Rosenspire A J, Choi Y S
Department of Biological Sciences, Wayne State University, Detroit, MI 48202.
Life Sci. 1988;42(5):497-504. doi: 10.1016/0024-3205(88)90089-6.
The binding of membrane immunoglobulin (mIg) by anti-Ig antibodies is known to initiate a mitogenic signal in B lymphocytes. Because in many instances growth control appears to be correlated with phosphokinase activity, as well as with alterations in cytoskeletal architecture, we asked the question whether antibodies binding to mIg would also lead to the specific phosphorylation of lymphocyte actin-associated proteins. Utilizing a myosin affinity technique, we directly examined phosphoproteins that were associated with actin in the chicken B cell. We found that in a few instances the level of phosphorylation was indeed modulated by mIg:anti-Ig interactions. These actin-binding phosphoproteins may be important control elements in the lymphocyte cytoskeleton.
已知抗Ig抗体与膜免疫球蛋白（mIg）的结合会在B淋巴细胞中引发促有丝分裂信号。因为在许多情况下，生长控制似乎与磷酸激酶活性以及细胞骨架结构的改变相关，所以我们提出了一个问题，即与mIg结合的抗体是否也会导致淋巴细胞肌动蛋白相关蛋白的特异性磷酸化。利用肌球蛋白亲和技术，我们直接检测了鸡B细胞中与肌动蛋白相关的磷蛋白。我们发现，在一些情况下，磷酸化水平确实受到mIg：抗Ig相互作用的调节。这些肌动蛋白结合磷蛋白可能是淋巴细胞细胞骨架中的重要控制元件。
