把最近查的摘要集放在这里，免得以后又找不到~

1	Two families of antimicrobial peptides with multiple functions from skin of rufous-spotted torrent frog, Amolops loloensis  • ARTICLE Peptides, Volume 27, Issue 12, December 2006, Pages 3085-3091 Yi Lu, Jianxu Li, Haining Yu, Xueqing Xu, Jianguo Liang, Yongqiang Tian, Dongying Ma, Guoqing Lin, Guoqiang Huang and Ren Lai SummaryPlus | Full Text + Links | PDF (269 K)
	There are around 27 species of Amolops amphibian distributed in South-east of Asia. Seven antimicrobial peptides (AMPs) belonging to two different families were purified from skin of rufous-spotted torrent frog, Amolops loloensis, and designated brevinins-ALa, b, c, and d, and temporins-ALa, b, and c. The brevinins-AL family which is structurally related to brevinins-1 from skin secretions of the European frog, Rana brevipoda, is composed of 24 amino acids and has an intra-disulfide bridge at the C-terminus. The temporins-AL family, composed of 13 or 16 amino acid residues, is related with temporins from the skin secretions of R. temporaria. The findings of this study will facilitate the solutions to the taxonomic questions of the ranid genus Amolops and Staurois. In the work of this paper, both brevinins-ALb and temporin-Ma induced mast cell degranulation and histamine release, and had cytotoxic activity toward solid tumor cell line HepG2. Brevinins-ALb also exerted strong hemolytic activity while temporin-Ma had no such activity.

 

2	Molecular cloning and functional characterization of a prolactin-releasing peptide homolog from Xenopus laevis  • ARTICLE Peptides, Volume 27, Issue 12, December 2006, Pages 3347-3351 Tatsuya Sakamoto, Aiko Oda, Kazutoshi Yamamoto, Miyoko Kaneko, Sakae Kikuyama, Akio Nishikawa, Akiyoshi Takahashi, Hiroshi Kawauchi, Kazuyoshi Tsutsui and Masaaki Fujimoto SummaryPlus | Full Text + Links | PDF (227 K)
	Amino acid sequences for identified prolactin (PRL)-releasing peptides (PrRPs) were conserved in mammals (>90%) or teleost fishes (100%), but there were considerable differences between these classes in the sequence (<65%) as well as in the role of PrRP. In species other than fishes and mammals, we have identified frog PrRP. The cDNA encoding Xenopus laevis prepro-PrRP, which can generate putative PrRPs, was cloned and sequenced. Sequences for the coding region showed higher identity with teleost PrRPs than mammalian homologues, but suggested the occurrence of putative PrRPs of 20 and 31 residues as in mammals. The amino acid sequence of PrRP20 was only one residue different from teleost PrRP20, but shared 70% identity with mammalian PrRP20s. In primary cultures of bullfrog (Rana catesbeiana) pituitary cells, Xenopus PrRPs increased prolactin concentrations in culture medium to 130–160% of the control, but PrRPs was much less potent than thyrotropin-releasing hormone (TRH) causing a three- to four-fold increase in prolactin concentrations. PrRP mRNA levels in the developing Xenopus brain peak in early prometamorphosis, different from prolactin levels. PrRP may not be a major prolactin-releasing factor (PRF), at least in adult frogs, as in mammals.