The role of the egg jelly coat in protectingHyla regilla andBufo canorus embryos from ultraviolet B radiation during development

2002 ◽  
Vol 9 (6) ◽  
pp. 412-416 ◽  
Author(s):  
Lara J. Hansen ◽  
David L. Fabacher ◽  
Robin Calfee
FEBS Letters ◽  
2003 ◽  
Vol 540 (1-3) ◽  
pp. 125-132 ◽  
Author(s):  
Zerihun Assefa ◽  
Marjan Garmyn ◽  
Annelies Vantieghem ◽  
Wim Declercq ◽  
Peter Vandenabeele ◽  
...  

Zygote ◽  
1996 ◽  
Vol 4 (3) ◽  
pp. 237-245 ◽  
Author(s):  
Takuya Nishigaki ◽  
Kazuyoshi Chiba ◽  
Wataru Miki ◽  
Motonori Hoshi

SummaryJelly coat of starfish eggs has the capacity to activate homologous spermatozoa and induce the acrosome reaction. We have isolated 12 sperm-activating peptides (SAPs) from the egg jelly of the starfish, Asterias amurensis. Eleven SAPs were structurally identified by sequence analysis and electro-spray ionisation mass spectrometry. All of them are glutamine-rich tetratriacontapeptides with an intramolecular disulphide linkage between Cys8 and Cys32. They are much larger than sea urchin SAPs and do not show any significant sequence similarities to known proteins. Thus we have collectively named them asterosaps. The amino terminal region, where structural diversity of asterosaps is observed, is not important for their activity, whereas the disulphide linkage is essential. Asterosaps do not induce the acrosome reaction by themselves, but are able to induce the acrosome reaction in combination with an egg jelly glycoconjugate named ARIS. Furthermore, anti-asterosap rabbit antibody significantly decreased the acrosome reaction-inducing activity of the jelly solution and the activity was restored by addition of excess asterosap. These results support our hypothesis that the main physiological role of SAPs is the induction of the acrosome reaction in cooperation with two other jelly components, ARIS and Co-ARIS.


2010 ◽  
Vol 33 (1) ◽  
pp. 156-167 ◽  
Author(s):  
Bothina L. Mahmoud ◽  
Abeer M. Shady ◽  
Usama A. G. El Meleegy ◽  
Mona A. Soliman

2011 ◽  
Vol 49 (3) ◽  
pp. 284-292 ◽  
Author(s):  
Mikael Ristilä ◽  
Hilja Strid ◽  
Leif A. Eriksson ◽  
Åke Strid ◽  
Helena Sävenstrand

2021 ◽  
Author(s):  
Cosme Marcos Moreno

Abstract Catalase under ultraviolet-B radiation (CATUVB) produces reactive oxygen species (ROS), but the role of that surprising photoactivity in CAT still remains uncertain. On the other hand, it is well-known that CAT breaking down a steady source of hydrogen peroxide (H2O2) becomes inactive due to compound II formation (CII), which results in typical changes in its absorption spectrum. On the basis of CII formation, here I show first that CATUVB produces and breaks down H2O2, via which UVB is converted into heat. I then show that CATUVB thermogenesis accelerates the ice melting and warms the medium. From data to nature, CAT converting harmful UVB into advantageous heat in microorganisms would be responsible for a hidden biogeochemical thermogenesis process under the ozone layer control with effects on sea ice melting and sea surface warming in cold regions.


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