Bi-functional peptides with both trypsin-inhibitory and antimicrobial activities are frequent defensive molecules in Ranidae amphibian skins

	Bi-functional peptides with both trypsin-inhibitory and antimicrobial activities are frequent defensive molecules in Ranidae amphibian skins
	Yan XW 1; Liu H2,3; Yang XN 2,3; Che QL 1; Liu R 2; Yang HL 2,3; Liu XH 1; You DW 2; Wang AL 2; Li JX 2; Lai R1,2; bjx.2007@yahoo.com.cn ; rlai@mail.kiz.ac.cn
	2012
发表期刊	AMINO ACIDS
卷号	43 期号:1 页码:309-316
合作性质	其它
摘要	Amphibian skins act as the first line against noxious aggression by microorganisms, parasites, and predators. Anti-microorganism activity is an important task of amphibian skins. A large amount of gene-encoded antimicrobial peptides (AMPs) has been identified from amphibian skins. Only a few of small protease inhibitors have been found in amphibian skins. From skin secretions of 5 species (Odorrana livida, Hylarana nigrovittata, Limnonectes kuhlii, Odorrana grahami, and Amolops loloensis) of Ranidae frogs, 16 small serine protease inhibitor peptides have been purified and characterized. They have lengths of 17-20 amino acid residues (aa). All of them are encoded by precursors with length of 65-70 aa. These small peptides show strong trypsin-inhibitory abilities. Some of them can exert antimicrobial activities. They share the conserved GCWTKSXXPKPC fragment in their primary structures, suggesting they belong to the same families of peptide. Signal peptides of precursors encoding these serine protease inhibitors share obvious sequence similarity with those of precursors encoding AMPs from Ranidae frogs. The current results suggest that these small serine protease inhibitors are the common defensive compounds in frog skin of Ranidae as amphibian skin AMPs.
关键词	Amphibian Skin Antimicrobial Peptide Innate Immunity Protease Inhibitor Serine
资助者	This work was supported by Chinese National Natural Science Foundation (30830021, 30800185, 31025025), the Ministry of Science and Technology (2010CB529800, 2009ZX09103- 1/091) and the Ministry of Agriculture (2009ZX08009-159B). ; This work was supported by Chinese National Natural Science Foundation (30830021, 30800185, 31025025), the Ministry of Science and Technology (2010CB529800, 2009ZX09103- 1/091) and the Ministry of Agriculture (2009ZX08009-159B). ; This work was supported by Chinese National Natural Science Foundation (30830021, 30800185, 31025025), the Ministry of Science and Technology (2010CB529800, 2009ZX09103- 1/091) and the Ministry of Agriculture (2009ZX08009-159B). ; This work was supported by Chinese National Natural Science Foundation (30830021, 30800185, 31025025), the Ministry of Science and Technology (2010CB529800, 2009ZX09103- 1/091) and the Ministry of Agriculture (2009ZX08009-159B).
收录类别	SCI
语种	英语
资助者	This work was supported by Chinese National Natural Science Foundation (30830021, 30800185, 31025025), the Ministry of Science and Technology (2010CB529800, 2009ZX09103- 1/091) and the Ministry of Agriculture (2009ZX08009-159B). ; This work was supported by Chinese National Natural Science Foundation (30830021, 30800185, 31025025), the Ministry of Science and Technology (2010CB529800, 2009ZX09103- 1/091) and the Ministry of Agriculture (2009ZX08009-159B). ; This work was supported by Chinese National Natural Science Foundation (30830021, 30800185, 31025025), the Ministry of Science and Technology (2010CB529800, 2009ZX09103- 1/091) and the Ministry of Agriculture (2009ZX08009-159B). ; This work was supported by Chinese National Natural Science Foundation (30830021, 30800185, 31025025), the Ministry of Science and Technology (2010CB529800, 2009ZX09103- 1/091) and the Ministry of Agriculture (2009ZX08009-159B).
WOS记录号	WOS:000305210800031
引用统计
文献类型	期刊论文
条目标识符	http://ir.kiz.ac.cn/handle/152453/7040
专题	科研部门_天然药物功能蛋白质学科组（赖仞）科研部门_动物模型与人类重大疾病机理重点实验室
通讯作者	bjx.2007@yahoo.com.cn; rlai@mail.kiz.ac.cn
作者单位	1.Life Sciences College of Nanjing Agricultural University, Nanjing, Jiangsu 210095, China 2.Key Laboratory of Animal Models and Human Disease Mechanisms, Kunming Institute of Zoology, Chinese Academy of Sciences, Kunming, 650223 Yunnan, China 3.Graduate School of the Chinese Academy of Sciences, Beijing 100009, China
推荐引用方式 GB/T 7714	Yan XW,Liu H*,Yang XN,et al. Bi-functional peptides with both trypsin-inhibitory and antimicrobial activities are frequent defensive molecules in Ranidae amphibian skins[J]. AMINO ACIDS,2012,43(1):309-316.
APA	Yan XW.,Liu H*.,Yang XN.,Che QL.,Liu R.,...&rlai@mail.kiz.ac.cn.(2012).Bi-functional peptides with both trypsin-inhibitory and antimicrobial activities are frequent defensive molecules in Ranidae amphibian skins.AMINO ACIDS,43(1),309-316.
MLA	Yan XW,et al."Bi-functional peptides with both trypsin-inhibitory and antimicrobial activities are frequent defensive molecules in Ranidae amphibian skins".AMINO ACIDS 43.1(2012):309-316.

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