Response of intercalated cells to chloride depletion metabolic alkalosis.
Response of intercalated cells to chloride depletion metabolic alkalosis.
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闰细胞对氯消耗代谢性碱中毒的反应。
DOI：
10.1152/ajprenal.1992.262.2.f309
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发表时间：
1992
期刊：
影响因子：
--
通讯作者：
Tisher,CC
中科院分区：
文献类型：
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作者：
Verlander,JW;Madsen,KM;Galla,JH;Luke,RG;Tisher,CC
本实验观察了去氯代谢性损伤（CDA）对大鼠皮质集合管（CCD）和外髓集合管（OMCD）闰层细胞（IC）H（+）-ATP酶和带3蛋白定位的影响。用0.15 M NaHCO 3进行30分钟腹膜透析以产生CDA，或林格氏碳酸氢盐作为对照（CON）后，两组均静脉输注80 mM Cl-溶液90分钟。对于CDA与CON，生理参数如下：血浆总CO2，38.0 +/- 1.1 vs. 27.8 +/- 0.6 meq/l（P小于0.001）;尿总CO2排泄量，141 +/- 89 vs. 20 +/- 3 neq.min-1.100 g体重-1;和尿氯排泄，20 +/- 10 vs. 486 +/- 144 neq.min-1.100 g体重-1（P <0.001）。用兔抗牛脑H（+）-ATP酶70-kDa亚基的多克隆抗体在薄切片中定位H（+）-ATP酶。使用针对人红细胞带3蛋白质的胞质结构域的43-kDa亚基的多克隆抗体定位带3蛋白。在CON大鼠，H（+）-ATP酶定位于沿着顶质膜和顶胞质囊泡的A型IC在CCD和IC的OMCD。沿着基底侧质膜和胞质囊泡上的H（+）-ATP酶在整个B型IC中可见。在CDA大鼠中，仅在A型IC和大多数OMCD IC的顶端胞质囊泡上观察到H（+）-ATP酶。在B型IC中，CDA中H（+）-ATP酶沿基底质膜沿着染色增强。带3蛋白始终定位于基底外侧质膜的所有A型细胞在CCD和IC的OMCD在CON和CDA。总之，刺激大鼠HCO 3-分泌导致H（+）-ATP酶从顶质膜撤回，并储存在顶胞质囊泡中的IC的OMCD和A型IC的CCD。H（+）-ATP酶插入到B型IC的基底膜上。这些研究结果表明，在校正CDA，质子分泌的A型和OMCD IC被抑制和质子运输跨基底外侧质膜的B型IC的刺激。
We examined the effect of Cl- depletion metabolic alkalosis (CDA) on H(+)-ATPase and band 3 protein localization in intercalated cells (IC) of the rat cortical collecting duct (CCD) and the outer medullary collecting duct (OMCD). After 30 min of peritoneal dialysis against 0.15 M NaHCO3 to produce CDA, or Ringer bicarbonate to serve as controls (CON), both groups were infused intravenously with an 80 mM Cl- solution for 90 min. For CDA vs. CON, physiological parameters were as follows: plasma total CO2, 38.0 +/- 1.1 vs. 27.8 +/- 0.6 meq/l (P less than 0.001); urinary total CO2 excretion, 141 +/- 89 vs. 20 +/- 3 neq.min-1.100 g body wt-1; and urinary Cl- excretion, 20 +/- 10 vs. 486 +/- 144 neq.min-1.100 g body wt-1 (P less than 0.001). H(+)-ATPase was localized in thin sections using a rabbit polyclonal antibody against the 70-kDa subunit of bovine brain H(+)-ATPase. Band 3 protein was localized using a polyclonal antibody against the 43-kDa subunit of the cytoplasmic domain of human erythrocyte band 3 protein. In CON rats, H(+)-ATPase localized along the apical plasma membrane and over the apical cytoplasmic vesicles of type A ICs in the CCD and ICs of the OMCD. H(+)-ATPase was observed along the basolateral plasma membrane and over cytoplasmic vesicles throughout type B ICs. In CDA rats, H(+)-ATPase was only observed over apical cytoplasmic vesicles in type A ICs and in the majority of OMCD ICs. In type B ICs, H(+)-ATPase staining was intensified along the basal plasma membrane in CDA. Band 3 protein was consistently localized in the basolateral plasma membrane of all type A cells in the CCD and ICs of the OMCD in both CON and CDA. In summary, stimulation of HCO3- secretion in rats caused withdrawal of H(+)-ATPase from the apical plasma membrane and storage in apical cytoplasmic vesicles of ICs of the OMCD and type A ICs of the CCD. H(+)-ATPase appeared to be inserted into the basal plasma membrane of type B ICs. These findings suggest that, during correction of CDA, proton secretion by type A and OMCD ICs is suppressed and proton transport across the basolateral plasma membrane of type B ICs is stimulated.