Soldati L, Vezzoli G, Salardi S, Spaventa R, Barber B R, Azzani T, Bianchi G
Department of Sciences and Biochemical Technologies, University of Milano, Italy.
Biochem Biophys Res Commun. 1996 May 15;222(2):572-5. doi: 10.1006/bbrc.1996.0785.
We studied the activity of plasma membrane (Ca+Mg)ATPase from erythrocytes of Milan hypertensive rat strain (MHS) and Milan low calpastatin rat strain (MLCS), that show an activity level of the specific calpain inhibitor, calpastatin, about five fold reduced in comparison with the Milan normotensive rat strain (MNS), while the protease activity level is similar. This imbalance of calpain:calpastatin ratio leads to a decrease of the erythrocyte plasma membrane (Ca+Mg)ATPase activity and to the appearance of 124 kDa fragments, which are the typical products of proteolytic calpain action on the 136 kDa (Ca+Mg)ATPase native form.
我们研究了米兰高血压大鼠品系(MHS)和米兰低钙蛋白酶抑制蛋白大鼠品系(MLCS)红细胞质膜(Ca+Mg)ATP酶的活性。这两个品系中特异性钙蛋白酶抑制剂钙蛋白酶抑制蛋白的活性水平,与米兰正常血压大鼠品系(MNS)相比降低了约五倍,而蛋白酶活性水平相似。钙蛋白酶与钙蛋白酶抑制蛋白比例的这种失衡,导致红细胞质膜(Ca+Mg)ATP酶活性降低,并出现124 kDa片段,这些片段是钙蛋白酶对136 kDa(Ca+Mg)ATP酶天然形式进行蛋白水解作用的典型产物。