期刊
INSECT BIOCHEMISTRY AND MOLECULAR BIOLOGY
卷 36, 期 1, 页码 47-53出版社
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.ibmb.2005.10.005
关键词
diapause; stress; kinase; phosphorylation; chilling; HCl
To clarify the molecular mechanisms of Bombyx diapause, we focused oil mitogen-activated protein kinases (MAPK), which are the major components or signal transduction cascades that regulate cell proliferation, differentiation, and stress responses. In the present Study, cloning of Bombyx extracellular signal-related kinase (ERK), MAPK-ERK kinase (MEK), and p38 MAPK cDNA, revealed that their amino acid sequences have close similarity with those of other species. We analyzed the roles of the kinases, in diapause initiation and termination by immuno-blotting with anti-phospho-kinase antibodies. Phospho-MEK levels remained consistently high in non-diapausing eggs, then declined after the diapausing stage in diapausing eggs, and began to increase 45 d after transfer to 5 degrees C Upon diapause termination. The phospho-ERK and phospho-MEK profiles were similar, Suggesting that ERK phosphorylation is regulated by MEK. The phospho-p38 MAPK levels declined 36 h after oviposition in diapausing eggs, and increased at 15-30 d at 5 degrees C in yolk cells, suggesting that p38 MAPK has a role in diapause initiation and termination. Phospho-ERK levels were maintained with diapause-interrupting treatment and declined with diapause-sustaining treatment. ERK phosphorylation is considered to have a role in diapause termination and in the resumption of development. (C) 2005 Elsevier Ltd. All rights reserved.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据