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氨肽酶N在到达肠上皮细胞刷状缘之前穿过基底外侧膜的证据。

Evidence for the transit of aminopeptidase N through the basolateral membrane before it reaches the brush border of enterocytes.

作者信息

Massey D, Feracci H, Gorvel J P, Rigal A, Soulié J M, Maroux S

出版信息

J Membr Biol. 1987;96(1):19-25. doi: 10.1007/BF01869331.

DOI:10.1007/BF01869331
PMID:2884323
Abstract

In vivo pulse-chase labeling of rabbit jejunum loops was used in conjunction with subcellular fractionation and quantitative immunoprecipitation to determine whether or not the newly synthesized aminopeptidase N transits through the basolateral membrane before it reaches the apical brush border, its final localization. The kinetics of the arrival of the newly synthesized enzyme in the Golgi complex, basolateral and brush border membrane fractions strongly suggest that on leaving the Golgi aminopeptidase N is transiently integrated into the basolateral domain before reaching the brush border.

摘要

采用兔空肠袢的体内脉冲追踪标记法,结合亚细胞分级分离和定量免疫沉淀法,以确定新合成的氨肽酶N在到达其最终定位——顶端刷状缘之前是否穿过基底外侧膜。新合成的酶到达高尔基体、基底外侧膜和刷状缘膜部分的动力学强烈表明,氨肽酶N离开高尔基体后在到达刷状缘之前会短暂整合到基底外侧结构域中。

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Transepithelial transport of a viral membrane glycoprotein implanted into the apical plasma membrane of Madin-Darby canine kidney cells. I. Morphological evidence.
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Direct targeting of neutral endopeptidase (EC 3.4.24.11) to the apical cell surface of transfected LLC-PK1 cells and unpolarized secretion of its soluble form.将中性内肽酶(EC 3.4.24.11)直接靶向转染的LLC-PK1细胞的顶端细胞表面及其可溶性形式的非极化分泌。
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