 |
论文 |
|
|
 |
| 论文编号: |
|
| 论文题目: |
YY-39, a tick anti-thrombosis peptide containing RGD domain |
| 作者: |
Jing Tang; Yaqun Fang; Yajun Han; Xuewei Bai; Xiuwen Yan; Yun Zhang; Ren Lai*; Zhiye Zhang* |
| 联系作者: |
zhangzhiye5225@163.com;rlai@mail.kiz.ac.cn |
| 外单位作者单位: |
|
| 发表年度: |
2015 |
| 卷: |
68 |
| 期: |
X |
| 页码: |
99-104 |
| 摘要: |
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. |
| 刊物名称: |
Peptides |
| 论文全文: |
点击查看 |
| 全文链接: |
点击下载 |
| Email:: |
|
| 学科: |
|
| 影响因子: |
2.618 (2014) |
| 第一作者所在部门: |
|
| 论文出处: |
|
| 论文类别: |
|
| 参与作者: |
|
|
|
