Verlander J W, Madsen K M, Galla J H, Luke R G, Tisher C C
Laboratory of Experimental Morphology, University of Florida, Gainesville 32610-0224.
Am J Physiol. 1992 Feb;262(2 Pt 2):F309-19. doi: 10.1152/ajprenal.1992.262.2.F309.
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.
我们研究了氯缺失代谢性碱中毒(CDA)对大鼠皮质集合管(CCD)和外髓集合管(OMCD)闰细胞(IC)中H(+)-ATP酶及带3蛋白定位的影响。用0.15M NaHCO3进行30分钟腹膜透析以产生CDA,或用林格氏碳酸氢盐作为对照(CON),两组均静脉输注80mM Cl-溶液90分钟。CDA组与CON组的生理参数如下:血浆总CO2,分别为38.0±1.1与27.8±0.6meq/l(P<0.001);尿总CO2排泄量,分别为141±89与20±3neq.min-1.100g体重-1;尿Cl-排泄量,分别为20±10与486±144neq.min-1.100g体重-1(P<0.001)。使用针对牛脑H(+)-ATP酶70kDa亚基的兔多克隆抗体在薄片中定位H(+)-ATP酶。使用针对人红细胞带3蛋白胞质结构域43kDa亚基的多克隆抗体定位带3蛋白。在CON组大鼠中,H(+)-ATP酶定位于CCD中A型IC和OMCD的IC的顶端质膜及顶端胞质小泡上。在整个B型IC中,H(+)-ATP酶见于基底外侧质膜及胞质小泡上。在CDA组大鼠中,H(+)-ATP酶仅见于A型IC和大多数OMCD的IC的顶端胞质小泡上。在B型IC中,CDA时H(+)-ATP酶染色在基底质膜处增强。带3蛋白始终定位于CON组和CDA组大鼠的CCD中所有A型细胞以及OMCD的IC的基底外侧质膜上。总之,大鼠中HCO3-分泌的刺激导致H(+)-ATP酶从顶端质膜撤回并储存于OMCD的IC及CCD的A型IC的顶端胞质小泡中。H(+)-ATP酶似乎插入到B型IC的基底质膜中。这些发现提示,在CDA纠正过程中,A型和OMCD的IC的质子分泌受到抑制,而B型IC的基底外侧质膜的质子转运受到刺激。