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Passage of 17kDa calmodulin through gap junctions of three vertebrate species

机译:17kDa钙调蛋白通过三种脊椎动物物种间隙连接的通道

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摘要

Gap junctions of some vertebrates are capable of passing the elongate molecule, calmodulin, with a molecular weight 8-17 times greater than the previously recognized size limits. Fluorescently labeled calmodulin (FCaM) (17.34kDa) microinjected into oocytes of ovarian follicles from an amphibian, Xenopus laevis, and from two species of teleost fish, Danio rerio (Zebrafish) and Oryzias latipes (Medaka), is shown to transit their gap junctions and enter the surrounding epithelial cells. Passage of FCaM was terminated when follicles were first treated with 1mM octanol, a molecule known to down-regulate gap junctions. There was no FCaM detected in the surrounding medium, nor did epithelial cells become fluorescent when follicles were incubated in medium containing dye. Calmodulin is well known to modulate many cytoplasmic reactions; thus, its passage through gap junctions opens possibilities of additional means by which cells may be supplied with this signaling molecule, and by which their supply may be regulated.
机译:一些脊椎动物的缝隙连接点能够通过伸长的分子钙调蛋白,其分子量比先前公认的大小限制大8-17倍。荧光标记的钙调蛋白(FCaM)(17.34kDa)被显微注射到两栖动物Xenopus laevis和两种硬骨鱼Danio rerio(Zebrafish)和Oryzias latipes(Medaka)的卵泡卵母细胞中,通过它们的间隙连接。并进入周围的上皮细胞当卵泡首先用1mM辛醇(一种已知能下调间隙连接的分子)处理时,FCaM的通道终止。在含有染料的培养基中孵育卵泡时,在周围的培养基中未检测到FCaM,上皮细胞也未发荧光。众所周知,钙调蛋白可调节许多细胞质反应。因此,其通过间隙连接的通过打开了附加手段的可能性,通过该手段可以向细胞提供该信号分子,并通过其调节其供给。

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