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Molecular physiology on H^+-translocating vacuolar-type ATPase in silkworms

家蚕H^-易位液泡型ATP酶的分子生理学

基本信息

批准号：
09660058
负责人：
AZUMA Masaaki
金额：
$ 2.5万
依托单位：
Tottori University
依托单位国家：
日本
项目类别：
Grant-in-Aid for Scientific Research (C)
财政年份：
1997
资助国家：
日本
起止时间：
1997 至 1998
项目状态：
已结题

来源：
https://kaken.nii.ac.jp/grant/KAKENHI-PROJECT-09660058/
关键词：
silkworm midgut amino acid transport V-ATPase Potassium pump Proton pump silk gland Bombyx mori

项目摘要

The silk gland in silkworms (the silk proteins, fibroin and sericin, factory) is an unique and indispensable tissue to produce the cocoons. The gland secretes and temporally stores the silk proteins within the glandular lumen without any denaturation of proteins till the silkworm starts to spin. The concentrations in the secreted protein reach up to 20-30% levels. Such a high concentration of the protein solution has to be regulated with a certain pH levels and a fixed water contents. We have investigated such a mechanism to understand the- ionic homeostasis and osmoregulation in the silk gland. Results are as-follows :(1) Immunocytochemicat studies were done with the specific antibody against Y-ATPase.. The V-ATFase can be- detected in the silk gland. V-A-TPase was located at the cell surface, suggesting that silkworm V-ATPases is a plasm a membrane-type not an endomanbrane-type.(2) In the silk gland, V-ATPase seems to contribute to produce an acidic milieu in the glandular lumen. This shows highly contrast to the lepidopteran midgut lumen, which produces. an extremely high alkalinity (pH-11-12).(3) The silk gland V-ATPase is quite-similar to other animal V-ATPase sharing the common subuits of V-ATPase.(4) The silk gland is a highly active tissue for silk protein syntesis and secretion The V-ATPase has to energize the plasma membrane and this supports that the active-amino acid transport from the haemolymph in order to synthesize the silkproteiri. Thus it is coming up as the near future subject to survey the K+/amino acid symporter in the silkgland. This would be expected as The breakthrough for identifying the K+/symportev molecule(s).

蚕的丝腺（丝蛋白、丝素蛋白和丝胶蛋白，工厂）是生产蚕茧的独特和不可缺少的组织。腺体分泌丝蛋白并将其暂时储存在腺腔内，直到蚕开始吐丝，蛋白质没有任何变性。分泌蛋白中的浓度达到20-30%水平。如此高浓度的蛋白质溶液必须用一定的pH水平和固定的水含量来调节。我们已经研究了这样一种机制，以了解丝腺中的离子稳态和离子调节。结果如下：（1）用Y-ATPase特异性抗体进行免疫细胞化学研究。在丝腺中可检测到V-ATFase。V-A-TPases定位于细胞表面，表明家蚕V-ATP酶是胞浆膜型而不是内膜型。(2)在丝腺中，V-ATPase似乎有助于在腺腔中产生酸性环境。这显示出与鳞翅目中肠腔的高度对比，中肠腔产生。碱度极高（pH-11-12）。(3)丝腺V-ATP酶与其它动物V-ATP酶十分相似，具有V-ATP酶的共同亚基。(4)丝腺是丝蛋白合成和分泌的高度活跃的组织。V-ATPase必须为质膜提供能量，这支持活性氨基酸从血淋巴中转运，以合成丝蛋白。因此，对丝腺K+/氨基酸同向转运体的研究将成为今后的研究课题。这将有望成为鉴定K+/symportev分子的突破。