Rab proteins in the brain and corpus allatum of Bombyx mori
Rab proteins in the brain and corpus allatum of Bombyx mori
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DOI:
10.1007/s00418-016-1422-y
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发表时间:
2016-03
影响因子:
2.3
通讯作者:
T. Uno;Masayuki Furutani;C. Watanabe;K. Sakamoto;Y. Uno;K. Kanamaru;H. Yamagata;A. Mizoguchi;M. Takeda
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文献类型:
--
作者:
T. Uno;Masayuki Furutani;C. Watanabe;K. Sakamoto;Y. Uno;K. Kanamaru;H. Yamagata;A. Mizoguchi;M. Takeda
In eukaryotic cells, Rab guanosine triphosphate-ases serve as key regulators of membrane-trafficking events, such as exocytosis and endocytosis. Rab3, Rab6, and Rab27 control the regulatory secretory pathway of neuropeptides and neurotransmitters. The cDNAs of Rab3, Rab6, and Rab27 fromB. moriwere inserted into a plasmid, transformed intoEscherichia coli, and then subsequently purified. We then produced antibodies against Rab3, Rab6, and Rab27 ofBombyx moriin rabbits and rats for use in western immunoblotting and immunohistochemistry. Western immunoblotting of brain tissue revealed a single band at approximately 26 kDa. Immunohistochemistry results revealed that Rab3, Rab6, and Rab27 expression was restricted to neurons in the pars intercerebralis and dorsolateral protocerebrum of the brain. Rab3 and Rab6 co-localized with bombyxin, an insect neuropeptide. However, there was no Rab that co-localized with prothoracicotropic hormone. The corpus allatum secretes neuropeptides synthesized in the brain into the hemolymph. Results showed that Rab3 and Rab6 co-localized with bombyxin in the corpus allatum. These findings suggest that Rab3 and Rab6 are involved in neurosecretion inB. mori.This study is the first to report a possible relationship between Rab and neurosecretion in the insect corpus allatum.