Chakravarty N, Nielsen E H
Agents Actions. 1981 Apr;11(1-2):67-9. doi: 10.1007/BF01991458.
A Ca++-Mg++ ATPase has been demonstrated in the plasma membrane of rat peritoneal mast cells. The enzyme is localized by electron microscopy on the outer surface of the membrane. This agrees with the biochemical findings. A Ca++-Mg++ activated ATPase has also been shown to be present in the granule membrane. The optimal pH of the plasma membrane enzyme is close to the optimal pH for the histamine release. All the 14 inhibitors of plasma membrane ATPase tested - which caused varying degrees of inhibition of the enzyme - also inhibited histamine release induced by antigen, compound 48/80 and the divalent ionophore A23187. The conclusion from the study with the inhibitors is that a mild inhibition of the enzyme is compatible with histamine release, but a pronounced inhibition of the enzyme is always associated with inhibition of histamine release. ATP in low concentrations potentiates the release.
在大鼠腹膜肥大细胞的质膜中已证实存在一种Ca++-Mg++ ATP酶。通过电子显微镜观察,该酶定位于膜的外表面。这与生化研究结果一致。还表明颗粒膜中存在一种Ca++-Mg++激活的ATP酶。质膜酶的最佳pH值接近组胺释放的最佳pH值。所测试的14种质膜ATP酶抑制剂——它们对该酶产生不同程度的抑制作用——也抑制了由抗原、化合物48/80和二价离子载体A23187诱导的组胺释放。从抑制剂研究得出的结论是,对该酶的轻度抑制与组胺释放相容,但对该酶的明显抑制总是与组胺释放的抑制相关。低浓度的ATP可增强释放。