Differential localization of human nongastric H(+)-K(+)-ATPase ATP1AL1 in polarized renal epithelial cells.
Differential localization of human nongastric H(+)-K(+)-ATPase ATP1AL1 in polarized renal epithelial cells.
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人非胃 H( )-K( )-ATP 酶 ATP1AL1 在极化肾上皮细胞中的差异定位。
DOI：
10.1152/ajprenal.2000.279.3.f417
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发表时间：
2000
期刊：
影响因子：
--
通讯作者：
Caplan,MJ
中科院分区：
文献类型：
--
作者：
Reinhardt,J;Grishin,AV;Oberleithner,H;Caplan,MJ
人H ~+-K ~+-ATP酶（ATP 1AL 1）属于非胃K ~+转运ATP酶亚类。与结构相关的胃H+-K+-ATP酶一致，它在各种组织（包括结肠和肾脏）的K+重吸收中起主要作用。生理和免疫细胞化学数据表明，功能性异聚体离子泵通常存在于肾上皮细胞的顶端质膜。然而，特征性非胃离子泵的低表达水平使得难以验证它们在体内的空间分布。为了研究ATP 1AL 1的分选行为，我们通过稳定转染MDCK和LLC-PK 1肾上皮细胞系来表达该泵。通过共聚焦免疫荧光显微镜和表面生物素化检测ATP 1AL 1与内源性Na+-K+-ATP酶β亚基或胃H+-K+-ATP酶β亚基的稳定相互作用。在单独用ATP 1AL 1转染的细胞中，α亚基在细胞内积累，这与其不能与内源性Na+-K+-ATP酶β亚基组装并行进至质膜一致。将ATP 1AL 1与胃H+-K+-ATP酶β亚基共转染后，两种泵亚基均定位于质膜。在共转染MDCK细胞的异聚体离子泵主要极化顶端质膜。通过~（86）Rb ~+摄取测量证实ATP 1AL 1的功能性表达。相反，共转染LLC-PK 1细胞在侧膜上积累ATP 1AL 1。ATP 1AL 1的不同极化表明α亚基编码的分选信息被细胞类型特异性分选机制不同地解释。
The human H+-K+-ATPase, ATP1AL1, belongs to the subgroup of nongastric, K+-transporting ATPases. In concert with the structurally related gastric H+-K+-ATPase, it plays a major role in K+reabsorption in various tissues, including colon and kidney. Physiological and immunocytochemical data suggest that the functional heteromeric ion pumps are usually found in the apical plasma membranes of renal epithelial cells. However, the low expression levels of characteristic nongastric ion pumps makes it difficult to verify their spatial distribution in vivo. To investigate the sorting behavior of ATP1AL1, we expressed this pump by stable transfection in MDCK and LLC-PK1renal epithelial cell lines. Stable interaction of ATP1AL1 with either the endogenous Na+-K+-ATPase β-subunit or the gastric H+-K+-ATPase β-subunit was tested by confocal immunofluorescence microscopy and surface biotinylation. In cells transfected with ATP1AL1 alone, the α-subunit accumulated intracellularly, consistent with its inability to assemble and travel to the plasma membrane with the endogenous Na+-K+-ATPase β-subunit. Cotransfection of ATP1AL1 with the gastric H+-K+-ATPase β-subunit resulted in plasma membrane localization of both pump subunits. In cotransfected MDCK cells the heteromeric ion pump was predominantly polarized to the apical plasma membrane. Functional expression of ATP1AL1 was confirmed by86Rb+uptake measurements. In contrast, cotransfected LLC-PK1cells accumulate ATP1AL1 at the lateral membrane. The distinct polarization of ATP1AL1 indicates that the α-subunit encodes sorting information that is differently interpreted by cell type-specific sorting mechanisms.
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极化上皮细胞中离子泵的分类。
影响因子：
5.2
作者：
L. Dunbar;D. Roush;N. Courtois;T. Muth;C. Gottardi;V. Rajendran;J. Geibel;M. Kashgarian;Michael J. Caplan
通讯作者：
Michael J. Caplan
[人类Na,K-ATP酶基因家族。
DOI：
--
发表时间：
1987
期刊：
Doklady Akademii nauk SSSR
影响因子：
--
作者：
E. Sverdlov;Monastyrskaia Gs;N. Broude;Ushkarev IuA;R. L. Allikmets
通讯作者：
R. L. Allikmets
大鼠结肠 K-腺苷三磷酸酶的功能表达和节段定位。
DOI：
10.1172/jci118247
发表时间：
1995
期刊：
The Journal of clinical investigation
影响因子：
--
作者：
Lee,J;Rajendran,VM;Mann,AS;Kashgarian,M;Binder,HJ
通讯作者：
Binder,HJ
大鼠和兔肾中 H-K-ATPase β 亚基 mRNA 的原位杂交。
DOI：
10.1152/ajprenal.1995.269.3.f345
发表时间：
1995
期刊：
The American journal of physiology
影响因子：
--
作者：
Campbell-Thompson,ML;Verlander,JW;Curran,KA;Campbell,WG;Cain,BD;Wingo,CS;McGuigan,JE
通讯作者：
McGuigan,JE
结肠 H-K-ATP 酶 β 亚基：顶膜中的识别和饮食 K 消耗的调节。
DOI：
--
发表时间：
1999
期刊：
American Journal of Physiology - Cell Physiology
影响因子：
--
作者：
P. Sangan;S. Kolla;V. Rajendran;M. Kashgarian;H. Binder
通讯作者：
H. Binder