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A novel disintegrin, jerdonatin, inhibits platelet aggregation and sperm-egg binding
Xing-Ding Zhou1, Chen-Hui Ding, Hong Tai
1Department of Animal Toxinology, Kunming Institute of Zoology, The Chinese Academy of Sciences, No. 32 Jiaochangdonglu, Kunming 650223, Yunnan, PR China.
Summary
A novel disintegrin, jerdonatin, from snake venom inhibits human platelet aggregation and sperm-egg binding. This suggests egg integrins play a role in mammalian fertilization processes.
Area of Science:
- Biochemistry
- Molecular Biology
- Reproductive Biology
Background:
- Disintegrins are a class of proteins known for their role in cell adhesion.
- Snake venom is a rich source of bioactive molecules with diverse pharmacological properties.
Purpose of the Study:
- To isolate and characterize a novel disintegrin, jerdonatin, from Trimeresurus jerdonii venom.
- To investigate the effects of jerdonatin on platelet aggregation and sperm-egg interactions.
Main Methods:
- Purification of jerdonatin using gel filtration and reversed-phase high-pressure liquid chromatography.
- Isolation of the encoding cDNA from snake venom gland.
- Determination of molecular mass using MALDI-TOF-MS.
- Assays for platelet aggregation inhibition and sperm-egg binding/fusion.
Main Results:
- Jerdonatin, a 72-amino acid protein with an RGD motif, was purified and characterized.
- Jerdonatin significantly inhibited ADP- and collagen-induced human platelet aggregation.
- Jerdonatin concentration-dependently inhibited sperm-egg binding but not fusion in mice.
Conclusions:
- Jerdonatin exhibits potent anti-platelet aggregation activity.
- Jerdonatin's inhibition of sperm-egg binding suggests a role for egg integrins in mammalian fertilization.
- This study identifies jerdonatin as a potential tool for studying fertilization mechanisms.