Immunoelectophoretic Identification of Jelly Coat Ligands Bound by the Cortical Granule Lectin from Xenopus laevis Eggs. (anuran fertilization/egg jelly/lectin/Xenopus laevis/immunoelectrophoresis)

1992 ◽  
Vol 34 (1) ◽  
pp. 91-98 ◽  
Author(s):  
Cynthia A. Birr ◽  
Jerry L. Hedrick
2000 ◽  
Vol 352 (2) ◽  
pp. 449-463 ◽  
Author(s):  
Yann GUERARDEL ◽  
Ossarath KOL ◽  
Emmanuel MAES ◽  
Tony LEFEBVRE ◽  
Bénoni BOILLY ◽  
...  

Eggs from Xenopus laevis are surrounded by several layers of jelly that are needed for proper fertilization. Jelly coat is composed of high-molecular-mass glycoconjugates to which are bound many globular proteins. O-glycans released from the jelly coat of X. laevis have been partially described in previous studies. In this study, we compared the glycosylation pattern of the egg jelly coat isolated from six specimens of X. laevis. The O-glycans were released from jelly coats by alkali/borohydride treatment. Structural characterization was performed through a combination of one- and two-dimensional 1H-NMR and methylation analysis. This allowed the description of a new family of sulphated O-glycans present in jelly coats of all X. laevis. However, the jelly O-glycans showed a low extent of polymorphism between specimens. This intra-specific variability was restricted to the terminal substitution of O-linked oligosaccharides. The differential expression of two glycosyltransferase [an α-(1 → 4) galactosyltransferase and an α-(1 → 3) fucosyltransferase] activities resulted in the characterization of four phenotypes of X. laevis. Furthermore, electrophoretic analysis suggested that the high-molecular-mass fraction of jelly coat was mostly composed of mucin-type glycoproteins. Blot analysis with lectins confirmed that the glycan variability was borne by these mucin-type components. However, fertilization assays suggested that the glycan polymorphism had no repercussion on egg fertilizability.


Biochemistry ◽  
1975 ◽  
Vol 14 (14) ◽  
pp. 3101-3107 ◽  
Author(s):  
Edward C. Yurewicz ◽  
Gene Oliphant ◽  
Jerry L. Hedrick

2000 ◽  
Vol 352 (2) ◽  
pp. 449 ◽  
Author(s):  
Yann GUERARDEL ◽  
Ossarath KOL ◽  
Emmanuel MAES ◽  
Tony LEFEBVRE ◽  
Bénoni BOILLY ◽  
...  
Keyword(s):  

2006 ◽  
Vol 52 (1) ◽  
pp. 113-120 ◽  
Author(s):  
Andrea N. Edginton ◽  
Claude Rouleau ◽  
Gerald R. Stephenson ◽  
Herman J. Boermans

1990 ◽  
Vol 1 (3) ◽  
pp. 315-326 ◽  
Author(s):  
W M Bement ◽  
D G Capco

Transit into interphase of the first mitotic cell cycle in amphibian eggs is a process referred to as activation and is accompanied by an increase in intracellular free calcium [( Ca2+]i), which may be transduced into cytoplasmic events characteristic of interphase by protein kinase C (PKC). To investigate the respective roles of [Ca2+]i and PKC in Xenopus laevis egg activation, the calcium signal was blocked by microinjection of the calcium chelator BAPTA, or the activity of PKC was blocked by PKC inhibitors sphingosine or H7. Eggs were then challenged for activation by treatment with either calcium ionophore A23187 or the PKC activator PMA. BAPTA prevented cortical contraction, cortical granule exocytosis, and cleavage furrow formation in eggs challenged with A23187 but not with PMA. In contrast, sphingosine and H7 inhibited cortical granule exocytosis, cortical contraction, and cleavage furrow formation in eggs challenged with either A23187 or PMA. Measurement of egg [Ca2+]i with calcium-sensitive electrodes demonstrated that PMA treatment does not increase egg [Ca2+]i in BAPTA-injected eggs. Further, PMA does not increase [Ca2+]i in eggs that have not been injected with BAPTA. These results show that PKC acts downstream of the [Ca2+]i increase to induce cytoplasmic events of the first Xenopus mitotic cell cycle.


1990 ◽  
Vol 105 (1-3) ◽  
pp. 123-132 ◽  
Author(s):  
Barry Bonnell ◽  
Douglas Chandler

2008 ◽  
Vol 231 (2) ◽  
pp. 434-439
Author(s):  
Yves Plancke ◽  
Jean-Michel Wieruszeski ◽  
Catherine Alonso ◽  
Benoni Boilly ◽  
Gérard Strecker
Keyword(s):  

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