肝细胞质膜的一种域特异性标记物。II. 亮氨酸氨基肽酶在分离的大鼠肝质膜胆小管域的超微结构定位
A domain-specific marker for the hepatocyte plasma membrane. II. Ultrastructural localization of leucine aminopeptidase to the bile canalicular domain of isolated rat liver plasma membranes.
作者信息
Roman L M, Hubbard A L
出版信息
J Cell Biol. 1984 Apr;98(4):1488-96. doi: 10.1083/jcb.98.4.1488.
Abstract
Leucine aminopeptidase (LAP) is an integral membrane glycoprotein localized to the apical membrane domain of intestinal and kidney epithelial cells. By indirect immunofluorescence, we have shown that antibodies raised against rat intestinal LAP recognized a similar protein concentrated in the bile canalicular (BC) domain of the hepatocyte in situ (Roman, L.M., and A.L. Hubbard, 1983, J. Cell Biol., 96:1548-1558). We have extended this localization to the ultrastructural level. When a saponin-permeabilized, agarose-embedded plasma membrane (PM) fraction was incubated with affinity-purified anti-LAP, 85% of the protein A-gold particles associated with the three recognizable PM domains were present in the BC. The levels of labeling on the other two domains (sinusoidal and lateral) did not exceed that observed with nonimmune controls. The concentration of LAP in the BC domain in isolated PM sheets prompted us to use this antigen for the affinity isolation of BC membrane (Roman, L.M., and A.L. Hubbard, 1984, J. Cell Biol., 98:1497-1504, companion paper).
摘要
亮氨酸氨肽酶（LAP）是一种整合膜糖蛋白，定位于肠道和肾脏上皮细胞的顶端膜结构域。通过间接免疫荧光法，我们发现针对大鼠肠道LAP产生的抗体能够识别一种类似的蛋白质，该蛋白质在原位肝细胞的胆小管（BC）结构域中富集（罗曼，L.M.，和A.L.哈伯德，1983年，《细胞生物学杂志》，96:1548 - 1558）。我们已将这种定位扩展到超微结构水平。当用皂苷通透、琼脂糖包埋的质膜（PM）组分与亲和纯化的抗LAP一起孵育时，与三个可识别的PM结构域相关的蛋白A - 金颗粒中有85%存在于BC中。另外两个结构域（窦状和侧面）的标记水平不超过非免疫对照所观察到的水平。在分离的PM片中BC结构域中LAP的富集促使我们使用这种抗原来亲和分离BC膜（罗曼，L.M.，和A.L.哈伯德，1984年，《细胞生物学杂志》，98:1497 - 1504，配套论文）。
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