Karlmark B, Agerup B, Wistrand P J
Acta Physiol Scand. 1979 Jun;106(2):145-50. doi: 10.1111/j.1748-1716.1979.tb06383.x.
Carbonic anhydrase is found in the cytoplasm and brush border membranes of renal proximal tubular cells. Both the soluble and the membrane-bound enzyme have been assigned roles for the secretion of hydrogen ions into the tubular fluid and hence also for the reabsorption of bicarbonate. Attempts were made to differentiate between the roles of these enzymes for the rate of proximal tubular acidification. Proximal tubules of rats were instilled and perfused with bicarbonate solutions containing carbonic anhydrase inhibitors, especially designed to be impermeable to cell membranes. The acidification rate was measured with an antimony micro-electrode system--the only instantly responding micro-pH electrode. The membrane impermeable inhibitors had no effect on this rate in contrast to acetazolamide, which markedly inhibited the acidification rate when administered intraluminally. It is therefore concluded that the cytoplasmic carbonic anhydrase is the important enzyme for the proximal tubular acidification rate, and hence the rate of bicarbonate reabsorption. The function of the brush border enzyme remains an outstanding problem.
碳酸酐酶存在于肾近端小管细胞的细胞质和刷状缘膜中。可溶性酶和膜结合酶都在向小管液中分泌氢离子以及重吸收碳酸氢盐的过程中发挥作用。人们试图区分这些酶在近端小管酸化速率方面的作用。给大鼠的近端小管灌注含有碳酸酐酶抑制剂的碳酸氢盐溶液,这些抑制剂经过特殊设计,不能透过细胞膜。用锑微电极系统(唯一能即时响应的微pH电极)测量酸化速率。与乙酰唑胺不同,不能透过细胞膜的抑制剂对该速率没有影响,当腔内给予乙酰唑胺时,它会显著抑制酸化速率。因此得出结论,细胞质中的碳酸酐酶是近端小管酸化速率以及碳酸氢盐重吸收速率的重要酶。刷状缘酶的功能仍然是一个突出的问题。