Knipper M, Zimmermann U, Köpschall I, Rohbock K, Jüngling S, Zenner H P
Department of Otolaryngology, University of Tübingen, FRG.
Hear Res. 1995 Jun;86(1-2):100-10. doi: 10.1016/0378-5955(95)00060-h.
By employing immunological methods, it has been demonstrated that myosin, myosin light chain (MLC) and myosin light chain kinase (MLCK) proteins in outer hair cells (OHC) are immunologically different from isoforms in platelets, smooth muscle and heart muscle, and are probably more related to isoforms found in red blood cells (RBC). Moreover, proteins related to band 3 protein (b3p) and protein 4.1 (p 4.1), ankyrin as well as fodrin and spectrin, but not glycophorin, have been identified in isolated OHCs. Both OHCs and RBC differ from other motile non-muscle cells in their lack of smooth muscle isoforms of actin, their common high levels of spectrin-, ankyrin- and band 3-like proteins, as well as the expression of the 80 kDa protein 4.1 isoform. The data support the notion that motility of OHC may be based upon regulation of the b3p/p 4.1/ankyrin complex, and thus may be reminiscent to the active shape changes in RBC.
通过采用免疫学方法已证明，外毛细胞（OHC）中的肌球蛋白、肌球蛋白轻链（MLC）和肌球蛋白轻链激酶（MLCK）蛋白在免疫学上与血小板、平滑肌和心肌中的同种型不同，并且可能与红细胞（RBC）中发现的同种型更相关。此外，在分离的外毛细胞中已鉴定出与带3蛋白（b3p）和蛋白4.1（p 4.1）、锚蛋白以及血影蛋白和肌动蛋白相关的蛋白，但未发现血型糖蛋白。外毛细胞和红细胞与其他可运动的非肌肉细胞不同，它们缺乏肌动蛋白的平滑肌同种型，它们共同具有高水平的血影蛋白、锚蛋白和类带3蛋白，以及80 kDa蛋白4.1同种型的表达。这些数据支持这样一种观点，即外毛细胞的运动性可能基于b3p/p 4.1/锚蛋白复合物的调节，因此可能使人联想到红细胞中的主动形状变化。
