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首页> 外文期刊>Journal of Cellular Physiology >Differential intracellular transport and binding of verotoxin 1 and verotoxin 2 to globotriaosylceramide-containing lipid assemblies.
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Differential intracellular transport and binding of verotoxin 1 and verotoxin 2 to globotriaosylceramide-containing lipid assemblies.

机译：微分胞内运输和绑定verotoxin 1和verotoxin 2globotriaosylceramide-containing脂质程序集。

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摘要

Although verotoxin-1 (VT1) and verotoxin-2 (VT2) share a common receptor, globotriaosyl ceramide (Gb(3)), VT2 induces distinct animal pathology and is preferentially associated with human disease. Moreover VT2 cytotoxicity in vitro is less than VT1. We therefore investigated whether these toxins similarly traffic within cells via similar Gb(3) assemblies. At 4 degrees C, fluorescent-VT1 and VT2 bound both coincident and distinct punctate surface Gb(3) microdomains. After 10 min at 37 degrees C, similar distinct/coincident micropunctate intracellular localization was observed. Most internalized VT2, but not VT1, colocalized with transferrin. After 1 h, VT1 and VT2 coalesced during retrograde transport to the Golgi. During prolonged incubation (3-6 h), VT1, and VT2 (more slowly), exited the Golgi to reach the ER/nuclear envelope. At this time, VT2 induced a previously unreported, retrograde transport-dependent vacuolation. Cell surface and intracellular VT1 showed greater detergent resistance than VT2, suggesting differential 'raft' association. >90% (125)I-VT1 cell surface bound, or added to detergent-resistant cell membrane extracts (DRM), was in the Gb(3)-containing sucrose gradient 'insoluble' fraction, whereas only 30% (125)I-VT2 was similarly DRM-associated. VT1 bound more efficiently to Gb(3)/cholesterol DRMs generated in vitro. Only VT1 binding was inhibited by high cholesterol/Gb(3) ratios. VT2 competed less effectively for (125)I-VT1/Gb(3) DRM-binding but only VT2-Gb(3)/cholesterol DRM-binding was augmented by sphingomyelin. Differential VT1/VT2 Gb(3) raft-binding may mediate differential cell binding/intracellular trafficking and cytopathology.
机译：尽管verotoxin-1 (VT1)和verotoxin-2 (VT2)共享一个共同的受体,globotriaosyl神经酰胺(Gb (3)), VT2诱发不同的动物病理学并优先与人类有关疾病。不到VT1。这些毒素类似交通细胞内通过类似Gb(3)程序集。fluorescent-VT1和VT2重合和约束(3) microdomains截然不同的点状的表面Gb。在37摄氏度10分钟后,相似的定位观察。但不是VT1,与转铁蛋白。1 h, VT1和VT2逆行期间合并运输到高尔基体。孵化(3 - 6 h)、VT1 VT2(较慢),退出了高尔基体达到ER /核信封。上报,逆行transport-dependent空泡形成。显示更大的洗涤剂比VT2阻力,表明微分“木筏”协会。(125) I-VT1细胞表面,或添加到detergent-resistant细胞膜提取物(DRM),在Gb(3)含有蔗糖梯度不溶性的分数,而只有30% (125)I-VT2同样是DRM-associated。有效地Gb(3) /胆固醇生成drm体外。胆固醇/ Gb(3)比率。有效(125)I-VT1 / Gb (3) DRM-binding但是只有VT2-Gb(3) /胆固醇DRM-binding增强了鞘磷脂。Gb (3) raft-binding可能调解微分单元绑定/胞内贩卖细胞病理学。

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