YY-39, a tick anti-thrombosis peptide containing RGD domain
Peptides, ISSN: 0196-9781, Vol: 68, Page: 99-104
2015
- 25Citations
- 22Captures
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Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
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Metrics Details
- Citations25
- Citation Indexes25
- 25
- CrossRef19
- Captures22
- Readers22
- 22
Article Description
Ticks are obligatory blood feeding ectoparasites, which continuously attach to their hosts for 1–2 weeks. There are many biologically active compounds in tick salivary glands interfering host haemostatic system and to successfully obtain blood meal. Several platelet aggregation inhibitors have been identified from ticks. A family of conserved peptides, which were identified from transcriptome analysis of many tick salivary glands, were found to contain unique primary structure including predicted mature peptides of 39–47 amino acid residues in length and a Pro/Glu(P/E)-Pro/His(P/H)-Lys-Gly-Asp(RGD) domain. Given their unique structure and RGD domain, they are considered a novel family of disintegrins that inhibit platelet aggregation. One of them (YY-39) was tested for its effects on platelets and thrombosis in vivo. YY-39 was found effectively to inhibit platelet aggregation induced by adenosine diphosphate (ADP), thrombin and thromboxane A 2 (TXA2). Furthermore, YY-39 blocked platelet adhesion to soluble collagen and bound to purified GPIIb/IIIa in a dose-dependent manner. In in vivo experiments, YY-39 reduced thrombus weight effectively in a rat arteriovenous shunt model and inhibited thrombosis in a carrageenan-induced mouse tail thrombosis model. Combined with their prevalence in ticks and platelet inhibitory functions, this family of peptides might be conserved tick anti-haemostatic molecules.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/S0196978114002514; http://dx.doi.org/10.1016/j.peptides.2014.08.008; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=84929318216&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/25152502; https://linkinghub.elsevier.com/retrieve/pii/S0196978114002514
Elsevier BV
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