• 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Journal of Cellular Physiology >Synergistic actions of a thrombin-derived synthetic peptide and a thrombin receptor-activating peptide in stimulating fibroblast mitogenesis.
【24h】

Synergistic actions of a thrombin-derived synthetic peptide and a thrombin receptor-activating peptide in stimulating fibroblast mitogenesis.

机译：thrombin-derived的协同行动合成肽,凝血酶receptor-activating肽在刺激纤维原细胞有丝分裂发生。

获取原文
获取原文并翻译 | 示例
           
页面导航
  • 摘要
  • 著录项
  • 相似文献
  • 相关主题

摘要

We measured the ability of the thrombin receptor activating peptide, SFLLR-NH2 (P5A) to stimulate 3H-thymidine incorporation in hamster CCL-39 fibroblasts either alone or in combination with the thrombin-derived polypeptides, YPPWNKNFTENDLL (TDP-1) and AGYKPDEGKRGDACEGDSGGPFV (TDP-2). In the presence (but not absence) of the amino peptidase inhibitor amastatin (10 microM), P5A alone (7.5 to 100 microM) caused a 1.5- to 2-fold stimulation of thymidine incorporation above basal, even though this inhibitor did not abrogate the degradation of P5A by other peptidases present in the assay medium. Neither TDP-1 nor TDP-2 alone had any effect on thymidine incorporation. However, TDP-1 (30 to 90 microM) considerably augmented P5A-mediated thymidine incorporation at low P5A concentrations (7.5 to 30 microM), shifting the P5A concentration-effect curve to the left. TDP-2 was inactive in this regard. The EC50 for this potentiating action of TDP-1 was approximately 40 microM. Further, thrombin, rendered proteolytically inactive by a low-molecular-weight bifunctional inhibitor, hirutonin-6, also acted synergistically with P5A to stimulate CCL-39 cell thymidine incorporation. We hypothesize that thrombin can cause its cellular effects, such as thymidine incorporation, not only via the proteolytic activation of its G-protein-coupled receptor, but also via the concurrent and synergistic interaction of its TDP-1 peptide domain with a separate cell surface docking site.
机译：我们测量了凝血酶受体的能力激活肽,SFLLR-NH2 (P5A)刺激3在仓鼠CCL-39 h-thymidine公司成纤维细胞单独或结合YPPWNKNFTENDLL thrombin-derived多肽(TDP-1)和AGYKPDEGKRGDACEGDSGGPFV (TDP-2)。氨基酸的存在(但不是没有)肽酶抑制剂amastatin (10 microM), P5A独自一人(7.5至100 microM)引起了1.5 - 2倍刺激胸腺嘧啶核苷掺入基底,尽管这抑制剂没有废除P5A的退化肽酶存在于试验介质。对胸苷TDP-1也独自TDP-2有任何影响合并。大大增强P5A-mediated胸苷合并P5A浓度较低(7.530 microM),将P5A浓度效应曲线向左。把。TDP-1大约是40 microM。由凝血酶,使proteolytically无所作为低分子量双官能团的抑制剂,hirutonin-6,还与P5A协同行动刺激CCL-39细胞胸腺嘧啶核苷掺入。我们假设凝血酶可以使其细胞的影响,如胸苷公司不仅通过蛋白水解G-protein-coupled受体的激活,但是也通过并行和协同交互的TDP-1肽领域了单独的细胞表面对接网站。

著录项

相似文献

  • 外文文献
  • 中文文献
获取原文

客服邮箱：kefu@zhangqiaokeyan.com

京公网安备：11010802029741号 ICP备案号：京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有

  • 客服微信

  • 服务号