Tsung P K, Palek J
Muscle Nerve. 1980 Jan-Feb;3(1):55-69. doi: 10.1002/mus.880030107.
We review our current understanding of membrane phosphorylation in normal and abnormal erythrocytes. The major phosphoproteins in red blood cell (RBC) membranes are spectrin (band 2), bands 3, 2.1, and 4.5, and glycophorin A. At least two protein kinases can be distinguished on the basis of their stimulation by cyclic AMP and salt; they are present both in the membrane and in the cytosol. Analysis of the conflicting data on endogenous membrane-protein phosphorylation in abnormal RBCs indicates a considerable variability of phosphorylation rates which largely depends on the manner of preparation of ghosts and enzyme assay conditions. This variability reflects differences in the partitioning of protein kinases between the membrane and cytosol, the specificity and accessibility of membrane-protein substrates, and reaction kinetics. We select examples of data from several hemolytic anemias to illustrate that precautions are needed to interpret abnormalities of membrane-protein phosphorylation properly; we discuss possible new methodological approaches.
我们回顾了目前对正常和异常红细胞中膜磷酸化的理解。红细胞(RBC)膜中的主要磷蛋白是血影蛋白(带2)、带3、2.1和4.5,以及血型糖蛋白A。至少可以根据环磷酸腺苷和盐对它们的刺激来区分两种蛋白激酶;它们既存在于膜中,也存在于细胞质中。对异常红细胞内源性膜蛋白磷酸化的相互矛盾的数据进行分析表明,磷酸化速率存在相当大的变异性,这在很大程度上取决于血影的制备方式和酶测定条件。这种变异性反映了蛋白激酶在膜和细胞质之间的分配差异、膜蛋白底物的特异性和可及性以及反应动力学。我们从几种溶血性贫血中选取数据实例来说明,正确解释膜蛋白磷酸化异常需要谨慎;我们讨论了可能的新方法。