Characterization of the βγ-crystallin domains of βγ-CAT, a non-lens βγ-crystallin and trefoil factor complex, from the skin of the toad Bombina maxima
文献类型：期刊论文
| 作者 | Gao Q1,2; Xiang Y1,3; Lee WH1; Zhang Y[*]1; Zeng L1,3; Ma XT1,3 |
| 刊名 | BIOCHIMIE
 |
| 出版日期 | 2011 |
| 卷号 | 93期号:10页码:1865–1872 |
| 关键词 | Non-lens βγ-crystallins βγ-CAT Ca2+ binding Hemolysis Ca2+ influx |
| 通讯作者 | zhangy@mail.kiz.ac.cn |
| 合作状况 | 其它 |
| 英文摘要 | βγ-CAT is a naturally existing 72-kDa complex of a non-lens βγ-crystallin (α-subunit, CAT-α) and a trefoil factor (β-subunit, CAT-β) that contains a non-covalently linked form of αβ(2) and was isolated from the skin secretions of the toad Bombina maxima. The N-terminal region of CAT-α (CAT-αN, residues 1-170) contains two βγ-crystallin domains while the C-terminal region (CAT-αC) has sequence homology to the membrane insertion domain of the Clostridium perfringens epsilon toxin. To examine the biochemical characteristics of the βγ-crystallin domains of βγ-CAT, CAT-αN, CAT-αC and CAT-β were expressed in Escherichia coli. Co-immunoprecipitation of the naturally assembled βγ-CAT confirmed that the CAT-α and CAT-β complex always exists. Furthermore, recombinant CAT-β bound recombinant CAT-αN. Ca(2+)-binding motifs were identified in CAT-αN, and recombinant CAT-αN was able to bind the calcium probe terbium. However, the conformation of CAT-αN was not significantly altered upon Ca(2+) binding. βγ-CAT possesses strong hemolytic activity toward human erythrocytes, and treatment of erythrocytes with βγ-CAT resulted in a rapid Ca(2+) influx, eventually leading to hemolysis. However, in the absence of extracellular Ca(2+), no significant hemolysis was detected, even though the binding and oligomerization of βγ-CAT in the erythrocyte membrane was observed. Our data demonstrate the binding of CAT-β (a trefoil factor) to CAT-αN (βγ-crystallin domains) and provide a basis for the formation of a βγ-crystallin and trefoil factor complex in vivo. Furthermore, the βγ-crystallin domains of βγ-CAT are able to bind Ca(2+), and βγ-CAT-induced hemolysis is Ca(2+) dependent. |
| 收录类别 | SCI |
| 资助信息 | This work was supported by grants from the National Basic Research Program of China (973 Program, 2010CB529800) and the Chinese National Natural Science Foundation (30630014 and 30870304) to Yun Zhang. |
| 语种 | 英语 |
| 源URL | [http://159.226.149.26:8080/handle/152453/9590]  |
| 专题 | 昆明动物研究所_动物活性蛋白多肽组学 昆明动物研究所_动物模型与人类重大疾病机理重点实验室 |
| 作者单位 | 1.Key Laboratory of Animal Models and Human Disease Mechanisms of the Chinese Academy of Sciences, Kunming Institute of Zoology, The Chinese Academy of Sciences, 32 East Jiao Chang Road, Kunming 650223, China 2.Yunnan Academy of Tobacco Science, Kunming, China 3.Graduate School of Chinese Academy of Sciences, Beijing, China |
| 推荐引用方式 GB/T 7714 | Gao Q,Xiang Y,Lee WH,et al. Characterization of the βγ-crystallin domains of βγ-CAT, a non-lens βγ-crystallin and trefoil factor complex, from the skin of the toad Bombina maxima[J]. BIOCHIMIE,2011,93(10):1865–1872. |
| APA | Gao Q,Xiang Y,Lee WH,Zhang Y[*],Zeng L,&Ma XT.(2011).Characterization of the βγ-crystallin domains of βγ-CAT, a non-lens βγ-crystallin and trefoil factor complex, from the skin of the toad Bombina maxima.BIOCHIMIE,93(10),1865–1872. |
| MLA | Gao Q,et al."Characterization of the βγ-crystallin domains of βγ-CAT, a non-lens βγ-crystallin and trefoil factor complex, from the skin of the toad Bombina maxima".BIOCHIMIE 93.10(2011):1865–1872. |
入库方式： OAI收割
来源：昆明动物研究所
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