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Published on: May 11, 2017
The morphological and molecular susceptibility of sheep and mouse zona pellucida to acrosin
Abstract:
The effect of acrosin on the gross morphology and macromolecular constituents of the mouse and sheep zona pellucida has been examined by light microscopy and SDS-PAGE following labelling of the zona with 125I. Ram and boar acrosin had similar effects on the sheep zona in that while there was no discernible alteration in the gross morphology of the investment it was proteolysed to the same limited extent by both enzymes; during 1 h major polypeptides of Mr 180,000 (present on the zona pellucida of eggs but absent from that of oocytes) and 80,000 were hydrolysed, giving rise to polypeptides of Mr 68,000, 54,000 and 46,000, of which the last accumulated and represented the lowest molecular weight hydrolysis product. By contrast, the mouse zona pellucida was completely dissolved from the egg by ram acrosin and the investment's macromolecules were extensively hydrolysed.
Insights
Acrosin, an enzyme, differentially affects the zona pellucida (egg
Area of Science:
- Reproductive Biology
- Enzymology
- Proteomics
Background:
- The zona pellucida is a crucial glycoprotein layer surrounding mammalian oocytes.
- Acrosin, a serine protease, is released during the acrosome reaction and plays a role in fertilization.
Purpose of the Study:
- To investigate the differential effects of ram and boar acrosin on the mouse and sheep zona pellucida.
- To analyze the proteolysis of zona pellucida macromolecules by acrosin.
Main Methods:
- Zona pellucida labeling with Iodine-125.
- Analysis of macromolecular constituents using SDS-PAGE.
- Microscopic examination of gross morphology.
Main Results:
- Ram and boar acrosin partially hydrolyzed sheep zona pellucida polypeptides (180,000 and 80,000 Mr) into smaller fragments (68,000, 54,000, and 46,000 Mr).
- Ram acrosin completely dissolved the mouse zona pellucida and extensively hydrolyzed its macromolecules.
- Specific polypeptides (180,000 and 80,000 Mr) were identified as targets for acrosin hydrolysis.
Conclusions:
- Acrosin exhibits species-specific differences in its lytic activity on the zona pellucida.
- The differential hydrolysis of zona pellucida components by acrosin may have implications for species-specific fertilization barriers.
