Cloning of bradykinin precursor cDNAs from skin of Bombina maxima reveals novel bombinakinin M antagonists and a bradykinin potential peptide
文献类型:期刊论文
作者 | Lee WH1; Liu SB1,2; Shen JH1,3; Jin Y1; Zhang Y[*]1 |
刊名 | Regulatory Peptides
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出版日期 | 2005 |
卷号 | 127期号:X页码:207-215 |
关键词 | Bradykinin Amphibian Bombinakinin M Bombina maxima cDNA clone Variant |
通讯作者 | zhangy@mail.kiz.ac.cn |
英文摘要 | Bombinakinin M (DLPKINRKGP-bradykinin) is a bradykinin-related peptide purified from skin secretions of the frog Bombina maxima. As previously reported, its biosynthesis is characterized by a tandem repeats with various copy numbers of the peptide and sometimes co-expressed with other structure-function distinguishable peptides. At present study, two novel cDNAs encoding bombinakinin M and its variants were cloned from a cDNA library from the skin of the frog. The encoded two precursor proteins are common in that each contains three repeats of a novel 16-amino acid peptide unit and one copy of kinestatin at their N- and C-terminal parts, respectively. They differ in that the first precursor contains two copies of bombinakinin M and the second one contains one copy of a novel bombinakinin M variant. Bombinakinin M was found to elicit concentration-dependent contractile effects on guinea pig ileum, with an EC50 value of 4 nM that is four times higher than that of bradykinin (1 nM). Interestingly, the synthetic peptide (DYTIRTRLH-amide), as deduced from the 16-amino acid peptide repeats in the newly cloned cDNAs, possessed weak inhibitory activity on the contractile effects of bombinakinin M, but not on that of bradykinin. Furthermore, the newly identified bombinakinin M variant (DLSKMSFLHG-Ile(1)-bradykinin), did not show contractile activity on guinea pig ileum, but showed potentiation effect on the myotropic activity of bradykinin. In a molar raito of 1:58, it augmented the activity of bradykinin up to two-fold. |
收录类别 | SCI |
资助信息 | This work was supported by the grants of bSTZ98-3-01Q, bWestern LightQ Projects and bTenth Five Years PlanQ pre- research project from the Chinese Academy of Sciences; and grants from the National Natural Science Foundation (30170195, 30470380) and the Yunnan Science and Technology Commission (2001C0061M, 2001C0062M, 2003C0066M). |
语种 | 英语 |
源URL | [http://159.226.149.26:8080/handle/152453/11052] ![]() |
专题 | 昆明动物研究所_动物活性蛋白多肽组学 |
作者单位 | 1.Department of Animal Toxinology, Kunming Institute of Zoology, The Chinese Academy of Sciences, 32 East Jiao Chang Road, Kunming, Yunnan 650223, China 2.Graduate School of The Chinese Academy of Sciences, Beijing 100039, China 3.The First Affiliated Hospital of Kunming Medical College, Kunming, Yunnan 650032, China |
推荐引用方式 GB/T 7714 | Lee WH,Liu SB,Shen JH,et al. Cloning of bradykinin precursor cDNAs from skin of Bombina maxima reveals novel bombinakinin M antagonists and a bradykinin potential peptide[J]. Regulatory Peptides,2005,127(X):207-215. |
APA | Lee WH,Liu SB,Shen JH,Jin Y,&Zhang Y[*].(2005).Cloning of bradykinin precursor cDNAs from skin of Bombina maxima reveals novel bombinakinin M antagonists and a bradykinin potential peptide.Regulatory Peptides,127(X),207-215. |
MLA | Lee WH,et al."Cloning of bradykinin precursor cDNAs from skin of Bombina maxima reveals novel bombinakinin M antagonists and a bradykinin potential peptide".Regulatory Peptides 127.X(2005):207-215. |
入库方式: OAI收割
来源:昆明动物研究所
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