Identification of molting fluid carboxypeptidase A (MF-CPA) in Bombyx mori
Identification of molting fluid carboxypeptidase A (MF-CPA) in Bombyx mori
复制标题
DOI：
10.1016/j.cbpc.2005.04.005
复制
发表时间：
2005-07-01
影响因子：
2.2
通讯作者：
Shimada, T
中科院分区：
文献类型：
--
作者：
Ote, M;Mita, K;Shimada, T
利用微阵列分析，我们确定羧肽酶A（MF-CPA），这是诱导蛹蜕皮过程中的翅盘的家蚕。在这里，我们报告MF-CPA的功能特性。MF-CPA与从人类到线虫的羧肽酶A/B亚家族中的蛋白质具有氨基酸序列相似性。MF-CPA基因在蜕皮期间在上皮组织中表达。MF-CPA在蜕皮液中检测到，其在蜕皮期间填充新旧角质层之间的空间。通过蛋白质印迹分析，我们表明，MF-CPA分泌作为酶原和加工的蜕皮液。在昆虫细胞中表达的重组MF-CPA具有羧肽酶A活性。我们建议，MF-CPA降解蛋白质从旧角质层在蜕皮期间，并有助于回收的氨基酸。(c)2005年爱思唯尔公司All rights reserved.
Using microarray analyses, we identified carboxypeptidase A (MF-CPA), which was induced during pupal ecdysis in the wing discs of Bombyx mori. Here, we report the functional characterization of MF-CPA. MF-CPA has amino acid sequence similarities with the proteins in the carboxypeptidase A/B subfamily, from human to nematode. The MF-CPA gene is expressed during the molting periods in the epithelial tissues. MF-CPA is detected in the molting fluid, which fills the space between the old and new cuticle during molting. By Western blot analysis, we show that MF-CPA is secreted as a zymogen and processed in the molting fluid. Recombinant MF-CPA expressed in the insect cells has carboxypeptidase A activity. We propose that MF-CPA degrades the proteins from the old cuticle during the molting periods and contributes to recycling of the amino acids. (c) 2005 Elsevier Inc. All rights reserved.