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糖基磷脂酰肌醇锚定蛋白优先靶向至肝细胞胆小管(顶端)质膜。“晚期”内体的参与。

Priority targeting of glycosyl-phosphatidylinositol-anchored proteins to the bile-canalicular (apical) plasma membrane of hepatocytes. Involvement of 'late' endosomes.

作者信息

Ali N, Evans W H

机构信息

National Institute for Medical Research, Mill Hill, London, U.K.

出版信息

Biochem J. 1990 Oct 1;271(1):193-9. doi: 10.1042/bj2710193.

Abstract
  1. Liver plasma membranes originating from the sinusoidal, lateral and canalicular surface domains of hepatocytes were covalently labelled with sulpho-N-hydroxysuccinamide-biotin. After solubilization in Triton X-114, treatment with a phosphatidylinositol-specific phospholipase C (PI-PLC), two-phase partitioning and 125I-streptavidin labelling of the proteins resolved by PAGE, six major polypeptides (molecular masses 110, 85, 70, 55, 38 and 35 kDa) were shown to be anchored in bile canalicular membrane vesicles by a glycosyl-phosphatidylinositol (G-PI) 'tail'. 2. Permeabilized 'early' and 'late' endocytic vesicles isolated from liver were also examined. Two polypeptides (110 and 35 kDa) were shown to be anchored by a G-PI tail in 'late' endocytic vesicles. 3. Analysis of marker enzymes in bile-canalicular vesicles treated with PI-PLC showed that 5'-nucleotidase and alkaline phosphatase, but not leucine aminopeptidase and ecto-Ca2(+)-ATPase activities were released from the membrane. A low release and recovery of alkaline phosphodiesterase activity was noted. The cleavage from the membrane of 5'-nucleotidase as a 70 kDa polypeptide was confirmed by Western blotting using an antibody to this enzyme. 4. Antibodies raised to proteins released from bile-canalicular vesicles by PI-PLC treatment, and purified by partitioning in aqueous and Triton X-114 phases, localized to the bile canaliculi in thin liver sections. Antibodies to proteins not hydrolysed by this treatment stained by immunofluorescence the sinusoidal and canalicular surface regions of hepatocytes. 5. Antibodies generated to proteins cleaved by PI-PLC treatment of canalicular vesicles were shown to identify, by Western blotting, a major 110 kDa polypeptide in these vesicles. Two polypeptides (55 and 38 kDa) were detected in MDCK and HepG-2 cultured cells. 6. Since two of the six G-PI-anchored proteins targeted to the bile-canalicular plasma membrane were also detected in 'late' endocytic vesicles, the results suggest that a junction where exocytic and endocytic traffic routes meet occurs in a 'late' endocytic compartment.
摘要
  1. 源自肝细胞窦状、侧面和胆小管表面区域的肝细胞膜用磺基 - N - 羟基琥珀酰亚胺 - 生物素进行共价标记。在Triton X - 114中溶解后,用磷脂酰肌醇特异性磷脂酶C(PI - PLC)处理,进行两相分配以及对通过聚丙烯酰胺凝胶电泳(PAGE)分离的蛋白质进行125I - 链霉亲和素标记,结果显示六种主要多肽(分子量分别为110、85、70、55、38和35 kDa)通过糖基磷脂酰肌醇(G - PI)“尾巴”锚定在胆小管膜泡中。2. 对从肝脏分离的通透化“早期”和“晚期”内吞小泡也进行了检查。结果显示两种多肽(110和35 kDa)通过G - PI尾巴锚定在“晚期”内吞小泡中。3. 对用PI - PLC处理的胆小管小泡中的标记酶进行分析表明,5'-核苷酸酶和碱性磷酸酶的活性从膜上释放出来,但亮氨酸氨肽酶和胞外Ca2(+) - ATP酶的活性未释放。碱性磷酸二酯酶活性的释放和回收率较低。使用针对该酶的抗体通过蛋白质印迹法证实5'-核苷酸酶作为一种70 kDa的多肽从膜上裂解下来。4. 针对经PI - PLC处理从胆小管小泡中释放的蛋白质制备的抗体,通过在水相和Triton X - 114相中分配进行纯化,在薄肝切片中定位于胆小管。针对未被该处理水解的蛋白质的抗体通过免疫荧光染色肝细胞的窦状和胆小管表面区域。5. 针对经PI - PLC处理胆小管小泡后裂解的蛋白质产生的抗体,通过蛋白质印迹法显示可识别这些小泡中的一种主要的110 kDa多肽。在MDCK和HepG - 2培养细胞中检测到两种多肽(55和38 kDa)。6. 由于靶向胆小管质膜的六种G - PI锚定蛋白中的两种也在“晚期”内吞小泡中被检测到,结果表明胞吐和内吞运输途径交汇的连接点出现在“晚期”内吞区室中。
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/325a/1149532/b8e4ed190671/biochemj00174-0187-a.jpg

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