Is actin in eye lens a possible factor in visual accommodation?
Is actin in eye lens a possible factor in visual accommodation?
复制标题
晶状体中的肌动蛋白是否是视觉调节的可能因素？
作者：
M. Kibbelaar;F. Ramaekers;P. Ringens;A. Selten;L. Poels;P. Jap;A. L. Rossum;T. Feltkamp;H. Bloemendal
肌动蛋白已从各种非肌肉细胞中纯化出来，其特征在于其分子量和能够形成细丝。虽然这种蛋白质的发生已被假定在哺乳动物的眼睛透镜后，在电子显微镜中观察肌动蛋白样丝1，2，明确的（生物）化学证据已提供最近3。氨基酸分析、肽图分析和亲和层析表明，透镜肌动蛋白与其它组织中相应的蛋白质具有同一性。由于纤维可以通过与高度纯化的透镜质膜共分离获得，我们有兴趣知道含肌动蛋白的结构是如何在原位定位的。在这里报道的实验方法中，间接免疫荧光技术（IFT）4应用于透镜组织的未固定的低温恒温切片。本文描述了肌动蛋白在小牛、大鼠和鸽子透镜中的分布，并讨论了肌动蛋白在视觉调节中的作用。
Actin has been purified from various non-muscle cells and characterized by its molecular weight and ability to polymerize into filaments. Although the occurrence of this protein has been postulated in the mammalian eye lens after observation of actin-like filaments in the electron microscope1,2, definite (bio)chemical proof has been provided only recently3. Amino acid analysis, peptide mapping and affinity chromatography revealed the identity of lens actin with the corresponding protein in other tissues. As the filaments could be obtained by co-isolation with highly purified lens plasma membranes, we were interested to know how the actin-containing structures were located in situ. In the experimental approach reported here, the indirect immunofluorescence technique (IFT)4 was applied to unfixed cryostat sections of lens tissue. The distribution of actin in calf, rat and pigeon lens is described, and evidence from this for the role of actin in visual accommodation discussed.