaje:English
Publicado: BioMed Central 2003
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC153491/
https://www.ncbi.nlm.nih.gov/pubmed/12694627
http://dx.doi.org/10.1186/1477-7827-1-18
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author Barisone, Gustavo A
Albertali, Isabel E
Sánchez, Mercedes
Cabada, Marcelo O
author_facet Barisone, Gustavo A
Albertali, Isabel E
Sánchez, Mercedes
Cabada, Marcelo O
author_sort Barisone, Gustavo A
collection PubMed
description A characterization of the Amphibian Bufo arenarum oocyte envelope is presented. It was made in different functional conditions of the oocyte: 1) when it has been released into the coelomic cavity during ovulation (surrounded by the coelomic envelope, (CE), 2) after it has passed through the oviduct and is deposed (surrounded by the viteline envelope, (VE), and 3) after oocyte activation (surrounded by the fertilization envelope, (FE). The characterization was made by SDS-PAGE followed by staining for protein and glycoproteins. Labeled lectins were used to identify glycosidic residues both in separated components on nitrocellulose membranes or in intact oocytes and embryos. Proteolytic properties of the content of the cortical granules were also analyzed. After SDS-PAGE of CE and VE, a different protein pattern was observed. This is probably due to the activity of a protease present in the pars recta of the oviduct. Comparison of the SDS-PAGE pattern of VE and FE showed a different mobility for one of the glycoproteins, gp75. VE and FE proved to have different sugar residues in their oligosaccharide chains. Mannose residues are only present in gp120 of the three envelopes. N-acetyl-galactosamine residues are present in all of the components, except for gp69 in the FE. Galactose residues are present mainly in gp120 of FE. Lectin-binding assays indicate the presence of glucosamine, galactose and N-acetyl galactosamine residues and the absence (or non-availability) of N-acetyl-glucosamine or fucose residues on the envelopes surface. The cortical granule product (CGP) shows proteolytic activity on gp75 of the VE.
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spelling pubmed-1534912003-04-19 The envelopes of amphibian oocytes: physiological modifications in Bufo arenarum Barisone, Gustavo A Albertali, Isabel E Sánchez, Mercedes Cabada, Marcelo O Reprod Biol Endocrinol Research A characterization of the Amphibian Bufo arenarum oocyte envelope is presented. It was made in different functional conditions of the oocyte: 1) when it has been released into the coelomic cavity during ovulation (surrounded by the coelomic envelope, (CE), 2) after it has passed through the oviduct and is deposed (surrounded by the viteline envelope, (VE), and 3) after oocyte activation (surrounded by the fertilization envelope, (FE). The characterization was made by SDS-PAGE followed by staining for protein and glycoproteins. Labeled lectins were used to identify glycosidic residues both in separated components on nitrocellulose membranes or in intact oocytes and embryos. Proteolytic properties of the content of the cortical granules were also analyzed. After SDS-PAGE of CE and VE, a different protein pattern was observed. This is probably due to the activity of a protease present in the pars recta of the oviduct. Comparison of the SDS-PAGE pattern of VE and FE showed a different mobility for one of the glycoproteins, gp75. VE and FE proved to have different sugar residues in their oligosaccharide chains. Mannose residues are only present in gp120 of the three envelopes. N-acetyl-galactosamine residues are present in all of the components, except for gp69 in the FE. Galactose residues are present mainly in gp120 of FE. Lectin-binding assays indicate the presence of glucosamine, galactose and N-acetyl galactosamine residues and the absence (or non-availability) of N-acetyl-glucosamine or fucose residues on the envelopes surface. The cortical granule product (CGP) shows proteolytic activity on gp75 of the VE. BioMed Central 2003-02-11 /pmc/articles/PMC153491/ /pubmed/12694627 http://dx.doi.org/10.1186/1477-7827-1-18 Text en Copyright © 2003 Barisone et al; licensee BioMed Central Ltd. This is an Open Access article: verbatim copying and redistribution of this article are permitted in all media for any purpose, provided this notice is preserved along with the article's original URL.
spellingShingle Research
Barisone, Gustavo A
Albertali, Isabel E
Sánchez, Mercedes
Cabada, Marcelo O
The envelopes of amphibian oocytes: physiological modifications in Bufo arenarum
title The envelopes of amphibian oocytes: physiological modifications in Bufo arenarum
title_full The envelopes of amphibian oocytes: physiological modifications in Bufo arenarum
title_fullStr The envelopes of amphibian oocytes: physiological modifications in Bufo arenarum
title_full_unstemmed The envelopes of amphibian oocytes: physiological modifications in Bufo arenarum
title_short The envelopes of amphibian oocytes: physiological modifications in Bufo arenarum
title_sort envelopes of amphibian oocytes: physiological modifications in bufo arenarum
topic Research
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC153491/
https://www.ncbi.nlm.nih.gov/pubmed/12694627
http://dx.doi.org/10.1186/1477-7827-1-18
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