期刊
JOURNAL OF INSECT PHYSIOLOGY
卷 54, 期 8, 页码 1293-1300出版社
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.jinsphys.2008.06.012
关键词
Oncopeltus; innexon; connexon; intercellular communication
资金
- NSF [IBN 0314827]
Gap junctions between insect oocytes and follicular epithelia] cells allow transit of elongate Ca2+-binding proteins Calmodulin (CaM, 17 kDa) and Troponin-C (Trop-C, 18 kDa), but not multi-branched dextran (10 kDa) nor the Ca2+-binding protein Osteocalcin (Osten, 6 kDa). By microinjection of fluorescently labeled versions of each of these molecules we were able to obtain visual evidence that, despite their lesser molecular weight, molecules with greater cross-sections were unable to transit these gap junctions, while heavier but elongate molecules could. While CaM had previously been shown to pass through gap junctions from oocytes to their surrounding epithelial cells, the ability of CaM and Trop-C to transit the gap junctions between adjacent epithelial cells had not been demonstrated. Evidence shown here demonstrates that the homologous gap junctions among epithelial cells, like the heterologous gap junctions between epithelial cells and the oocyte they surround, allow transit of elongate molecules up to at least 18 kDa. Furthermore, the evidence for four different molecules of differing molecular weights and configurations supports the hypothesis that it is molecular configuration, not chemical activity, that primarily determines the observed permeability of gap junctions to molecules 5-6 times larger than the molecular weight limit previously acknowledged. (c) 2008 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